메뉴 건너뛰기




Volumn 48, Issue 3, 2009, Pages 517-526

Chemical tools for K + channel biology

Author keywords

[No Author keywords available]

Indexed keywords

CHART RECORDERS; CHEMICAL TOOLS; ELECTRICAL ACTIVITIES; EPITHELIAL TISSUES; HIGH-RESOLUTION STRUCTURES; LIGAND CONCENTRATIONS; MEMBRANE VOLTAGES; MOLECULAR MOTIONS; MULTISUBUNIT; NATURAL PRODUCTS; ORGANIC CATIONS; PATCH CLAMPS; SCREENING APPROACHES; SYNTHETIC METHODOLOGIES; WATER TRANSPORTS;

EID: 59249097768     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8018515     Document Type: Article
Times cited : (8)

References (94)
  • 1
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon, R., Cohen, S. L., Kuo, A., Lee, A., and Chait, B. T. (1998) Structural conservation in prokaryotic and eukaryotic potassium channels. Science 280, 106-109.
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 2
    • 0036701872 scopus 로고    scopus 로고
    • Structural basis of inward rectifying potassium channel gating
    • Loussouarn, G., Rose, T., and Nichols, C. G. (2002) Structural basis of inward rectifying potassium channel gating. Trends CardioVasc. Med. 12, 253-258.
    • (2002) Trends CardioVasc. Med , vol.12 , pp. 253-258
    • Loussouarn, G.1    Rose, T.2    Nichols, C.G.3
  • 3
    • 0034489180 scopus 로고    scopus 로고
    • Intracellular regulation of inward rectifier K+ channels
    • Ruppersberg, J. P. (2000) Intracellular regulation of inward rectifier K+ channels. Pfluegers Arch. 441, 1-11.
    • (2000) Pfluegers Arch , vol.441 , pp. 1-11
    • Ruppersberg, J.P.1
  • 5
    • 26444584556 scopus 로고    scopus 로고
    • Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography
    • Kuo, A., Domene, C., Johnson, L. N., Doyle, D. A., and Venien-Bryan, C. (2005) Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography. Structure 13, 1463-1472.
    • (2005) Structure , vol.13 , pp. 1463-1472
    • Kuo, A.1    Domene, C.2    Johnson, L.N.3    Doyle, D.A.4    Venien-Bryan, C.5
  • 6
    • 0030609143 scopus 로고    scopus 로고
    • Octameric stoichiometry of the KATP channel complex
    • Shyng, S., and Nichols, C. G (1997) Octameric stoichiometry of the KATP channel complex. J. Gen. Physiol. 110, 655-664.
    • (1997) J. Gen. Physiol , vol.110 , pp. 655-664
    • Shyng, S.1    Nichols, C.G.2
  • 7
    • 33645322386 scopus 로고    scopus 로고
    • KATP channels as molecular sensors of cellular metabolism
    • Nichols, C. G (2006) KATP channels as molecular sensors of cellular metabolism. Nature 440, 470-476.
    • (2006) Nature , vol.440 , pp. 470-476
    • Nichols, C.G.1
  • 8
    • 41149095488 scopus 로고    scopus 로고
    • How membrane proteins sense voltage
    • Bezanilla, F. (2008) How membrane proteins sense voltage. Nat. ReV. Mol. Cell Biol. 9, 323-332.
    • (2008) Nat. ReV. Mol. Cell Biol , vol.9 , pp. 323-332
    • Bezanilla, F.1
  • 9
    • 25644437209 scopus 로고    scopus 로고
    • Focused electric field across the voltage sensor of potassium channels
    • Ahern, C. A., and Horn, R. (2005) Focused electric field across the voltage sensor of potassium channels. Neuron 48, 25-29.
    • (2005) Neuron , vol.48 , pp. 25-29
    • Ahern, C.A.1    Horn, R.2
  • 10
    • 0037282379 scopus 로고    scopus 로고
    • The voltage sensor and the gate in ion channels
    • Bezanilla, F., and Perozo, E. (2003) The voltage sensor and the gate in ion channels. Adv. Protein Chem. 63, 211-241.
    • (2003) Adv. Protein Chem , vol.63 , pp. 211-241
    • Bezanilla, F.1    Perozo, E.2
  • 11
    • 33745216690 scopus 로고    scopus 로고
    • A structural interpretation of voltage-gated potassium channel inactivation
    • Kurata, H. T., and Fedida, D. (2006) A structural interpretation of voltage-gated potassium channel inactivation. Prog. Biophys. Mol. Biol. 92, 185-208.
    • (2006) Prog. Biophys. Mol. Biol , vol.92 , pp. 185-208
    • Kurata, H.T.1    Fedida, D.2
  • 12
    • 0025224223 scopus 로고
    • Biophysical and molecular mechanisms of Shaker potassium channel inactivation
    • Hoshi, T., Zagotta, W. N., and Aldrich, R. W. (1990) Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science 250, 533-538.
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 13
    • 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., and MacKinnon, R. (2001) Potassium channel receptor site for the inactivation gate and quaternary amine inhibitors. Nature 411, 657-661.
    • (2001) Nature , vol.411 , pp. 657-661
    • Zhou, M.1    Morais-Cabral, J.H.2    Mann, S.3    MacKinnon, R.4
  • 14
    • 0026079907 scopus 로고
    • Tetraethylammonium blockade distinguishes two inactivation mechanisms in voltage-activated K+ channels
    • Choi, K. L., Aldrich, R. W., and Yellen, G. (1991) Tetraethylammonium blockade distinguishes two inactivation mechanisms in voltage-activated K+ channels. Proc. Natl. Acad. Sci. U.S.A. 88, 5092-5095.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 5092-5095
    • Choi, K.L.1    Aldrich, R.W.2    Yellen, G.3
  • 16
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I. S., Moran, M. M., Chong, J. A., and Clapham, D. E. (2006) A voltage-gated proton-selective channel lacking the pore domain. Nature 440, 1213-1216.
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 17
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K., and Okamura, Y. (2005) Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435, 1239-1243.
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 18
    • 33646586039 scopus 로고    scopus 로고
    • Voltage-gated potassium channels: Regulation by accessory subunits
    • Li, Y., Um, S. Y., and McDonald, T. V. (2006) Voltage-gated potassium channels: Regulation by accessory subunits. Neuroscientist 12, 199-210.
    • (2006) Neuroscientist , vol.12 , pp. 199-210
    • Li, Y.1    Um, S.Y.2    McDonald, T.V.3
  • 28
    • 33744970273 scopus 로고    scopus 로고
    • Modulation of voltage-dependent Shaker family potassium channels by an aldoketo reductase
    • Weng, J., Cao, Y., Moss, N., and Zhou, M. (2006) Modulation of voltage-dependent Shaker family potassium channels by an aldoketo reductase. J. Biol. Chem. 281, 15194-15200.
    • (2006) J. Biol. Chem , vol.281 , pp. 15194-15200
    • Weng, J.1    Cao, Y.2    Moss, N.3    Zhou, M.4
  • 33
    • 0025743037 scopus 로고
    • Interaction between tetraethylammonium and amino acid residues in the pore of cloned voltage-dependent potassium channels
    • Kavanaugh, M. P., Varnum, M. D., Osborne, P. B., Christie, M. J., Busch, A. E., Adelman, J. P., and North, R. A. (1991) Interaction between tetraethylammonium and amino acid residues in the pore of cloned voltage-dependent potassium channels. J. Biol. Chem. 266, 7583-7587.
    • (1991) J. Biol. Chem , vol.266 , pp. 7583-7587
    • Kavanaugh, M.P.1    Varnum, M.D.2    Osborne, P.B.3    Christie, M.J.4    Busch, A.E.5    Adelman, J.P.6    North, R.A.7
  • 38
    • 0028276482 scopus 로고
    • + channel: Peptide and channel residues mediating molecular recognition
    • + channel: Peptide and channel residues mediating molecular recognition. Neuron 12, 1377-1388.
    • (1994) Neuron , vol.12 , pp. 1377-1388
    • Goldstein, S.A.1    Pheasant, D.J.2    Miller, C.3
  • 39
    • 34548615505 scopus 로고    scopus 로고
    • + Channel Complexes. ACS Chem. Biol. 2, 469-473.
    • + Channel Complexes. ACS Chem. Biol. 2, 469-473.
  • 40
    • 0018860646 scopus 로고
    • A covalently bound photoisomerizable agonist: Comparison with reversibly bound agonists at Electrophorus electroplaques
    • Lester, H. A., Krouse, M. E., Nass, M. M., Wassermann, N. H., and Erlanger, B. F. (1980) A covalently bound photoisomerizable agonist: Comparison with reversibly bound agonists at Electrophorus electroplaques. J. Gen. Physiol. 75, 207-232.
    • (1980) J. Gen. Physiol , vol.75 , pp. 207-232
    • Lester, H.A.1    Krouse, M.E.2    Nass, M.M.3    Wassermann, N.H.4    Erlanger, B.F.5
  • 42
    • 12344309164 scopus 로고    scopus 로고
    • Light-activated ion channels for remote control of neuronal firing
    • Banghart, M., Borges, K., Isacoff, E., Trauner, D., and Kramer, R. H. (2004) Light-activated ion channels for remote control of neuronal firing. Nat. Neurosci. 7, 1381-1386.
    • (2004) Nat. Neurosci , vol.7 , pp. 1381-1386
    • Banghart, M.1    Borges, K.2    Isacoff, E.3    Trauner, D.4    Kramer, R.H.5
  • 43
    • 0030471462 scopus 로고    scopus 로고
    • Lien, L., Jaikaran, D. C. J., Zhang, Z., and Woolley, G. A. (1996) Photomodulated Blocking of Gramicidin Ion Channels. J. Am. Chem. Soc. 118, 12222-12223.
    • Lien, L., Jaikaran, D. C. J., Zhang, Z., and Woolley, G. A. (1996) Photomodulated Blocking of Gramicidin Ion Channels. J. Am. Chem. Soc. 118, 12222-12223.
  • 44
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin, A., and Akabas, M. H. (1998) Substituted-cysteine accessibility method. Methods Enzymol. 293, 123-145.
    • (1998) Methods Enzymol , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 46
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C., and Schultz, P. G. (1989) A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244, 182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 47
    • 0032311418 scopus 로고    scopus 로고
    • In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system
    • Nowak, M. W., Gallivan, J. P., Silverman, S. K., Labarca, C. G., Dougherty, D. A., and Lester, H. A. (1998) In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system. Methods Enzymol. 293, 504-529.
    • (1998) Methods Enzymol , vol.293 , pp. 504-529
    • Nowak, M.W.1    Gallivan, J.P.2    Silverman, S.K.3    Labarca, C.G.4    Dougherty, D.A.5    Lester, H.A.6
  • 50
    • 0037204951 scopus 로고    scopus 로고
    • Probing protein electrostatics with a synthetic fluorescent amino acid
    • Cohen, B. E., McAnaney, T. B., Park, E. S., Jan, Y. N., Boxer, S. G., and Jan, L. Y. (2002) Probing protein electrostatics with a synthetic fluorescent amino acid. Science 296, 1700-1703.
    • (2002) Science , vol.296 , pp. 1700-1703
    • Cohen, B.E.1    McAnaney, T.B.2    Park, E.S.3    Jan, Y.N.4    Boxer, S.G.5    Jan, L.Y.6
  • 51
    • 4243468938 scopus 로고    scopus 로고
    • The Cation-π Interaction
    • Ma, J. C., and Dougherty, D. A. (1997) The Cation-π Interaction. Chem. Rev. 97, 1303-1324.
    • (1997) Chem. Rev , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 52
    • 0035113738 scopus 로고    scopus 로고
    • The tethered agonist approach to mapping ion channel proteins: Toward a structural model for the agonist binding site of the nicotinic acetylcholine receptor
    • Li, L., Zhong, W., Zacharias, N., Gibbs, C., Lester, H. A., and Dougherty, D. A. (2001) The tethered agonist approach to mapping ion channel proteins: Toward a structural model for the agonist binding site of the nicotinic acetylcholine receptor. Chem. Biol. 8, 47-58.
    • (2001) Chem. Biol , vol.8 , pp. 47-58
    • Li, L.1    Zhong, W.2    Zacharias, N.3    Gibbs, C.4    Lester, H.A.5    Dougherty, D.A.6
  • 53
    • 5644237713 scopus 로고    scopus 로고
    • Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis
    • Beene, D. L., Price, K. L., Lester, H. A., Dougherty, D. A., and Lummis, S. C. (2004) Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis. J. Neurosci. 24, 9097-9104.
    • (2004) J. Neurosci , vol.24 , pp. 9097-9104
    • Beene, D.L.1    Price, K.L.2    Lester, H.A.3    Dougherty, D.A.4    Lummis, S.C.5
  • 54
    • 38349142833 scopus 로고    scopus 로고
    • 5-Fluorotryptamine is a partial agonist at 5-HT3 receptors, and reveals that size and electronegativity at the 5 position of tryptamine are critical for efficient receptor function
    • Bower, K. S., Price, K. L., Sturdee, L. E., Dayrell, M., Dougherty, D. A., and Lummis, S. C. (2008) 5-Fluorotryptamine is a partial agonist at 5-HT3 receptors, and reveals that size and electronegativity at the 5 position of tryptamine are critical for efficient receptor function. Eur. J. Pharmacol. 580, 291-297.
    • (2008) Eur. J. Pharmacol , vol.580 , pp. 291-297
    • Bower, K.S.1    Price, K.L.2    Sturdee, L.E.3    Dayrell, M.4    Dougherty, D.A.5    Lummis, S.C.6
  • 55
    • 25144465496 scopus 로고    scopus 로고
    • A cation-π binding interaction with a tyrosine in the binding site of the GABAC receptor
    • Lummis, S. C. D. L. B., Harrison, N. J., Lester, H. A., and Dougherty, D. A. (2005) A cation-π binding interaction with a tyrosine in the binding site of the GABAC receptor. Chem. Biol. 12, 993-997.
    • (2005) Chem. Biol , vol.12 , pp. 993-997
    • Lummis, S.C.D.L.B.1    Harrison, N.J.2    Lester, H.A.3    Dougherty, D.A.4
  • 56
    • 33751517798 scopus 로고    scopus 로고
    • 2+ blockade site of an N-methyl-D-aspartate (NMDA) receptor with unnatural amino acid mutagenesis. ACS Chem. Biol. 1, 227-234.
    • 2+ blockade site of an N-methyl-D-aspartate (NMDA) receptor with unnatural amino acid mutagenesis. ACS Chem. Biol. 1, 227-234.
  • 57
    • 58149166932 scopus 로고    scopus 로고
    • A cation-π interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue
    • Pless, S. A., Millen, K. S., Hanek, A. P., Lynch, J. W., Lester, H. A., Lummis, S. C., and Dougherty, D. A. (2008) A cation-π interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue. J. Neurosci. 28, 10937-10942.
    • (2008) J. Neurosci , vol.28 , pp. 10937-10942
    • Pless, S.A.1    Millen, K.S.2    Hanek, A.P.3    Lynch, J.W.4    Lester, H.A.5    Lummis, S.C.6    Dougherty, D.A.7
  • 58
    • 37849001772 scopus 로고    scopus 로고
    • Electrostatic contributions of aromatic residues in the local anesthetic receptor of voltage-gated sodium channels
    • Ahern, C. A., Eastwood, A. L., Dougherty, D. A., and Horn, R. (2008) Electrostatic contributions of aromatic residues in the local anesthetic receptor of voltage-gated sodium channels. Circ. Res. 102, 86-94.
    • (2008) Circ. Res , vol.102 , pp. 86-94
    • Ahern, C.A.1    Eastwood, A.L.2    Dougherty, D.A.3    Horn, R.4
  • 59
    • 34848876603 scopus 로고    scopus 로고
    • Calcium block of single sodium channels: Role of a pore-lining aromatic residue
    • Santarelli, V. P., Eastwood, A. L., Dougherty, D. A., Ahern, C. A., and Horn, R. (2007) Calcium block of single sodium channels: Role of a pore-lining aromatic residue. Biophys. J. 93, 2341-2349.
    • (2007) Biophys. J , vol.93 , pp. 2341-2349
    • Santarelli, V.P.1    Eastwood, A.L.2    Dougherty, D.A.3    Ahern, C.A.4    Horn, R.5
  • 60
    • 34247267099 scopus 로고    scopus 로고
    • A cation-π interaction discriminates among sodium channels that are either sensitive or resistant to tetrodotoxin block
    • Santarelli, V. P., Eastwood, A. L., Dougherty, D. A., Horn, R., and Ahern, C. A. (2007) A cation-π interaction discriminates among sodium channels that are either sensitive or resistant to tetrodotoxin block. J. Biol. Chem. 282, 8044-8051.
    • (2007) J. Biol. Chem , vol.282 , pp. 8044-8051
    • Santarelli, V.P.1    Eastwood, A.L.2    Dougherty, D.A.3    Horn, R.4    Ahern, C.A.5
  • 61
    • 33751517446 scopus 로고    scopus 로고
    • A cation-π interaction between extracellular TEA and an aromatic residue in potassium channels
    • Ahern, C. A., Eastwood, A. L., Lester, H. A., Dougherty, D. A., and Horn, R. (2006) A cation-π interaction between extracellular TEA and an aromatic residue in potassium channels. J. Gen. Physiol. 128, 649-657.
    • (2006) J. Gen. Physiol , vol.128 , pp. 649-657
    • Ahern, C.A.1    Eastwood, A.L.2    Lester, H.A.3    Dougherty, D.A.4    Horn, R.5
  • 64
    • 34548602702 scopus 로고    scopus 로고
    • Xie, J., Supekova, L., and Schultz, P. G. (2007) A genetically encoded metabolically stable analogue of phosphotyrosine in Escherichia coli. ACS Chem. Biol. 2, 474-478.
    • Xie, J., Supekova, L., and Schultz, P. G. (2007) A genetically encoded metabolically stable analogue of phosphotyrosine in Escherichia coli. ACS Chem. Biol. 2, 474-478.
  • 65
    • 33745946445 scopus 로고    scopus 로고
    • A genetically encoded fluorescent amino acid
    • Wang, J., Xie, J., and Schultz, P. G. (2006) A genetically encoded fluorescent amino acid. J. Am. Chem. Soc. 128, 8738-8739.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 8738-8739
    • Wang, J.1    Xie, J.2    Schultz, P.G.3
  • 66
    • 33847648384 scopus 로고    scopus 로고
    • Genetic incorporation of unnatural amino acids into proteins in mammalian cells
    • Liu, W., Brock, A., Chen, S., and Schultz, P. G. (2007) Genetic incorporation of unnatural amino acids into proteins in mammalian cells. Nat. Methods 4, 239-244.
    • (2007) Nat. Methods , vol.4 , pp. 239-244
    • Liu, W.1    Brock, A.2    Chen, S.3    Schultz, P.G.4
  • 67
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir, T. W., Sondhi, D., and Cole, P. A. (1998) Expressed protein ligation: A general method for protein engineering. Proc. Natl. Acad. Sci. U.S.A. 95, 6705-6710.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 68
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • Muralidharan, V., and Muir, T. W. (2006) Protein ligation: An enabling technology for the biophysical analysis of proteins. Nat. Methods 3, 429-438.
    • (2006) Nat. Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 71
    • 0037036754 scopus 로고    scopus 로고
    • Semisynthesis and folding of the potassium channel KcsA
    • Valiyaveetil, F. I., MacKinnon, R., and Muir, T. W. (2002) Semisynthesis and folding of the potassium channel KcsA. J. Am. Chem. Soc. 124, 9113-9120.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 9113-9120
    • Valiyaveetil, F.I.1    MacKinnon, R.2    Muir, T.W.3
  • 72
    • 33748360106 scopus 로고    scopus 로고
    • Structural and functional consequences of an amide-to-ester substitution in the selectivity filter of a potassium channel
    • Valiyaveetil, F. I., Sekedat, M., MacKinnon, R., and Muir, T. W. (2006) Structural and functional consequences of an amide-to-ester substitution in the selectivity filter of a potassium channel. J. Am. Chem. Soc. 128, 11591-11599.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 11591-11599
    • Valiyaveetil, F.I.1    Sekedat, M.2    MacKinnon, R.3    Muir, T.W.4
  • 74
    • 0036014776 scopus 로고    scopus 로고
    • Conformations of amino acids in proteins
    • Hovmoller, S., Zhou, T., and Ohlson, T. (2002) Conformations of amino acids in proteins. Acta Crystallogr. D58, 768-776.
    • (2002) Acta Crystallogr , vol.D58 , pp. 768-776
    • Hovmoller, S.1    Zhou, T.2    Ohlson, T.3
  • 75
    • 0032313490 scopus 로고    scopus 로고
    • Identification of ion channel-associated proteins using the yeast two-hybrid system
    • Niethammer, M., and Sheng, M. (1998) Identification of ion channel-associated proteins using the yeast two-hybrid system. Methods Enzvmol. 293, 104-122.
    • (1998) Methods Enzvmol , vol.293 , pp. 104-122
    • Niethammer, M.1    Sheng, M.2
  • 76
    • 0024042922 scopus 로고
    • TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cereVisiae
    • Gaber, R. F., Styles, C. A., and Fink, G R. (1988) TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cereVisiae. Mol. Cell. Biol. 8, 2848-2859.
    • (1988) Mol. Cell. Biol , vol.8 , pp. 2848-2859
    • Gaber, R.F.1    Styles, C.A.2    Fink, G.R.3
  • 78
    • 0032313519 scopus 로고    scopus 로고
    • Studying ion channels using yeast genetics
    • Nakamura, R. L., and Gaber, R. F. (1998) Studying ion channels using yeast genetics. Methods Enzymol. 293, 89-104.
    • (1998) Methods Enzymol , vol.293 , pp. 89-104
    • Nakamura, R.L.1    Gaber, R.F.2
  • 79
    • 0026597932 scopus 로고
    • Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cereVisiae
    • Anderson, J. A., Huprikar, S. S., Kochian, L. V., Lucas, W. J., and Gaber, R. F. (1992) Functional expression of a probable Arabidopsis thaliana potassium channel in Saccharomyces cereVisiae. Proc. Natl. Acad. Sci. U.S.A. 89, 3736-3740.
    • (1992) Proc. Natl. Acad. Sci. U.S.A , vol.89 , pp. 3736-3740
    • Anderson, J.A.1    Huprikar, S.S.2    Kochian, L.V.3    Lucas, W.J.4    Gaber, R.F.5
  • 80
    • 0033582936 scopus 로고    scopus 로고
    • Transmembrane structure of an inwardly rectifying potassium channel
    • Minor, D. L., Jr., Masseling, S. J., Jan, Y. N., and Jan, L. Y. (1999) Transmembrane structure of an inwardly rectifying potassium channel. Cell 96, 879-891.
    • (1999) Cell , vol.96 , pp. 879-891
    • Minor Jr., D.L.1    Masseling, S.J.2    Jan, Y.N.3    Jan, L.Y.4
  • 82
    • 0037167878 scopus 로고    scopus 로고
    • Voltagesensing mechanism is conserved among ion channels gated by opposite voltages
    • Mannikko, R., Elinder, F., and Larsson, H. P. (2002) Voltagesensing mechanism is conserved among ion channels gated by opposite voltages. Nature 419, 837-841.
    • (2002) Nature , vol.419 , pp. 837-841
    • Mannikko, R.1    Elinder, F.2    Larsson, H.P.3
  • 83
    • 0141954276 scopus 로고    scopus 로고
    • Molecular coupling between voltage sensor and pore opening in the Arabidopsis inward rectifier K+ channel KAT1
    • Latorre, R., Olcese, R., Basso, C., Gonzalez, C., Munoz, F., Cosmelli, D., and Alvarez, O. (2003) Molecular coupling between voltage sensor and pore opening in the Arabidopsis inward rectifier K+ channel KAT1. J. Gen. Physiol. 122, 459-469.
    • (2003) J. Gen. Physiol , vol.122 , pp. 459-469
    • Latorre, R.1    Olcese, R.2    Basso, C.3    Gonzalez, C.4    Munoz, F.5    Cosmelli, D.6    Alvarez, O.7
  • 84
    • 23044489633 scopus 로고    scopus 로고
    • The S4 voltage sensor packs against the pore domain in the KAT1 voltagegated potassium channel
    • Lai, H. C., Grabe, M., Jan, Y. N., and Jan, L. Y. (2005) The S4 voltage sensor packs against the pore domain in the KAT1 voltagegated potassium channel. Neuron 47, 395-406.
    • (2005) Neuron , vol.47 , pp. 395-406
    • Lai, H.C.1    Grabe, M.2    Jan, Y.N.3    Jan, L.Y.4
  • 85
    • 33846694346 scopus 로고    scopus 로고
    • Structure prediction for the down state of a potassium channel voltage sensor
    • Grabe, M., Lai, H. C., Jain, M., Jan, Y. N., and Jan, L. Y. (2007) Structure prediction for the down state of a potassium channel voltage sensor. Nature 445, 550-553.
    • (2007) Nature , vol.445 , pp. 550-553
    • Grabe, M.1    Lai, H.C.2    Jain, M.3    Jan, Y.N.4    Jan, L.Y.5
  • 86
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa, N. E., McCormack, K., Tanouye, M. A., and Sigworth, F. J. (1992) The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255, 1712-1715.
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 87
    • 0030059224 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
  • 89
    • 38749119750 scopus 로고    scopus 로고
    • Activation of Kv7 (KCNQ) voltage-gated potassium channels by synthetic compounds
    • Xiong, Q., Gao, Z., Wang, W., and Li, M. (2008) Activation of Kv7 (KCNQ) voltage-gated potassium channels by synthetic compounds. Trends Pharmacol. Sci. 29, 99-107.
    • (2008) Trends Pharmacol. Sci , vol.29 , pp. 99-107
    • Xiong, Q.1    Gao, Z.2    Wang, W.3    Li, M.4
  • 90
    • 34247202495 scopus 로고    scopus 로고
    • Zinc pyrithione-mediated activation of voltage-gated KCNQ potassium channels rescues epileptogenic mutants
    • Xiong, Q., Sun, H., and Li, M. (2007) Zinc pyrithione-mediated activation of voltage-gated KCNQ potassium channels rescues epileptogenic mutants. Nat. Chem. Biol. 3, 287-296.
    • (2007) Nat. Chem. Biol , vol.3 , pp. 287-296
    • Xiong, Q.1    Sun, H.2    Li, M.3
  • 91
    • 10244237790 scopus 로고    scopus 로고
    • Nonradioactive rubidium ion efflux assay and its applications in drug discovery and development
    • Terstappen, G C. (2004) Nonradioactive rubidium ion efflux assay and its applications in drug discovery and development. Assay Drug DeV. Technol. 2, 553-559.
    • (2004) Assay Drug DeV. Technol , vol.2 , pp. 553-559
    • Terstappen, G.C.1
  • 92
    • 32844461535 scopus 로고    scopus 로고
    • Identification of novel Kv1.3 blockers using a fluorescent cell-based ion channel assay
    • Slack, M., Kirchhoff, C., Moller, C., Winkler, D., and Netzer, R. (2006) Identification of novel Kv1.3 blockers using a fluorescent cell-based ion channel assay. J. Biomol. Screening 11, 57-64.
    • (2006) J. Biomol. Screening , vol.11 , pp. 57-64
    • Slack, M.1    Kirchhoff, C.2    Moller, C.3    Winkler, D.4    Netzer, R.5
  • 93
    • 53049101647 scopus 로고    scopus 로고
    • Desensitization of chemical activation by auxiliary subunits: Convergence of molecular determinants critical for augmenting KCNQ1 potassium channels
    • Gao, Z., Xiong, Q., Sun, H., and Li, M. (2008) Desensitization of chemical activation by auxiliary subunits: Convergence of molecular determinants critical for augmenting KCNQ1 potassium channels. J. Biol. Chem. 283, 22649-22658.
    • (2008) J. Biol. Chem , vol.283 , pp. 22649-22658
    • Gao, Z.1    Xiong, Q.2    Sun, H.3    Li, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.