메뉴 건너뛰기




Volumn 5 APR, Issue , 2014, Pages

Principles of agonist recognition in Cys-loop receptors

Author keywords

Cys loop receptors; GABA A receptors; GluCl; Glycine receptors; Ion channels; Ligand recognition; Nicotinic acetylcholine receptors; Serotonin receptors

Indexed keywords

4 AMINOBUTYRIC ACID; ACETYLCHOLINE; CYSTEINE LOOP LIGAND GATED ION CHANNEL RECEPTOR; GLUTAMIC ACID; GLYCINE; IMIDAZOLE; SEROTONIN;

EID: 84901019633     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00160     Document Type: Review
Times cited : (48)

References (137)
  • 1
    • 40449130825 scopus 로고    scopus 로고
    • A molecular basis for agonist and antagonist actions at GABA(C) receptors
    • doi: 10.1111/j.1747-0285.2008.00642.x
    • Abdel-Halim, H., Hanrahan, J. R., Hibbs, D. E., Johnston, G. A., and Chebib, M. (2008). A molecular basis for agonist and antagonist actions at GABA(C) receptors. Chem. Biol. Drug Des. 71, 306-327. doi: 10.1111/j.1747-0285.2008.00642.x
    • (2008) Chem. Biol. Drug Des. , vol.71 , pp. 306-327
    • Abdel-Halim, H.1    Hanrahan, J.R.2    Hibbs, D.E.3    Johnston, G.A.4    Chebib, M.5
  • 2
    • 0027787023 scopus 로고
    • GABAA receptor needs two homologous domains of the beta-subunit for activation by GABA but not by pentobarbital
    • doi: 10.1038/366565a0
    • Amin, J., and Weiss, D. S. (1993). GABAA receptor needs two homologous domains of the beta-subunit for activation by GABA but not by pentobarbital. Nature 366, 565-569. doi: 10.1038/366565a0
    • (1993) Nature , vol.366 , pp. 565-569
    • Amin, J.1    Weiss, D.S.2
  • 3
    • 0028171915 scopus 로고
    • Homomeric rho 1 GABA channels: activation properties and domains
    • Amin, J., and Weiss, D. S. (1994). Homomeric rho 1 GABA channels: activation properties and domains. Receptors Channels 2, 227-236.
    • (1994) Receptors Channels , vol.2 , pp. 227-236
    • Amin, J.1    Weiss, D.S.2
  • 4
    • 84890810573 scopus 로고    scopus 로고
    • Stoichiometry for activation of neuronal alpha7 nicotinic receptors
    • doi: 10.1073/pnas.1315775110
    • Andersen, N., Corradi, J., Sine, S. M., and Bouzat, C. (2013). Stoichiometry for activation of neuronal alpha7 nicotinic receptors. Proc. Natl. Acad. Sci. U.S.A. 110, 20819-20824. doi: 10.1073/pnas.1315775110
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 20819-20824
    • Andersen, N.1    Corradi, J.2    Sine, S.M.3    Bouzat, C.4
  • 5
    • 0000549064 scopus 로고
    • Pyrantel tartrate, a new anthelmintic effective against infections of domestic animals
    • doi: 10.1038/2121273b0
    • Austin, W. C., Courtney, W., Danilewicz, J. C., Morgan, D. H., Conover, L. H., Howes, H. L., et al. (1966). Pyrantel tartrate, a new anthelmintic effective against infections of domestic animals. Nature 212, 1273-1274. doi: 10.1038/2121273b0
    • (1966) Nature , vol.212 , pp. 1273-1274
    • Austin, W.C.1    Courtney, W.2    Danilewicz, J.C.3    Morgan, D.H.4    Conover, L.H.5    Howes, H.L.6
  • 6
    • 0342716455 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptors in the nematode Caenorhabditis elegans
    • doi: 10.1006/jmbi.1996.0248
    • Ballivet, M., Alliod, C., Bertrand, S., and Bertrand, D. (1996). Nicotinic acetylcholine receptors in the nematode Caenorhabditis elegans. J. Mol. Biol. 258, 261-269. doi: 10.1006/jmbi.1996.0248
    • (1996) J. Mol. Biol. , vol.258 , pp. 261-269
    • Ballivet, M.1    Alliod, C.2    Bertrand, S.3    Bertrand, D.4
  • 7
    • 0037352879 scopus 로고    scopus 로고
    • Pharmacological characterization of the homomeric and heteromeric UNC-49 GABA receptors in C. elegans
    • doi: 10.1038/sj.bjp.0705119
    • Bamber, B. A., Twyman, R. E., and Jorgensen, E. M. (2003). Pharmacological characterization of the homomeric and heteromeric UNC-49 GABA receptors in C. elegans. Br. J. Pharmacol. 138, 883-893. doi: 10.1038/sj.bjp.0705119
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 883-893
    • Bamber, B.A.1    Twyman, R.E.2    Jorgensen, E.M.3
  • 8
    • 0035999833 scopus 로고    scopus 로고
    • Openings of the rat recombinant alpha 1 homomeric glycine receptor as a function of the number of agonist molecules bound
    • doi: 10.1085/jgp.20028530
    • Beato, M., Groot-Kormelink, P. J., Colquhoun, D., and Sivilotti, L. G. (2002). Openings of the rat recombinant alpha 1 homomeric glycine receptor as a function of the number of agonist molecules bound. J. Gen. Physiol. 119, 443-466. doi: 10.1085/jgp.20028530
    • (2002) J. Gen. Physiol. , vol.119 , pp. 443-466
    • Beato, M.1    Groot-Kormelink, P.J.2    Colquhoun, D.3    Sivilotti, L.G.4
  • 9
    • 84885372028 scopus 로고    scopus 로고
    • Characterization of cys-loop receptor genes involved in inhibitory amine neurotransmission in parasitic and free living nematodes
    • doi: 10.1016/j.parint.2013.03.010
    • Beech, R. N., Callanan, M. K., Rao, V. T., Dawe, G. B., and Forrester, S. G. (2013). Characterization of cys-loop receptor genes involved in inhibitory amine neurotransmission in parasitic and free living nematodes. Parasitol. Int. 62, 599-605. doi: 10.1016/j.parint.2013.03.010
    • (2013) Parasitol. Int. , vol.62 , pp. 599-605
    • Beech, R.N.1    Callanan, M.K.2    Rao, V.T.3    Dawe, G.B.4    Forrester, S.G.5
  • 10
    • 77953963380 scopus 로고    scopus 로고
    • Nematode parasite genes: what's in a name?
    • doi: 10.1016/j.pt.2010.04.003
    • Beech, R. N., Wolstenholme, A. J., Neveu, C., and Dent, J. A. (2010). Nematode parasite genes: what's in a name? Trends Parasitol. 26, 334-340. doi: 10.1016/j.pt.2010.04.003
    • (2010) Trends Parasitol. , vol.26 , pp. 334-340
    • Beech, R.N.1    Wolstenholme, A.J.2    Neveu, C.3    Dent, J.A.4
  • 11
    • 0037072311 scopus 로고    scopus 로고
    • Cation-p interactions in ligand recognition by serotonergic (5-HT3A) and nicotinic acetylcholine receptors: the anomalous binding properties of nicotine
    • doi: 10.1021/bi020266d
    • Beene, D. L., Brandt, G. S., Zhong, W., Zacharias, N. M., Lester, H. A., and Dougherty, D. A. (2002). Cation-p interactions in ligand recognition by serotonergic (5-HT3A) and nicotinic acetylcholine receptors: the anomalous binding properties of nicotine. Biochemistry 41, 10262-10269. doi: 10.1021/bi020266d
    • (2002) Biochemistry , vol.41 , pp. 10262-10269
    • Beene, D.L.1    Brandt, G.S.2    Zhong, W.3    Zacharias, N.M.4    Lester, H.A.5    Dougherty, D.A.6
  • 12
    • 5644237713 scopus 로고    scopus 로고
    • Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis
    • doi: 10.1523/JNEUROSCI.2429-04.2004
    • 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. doi: 10.1523/JNEUROSCI.2429-04.2004
    • (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
  • 13
    • 0025313553 scopus 로고
    • The human muscle nicotinic acetylcholine receptor alpha-subunit exist as two isoforms: a novel exon
    • Beeson, D., Morris, A., Vincent, A., and Newsom-Davis, J. (1990). The human muscle nicotinic acetylcholine receptor alpha-subunit exist as two isoforms: a novel exon. EMBO J. 9, 2101-2106.
    • (1990) EMBO J. , vol.9 , pp. 2101-2106
    • Beeson, D.1    Morris, A.2    Vincent, A.3    Newsom-Davis, J.4
  • 14
    • 0033981982 scopus 로고    scopus 로고
    • The concept of transmitter receptors: 100 years on
    • doi: 10.1016/S0028-3908(99)00137-9
    • Bennett, M. R. (2000). The concept of transmitter receptors: 100 years on. Neuropharmacology 39, 523-546. doi: 10.1016/S0028-3908(99)00137-9
    • (2000) Neuropharmacology , vol.39 , pp. 523-546
    • Bennett, M.R.1
  • 15
    • 84872033261 scopus 로고    scopus 로고
    • A unified model of the GABA(A) receptor comprising agonist and benzodiazepine binding sites
    • doi: 10.1371/journal.pone.0052323
    • Bergmann, R., Kongsbak, K., Sorensen, P. L., Sander, T., and Balle, T. (2013). A unified model of the GABA(A) receptor comprising agonist and benzodiazepine binding sites. PLoS ONE 8:e52323. doi: 10.1371/journal.pone.0052323
    • (2013) PLoS ONE , vol.8
    • Bergmann, R.1    Kongsbak, K.2    Sorensen, P.L.3    Sander, T.4    Balle, T.5
  • 16
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • doi: 10.1038/nature07462
    • Bocquet, N., Nury, H., Baaden, M., Le Poupon, C., Changeux, J. P., Delarue, M., et al. (2009). X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457, 111-114. doi: 10.1038/nature07462
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1    Nury, H.2    Baaden, M.3    Le Poupon, C.4    Changeux, J.P.5    Delarue, M.6
  • 17
    • 33846106078 scopus 로고    scopus 로고
    • A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family
    • doi: 10.1038/nature05371
    • Bocquet, N., Prado de Carvalho, L., Cartaud, J., Neyton, J., Le Poupon, C., Taly, A., et al. (2007). A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family. Nature 445, 116-119. doi: 10.1038/nature05371
    • (2007) Nature , vol.445 , pp. 116-119
    • Bocquet, N.1    Prado de Carvalho, L.2    Cartaud, J.3    Neyton, J.4    Le Poupon, C.5    Taly, A.6
  • 18
    • 80054036923 scopus 로고    scopus 로고
    • Functional reconstitution of Haemonchus contortus acetylcholine receptors in Xenopus oocytes provides mechanistic insights into levamisole resistance
    • doi: 10.1111/j.1476-5381.2011.01420.x
    • Boulin, T., Fauvin, A., Charvet, C. L., Cortet, J., Cabaret, J., Bessereau, J. L., et al. (2011). Functional reconstitution of Haemonchus contortus acetylcholine receptors in Xenopus oocytes provides mechanistic insights into levamisole resistance. Br. J. Pharmacol. 164, 1421-1432. doi: 10.1111/j.1476-5381.2011.01420.x
    • (2011) Br. J. Pharmacol. , vol.164 , pp. 1421-1432
    • Boulin, T.1    Fauvin, A.2    Charvet, C.L.3    Cortet, J.4    Cabaret, J.5    Bessereau, J.L.6
  • 19
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • doi: 10.1038/35077011
    • Brejc, K., van Dijk, W. J., Klaassen, R. V., Schuurmans, M., van der Oost, J., Smit, A. B., et al. (2001). Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411, 269-276. doi: 10.1038/35077011
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    van der Oost, J.5    Smit, A.B.6
  • 20
    • 0036792118 scopus 로고    scopus 로고
    • Evolution of amino acid frequencies in proteins over deep time: inferred order of introduction of amino acids into the genetic code
    • doi: 10.1093/oxfordjournals.molbev.a003988
    • Brooks, D. J., Fresco, J. R., Lesk, A. M., and Singh, M. (2002). Evolution of amino acid frequencies in proteins over deep time: inferred order of introduction of amino acids into the genetic code. Mol. Biol. Evol. 19, 1645-1655. doi: 10.1093/oxfordjournals.molbev.a003988
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1645-1655
    • Brooks, D.J.1    Fresco, J.R.2    Lesk, A.M.3    Singh, M.4
  • 21
    • 33846341182 scopus 로고    scopus 로고
    • Chemical-scale studies on the role of a conserved aspartate in preorganizing the agonist binding site of the nicotinic acetylcholine receptor
    • doi: 10.1021/bi061638b
    • Cashin, A. L., Torrice, M. M., McMenimen, K. A., Lester, H. A., and Dougherty, D. A. (2007). Chemical-scale studies on the role of a conserved aspartate in preorganizing the agonist binding site of the nicotinic acetylcholine receptor. Biochemistry 46, 630-639. doi: 10.1021/bi061638b
    • (2007) Biochemistry , vol.46 , pp. 630-639
    • Cashin, A.L.1    Torrice, M.M.2    McMenimen, K.A.3    Lester, H.A.4    Dougherty, D.A.5
  • 22
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • doi: 10.1016/S0896-6273(04)00115-1
    • Celie, P. H., van Rossum-Fikkert, S. E., van Dijk, W. J., Brejc, K., Smit, A. B., and Sixma, T. K. (2004). Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures. Neuron 41, 907-914. doi: 10.1016/S0896-6273(04)00115-1
    • (2004) Neuron , vol.41 , pp. 907-914
    • Celie, P.H.1    van Rossum-Fikkert, S.E.2    van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 23
    • 0030941561 scopus 로고    scopus 로고
    • Pharmacological characterization of recombinant human neuronal nicotinic acetylcholine receptors h alpha 2 beta 2, h alpha 2 beta 4, h alpha 3 beta 2, h alpha 3 beta 4, h alpha 4 beta 2, h alpha 4 beta 4 and h alpha 7 expressed in Xenopus oocytes
    • Chavez-Noriega, L. E., Crona, J. H., Washburn, M. S., Urrutia, A., Elliott, K. J., and Johnson, E. C. (1997). Pharmacological characterization of recombinant human neuronal nicotinic acetylcholine receptors h alpha 2 beta 2, h alpha 2 beta 4, h alpha 3 beta 2, h alpha 3 beta 4, h alpha 4 beta 2, h alpha 4 beta 4 and h alpha 7 expressed in Xenopus oocytes. J. Pharmacol. Exp. Ther. 280, 346-356.
    • (1997) J. Pharmacol. Exp. Ther. , vol.280 , pp. 346-356
    • Chavez-Noriega, L.E.1    Crona, J.H.2    Washburn, M.S.3    Urrutia, A.4    Elliott, K.J.5    Johnson, E.C.6
  • 24
    • 0034982289 scopus 로고    scopus 로고
    • High-affinity ivermectin binding to recombinant subunits of the Haemonchus contortus glutamate-gated chloride channel
    • doi: 10.1016/S0166-6851(01)00258-4
    • Cheeseman, C. L., Delany, N. S., Woods, D. J., and Wolstenholme, A. J. (2001). High-affinity ivermectin binding to recombinant subunits of the Haemonchus contortus glutamate-gated chloride channel. Mol. Biochem. Parasitol. 114, 161-168. doi: 10.1016/S0166-6851(01)00258-4
    • (2001) Mol. Biochem. Parasitol. , vol.114 , pp. 161-168
    • Cheeseman, C.L.1    Delany, N.S.2    Woods, D.J.3    Wolstenholme, A.J.4
  • 25
    • 58049126584 scopus 로고    scopus 로고
    • A nomenclature for ligand-gated ion channels
    • doi: 10.1016/j.neuropharm.2008.06.063
    • Collingridge, G. L., Olsen, R. W., Peters, J., and Spedding, M. (2009). A nomenclature for ligand-gated ion channels. Neuropharmacology 56, 2-5. doi: 10.1016/j.neuropharm.2008.06.063
    • (2009) Neuropharmacology , vol.56 , pp. 2-5
    • Collingridge, G.L.1    Olsen, R.W.2    Peters, J.3    Spedding, M.4
  • 26
    • 0029078817 scopus 로고
    • Identification of a new component of the agonist binding-site of the nicotinic alpha-7 homooligomeric receptor
    • doi: 10.1074/jbc.270.20.11749
    • Corringer, P. J., Galzi, J. L., Eisele, J. L., Bertrand, S., Changeux, J. P., and Bertrand, D. (1995). Identification of a new component of the agonist binding-site of the nicotinic alpha-7 homooligomeric receptor. J. Biol. Chem. 270, 11749-11752. doi: 10.1074/jbc.270.20.11749
    • (1995) J. Biol. Chem. , vol.270 , pp. 11749-11752
    • Corringer, P.J.1    Galzi, J.L.2    Eisele, J.L.3    Bertrand, S.4    Changeux, J.P.5    Bertrand, D.6
  • 27
    • 0036607862 scopus 로고    scopus 로고
    • Anxiety over GABA(A) receptor structure relieved by AChBP
    • doi: 10.1016/S0968-0004(02)02092-3
    • Cromer, B. A., Morton, C. J., and Parker, M. W. (2002). Anxiety over GABA(A) receptor structure relieved by AChBP. Trends Biochem. Sci. 27, 280-287. doi: 10.1016/S0968-0004(02)02092-3
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 280-287
    • Cromer, B.A.1    Morton, C.J.2    Parker, M.W.3
  • 28
    • 0028036881 scopus 로고
    • Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans
    • doi: 10.1038/371707a0
    • Cully, D. F., Vassilatis, D. K., Liu, K. K., Paress, P. S., Van der Ploeg, L. H., Schaeffer, J. M., et al. (1994). Cloning of an avermectin-sensitive glutamate-gated chloride channel from Caenorhabditis elegans. Nature 371, 707-711. doi: 10.1038/371707a0
    • (1994) Nature , vol.371 , pp. 707-711
    • Cully, D.F.1    Vassilatis, D.K.2    Liu, K.K.3    Paress, P.S.4    Van der Ploeg, L.H.5    Schaeffer, J.M.6
  • 29
    • 0037428517 scopus 로고    scopus 로고
    • A novel class of ligand-gated ion channel is activated by Zn2+
    • doi: 10.1074/jbc.M208814200
    • Davies, P. A., Wang, W., Hales, T. G., and Kirkness, E. F. (2003). A novel class of ligand-gated ion channel is activated by Zn2+. J. Biol. Chem. 278, 712-717. doi: 10.1074/jbc.M208814200
    • (2003) J. Biol. Chem. , vol.278 , pp. 712-717
    • Davies, P.A.1    Wang, W.2    Hales, T.G.3    Kirkness, E.F.4
  • 30
    • 0035851193 scopus 로고    scopus 로고
    • The role and predicted propensity of conserved proline residues in the 5-HT3 receptor
    • doi: 10.1074/jbc.M104569200
    • Deane, C. M., and Lummis, S. C. (2001). The role and predicted propensity of conserved proline residues in the 5-HT3 receptor. J. Biol. Chem. 276, 37962-37966. doi: 10.1074/jbc.M104569200
    • (2001) J. Biol. Chem. , vol.276 , pp. 37962-37966
    • Deane, C.M.1    Lummis, S.C.2
  • 31
    • 0024278367 scopus 로고
    • Amino acids of the Torpedo marmorata acetylcholine receptor alpha subunit labeled by a photoaffinity ligand for the acetylcholine binding site
    • doi: 10.1021/bi00407a016
    • Dennis, M., Giraudat, J., Kotzyba-Hibert, F., Goeldner, M., Hirth, C., Chang, J. Y., et al. (1988). Amino acids of the Torpedo marmorata acetylcholine receptor alpha subunit labeled by a photoaffinity ligand for the acetylcholine binding site. Biochemistry 27, 2346-2357. doi: 10.1021/bi00407a016
    • (1988) Biochemistry , vol.27 , pp. 2346-2357
    • Dennis, M.1    Giraudat, J.2    Kotzyba-Hibert, F.3    Goeldner, M.4    Hirth, C.5    Chang, J.Y.6
  • 32
    • 44849128243 scopus 로고    scopus 로고
    • Cys-loop neuroreceptors: structure to the rescue?
    • doi: 10.1021/cr078207z
    • Dougherty, D. A. (2008). Cys-loop neuroreceptors: structure to the rescue? Chem. Rev. 108, 1642-1653. doi: 10.1021/cr078207z
    • (2008) Chem. Rev. , vol.108 , pp. 1642-1653
    • Dougherty, D.A.1
  • 33
    • 0025675821 scopus 로고
    • Acetylcholine binding by a synthetic receptor: implications for biological recognition
    • doi: 10.1126/science.2274786
    • Dougherty, D. A., and Stauffer, D. A. (1990). Acetylcholine binding by a synthetic receptor: implications for biological recognition. Science 250, 1558-1560. doi: 10.1126/science.2274786
    • (1990) Science , vol.250 , pp. 1558-1560
    • Dougherty, D.A.1    Stauffer, D.A.2
  • 34
    • 84877250684 scopus 로고    scopus 로고
    • The serotonin 5-HT3 receptor: a novel neurodevelopmental target
    • doi: 10.3389/fncel.2013.00076
    • Engel, M., Smidt, M. P., and Van Hooft, J. A. (2013). The serotonin 5-HT3 receptor: a novel neurodevelopmental target. Front. Cell. Neurosci. 7:76. doi: 10.3389/fncel.2013.00076
    • (2013) Front. Cell. Neurosci. , vol.7 , pp. 76
    • Engel, M.1    Smidt, M.P.2    Van Hooft, J.A.3
  • 35
    • 0027280680 scopus 로고
    • A point mutation in a Drosophila GABA receptor confers insecticide resistance
    • doi: 10.1038/363449a0
    • Ffrench-Constant, R. H., Rocheleau, T. A., Steichen, J. C., and Chalmers, A. E. (1993). A point mutation in a Drosophila GABA receptor confers insecticide resistance. Nature 363, 449-451. doi: 10.1038/363449a0
    • (1993) Nature , vol.363 , pp. 449-451
    • Ffrench-Constant, R.H.1    Rocheleau, T.A.2    Steichen, J.C.3    Chalmers, A.E.4
  • 36
    • 84880539359 scopus 로고    scopus 로고
    • An engineered glutamate-gated chloride (GluCl) channel for sensitive, consistent neuronal silencing by ivermectin
    • doi: 10.1074/jbc.M112.423921
    • Frazier, S. J., Cohen, B. N., and Lester, H. A. (2013). An engineered glutamate-gated chloride (GluCl) channel for sensitive, consistent neuronal silencing by ivermectin. J. Biol. Chem. 288, 21029-21042. doi: 10.1074/jbc.M112.423921
    • (2013) J. Biol. Chem. , vol.288 , pp. 21029-21042
    • Frazier, S.J.1    Cohen, B.N.2    Lester, H.A.3
  • 37
    • 0033578302 scopus 로고    scopus 로고
    • Cation-p interactions in structural biology
    • doi: 10.1073/pnas.96.17.9459
    • Gallivan, J. P., and Dougherty, D. A. (1999). Cation-p interactions in structural biology. Proc. Natl. Acad. Sci. U.S.A. 96, 9459-9464. doi: 10.1073/pnas.96.17.9459
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 9459-9464
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 38
    • 0034624393 scopus 로고    scopus 로고
    • A Computational study of cation-p Interactions vs salt bridges in aqueous media: implications for protein engineering
    • doi: 10.1021/ja991755c
    • Gallivan, J. P., and Dougherty, D. A. (2000). A Computational study of cation-p Interactions vs salt bridges in aqueous media: implications for protein engineering. J. Am. Chem. Soc. 122, 870-874. doi: 10.1021/ja991755c
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 870-874
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 39
    • 0025346780 scopus 로고
    • Identification of a novel amino acid alpha-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-binding sites
    • Galzi, J. L., Revah, F., Black, D., Goeldner, M., Hirth, C., and Changeux, J. P. (1990). Identification of a novel amino acid alpha-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine receptor by photoaffinity labeling. Additional evidence for a three-loop model of the cholinergic ligands-binding sites. J. Biol. Chem. 265, 10430-10437.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10430-10437
    • Galzi, J.L.1    Revah, F.2    Black, D.3    Goeldner, M.4    Hirth, C.5    Changeux, J.P.6
  • 40
    • 80053209156 scopus 로고    scopus 로고
    • Three arginines in the GABAA receptor binding pocket have distinct roles in the formation and stability of agonist- versus antagonist-bound complexes
    • doi: 10.1124/mol.111.072033
    • Goldschen-Ohm, M. P., Wagner, D. A., and Jones, M. V. (2011). Three arginines in the GABAA receptor binding pocket have distinct roles in the formation and stability of agonist- versus antagonist-bound complexes. Mol. Pharmacol. 80, 647-656. doi: 10.1124/mol.111.072033
    • (2011) Mol. Pharmacol. , vol.80 , pp. 647-656
    • Goldschen-Ohm, M.P.1    Wagner, D.A.2    Jones, M.V.3
  • 41
    • 14644414132 scopus 로고    scopus 로고
    • The beta subunit determines the ligand binding properties of synaptic glycine receptors
    • doi: 10.1016/j.neuron.2005.01.028
    • Grudzinska, J., Schemm, R., Haeger, S., Nicke, A., Schmalzing, G., Betz, H., et al. (2005). The beta subunit determines the ligand binding properties of synaptic glycine receptors. Neuron 45, 727-739. doi: 10.1016/j.neuron.2005.01.028
    • (2005) Neuron , vol.45 , pp. 727-739
    • Grudzinska, J.1    Schemm, R.2    Haeger, S.3    Nicke, A.4    Schmalzing, G.5    Betz, H.6
  • 43
    • 0037544107 scopus 로고    scopus 로고
    • An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors
    • doi: 10.1093/emboj/cdg197
    • Grutter, T., Prado de Carvalho, L., Le Novere, N., Corringer, P. J., Edelstein, S., and Changeux, J. P. (2003). An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors. EMBO J. 22, 1990-2003. doi: 10.1093/emboj/cdg197
    • (2003) EMBO J. , vol.22 , pp. 1990-2003
    • Grutter, T.1    Prado de Carvalho, L.2    Le Novere, N.3    Corringer, P.J.4    Edelstein, S.5    Changeux, J.P.6
  • 44
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • doi: 10.1038/sj.emboj.7600828
    • Hansen, S. B., Sulzenbacher, G., Huxford, T., Marchot, P., Taylor, P., and Bourne, Y. (2005). Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. EMBO J. 24, 3635-3646. doi: 10.1038/sj.emboj.7600828
    • (2005) EMBO J. , vol.24 , pp. 3635-3646
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 45
    • 81055154363 scopus 로고    scopus 로고
    • Arginine residues at internal positions in a protein are always charged
    • doi: 10.1073/pnas.1104808108
    • Harms, M. J., Schlessman, J. L., Sue, G. R., and Garcia-Moreno, B. (2011). Arginine residues at internal positions in a protein are always charged. Proc. Natl. Acad. Sci. U.S.A. 108, 18954-18959. doi: 10.1073/pnas.1104808108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 18954-18959
    • Harms, M.J.1    Schlessman, J.L.2    Sue, G.R.3    Garcia-Moreno, B.4
  • 46
    • 79960953776 scopus 로고    scopus 로고
    • Unraveling the high- and low-sensitivity agonist responses of nicotinic acetylcholine receptors
    • doi: 10.1523/JNEUROSCI.1509-11.2011
    • Harpsoe, K., Ahring, P. K., Christensen, J. K., Jensen, M. L., Peters, D., and Balle, T. (2011). Unraveling the high- and low-sensitivity agonist responses of nicotinic acetylcholine receptors. J. Neurosci. 31, 10759-10766. doi: 10.1523/JNEUROSCI.1509-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 10759-10766
    • Harpsoe, K.1    Ahring, P.K.2    Christensen, J.K.3    Jensen, M.L.4    Peters, D.5    Balle, T.6
  • 47
    • 84987034433 scopus 로고
    • Mode of action of the anthelmintics morantel, pyrantel and levamisole on muscle-cell membrane of the nematode Ascaris-suum
    • doi: 10.1002/ps.2780160612
    • Harrow, I. D., and Gration, A. F. (1985). Mode of action of the anthelmintics morantel, pyrantel and levamisole on muscle-cell membrane of the nematode Ascaris-suum. Pestic. Sci. 16, 662-672. doi: 10.1002/ps.2780160612
    • (1985) Pestic. Sci. , vol.16 , pp. 662-672
    • Harrow, I.D.1    Gration, A.F.2
  • 48
    • 0034075940 scopus 로고    scopus 로고
    • Glycine receptors containing the alpha4 subunit in the embryonic sympathetic nervous system, spinal cord and male genital ridge
    • doi: 10.1046/j.1460-9568.2000.00993.x
    • Harvey, R. J., Schmieden, V., Von Holst, A., Laube, B., Rohrer, H., and Betz, H. (2000). Glycine receptors containing the alpha4 subunit in the embryonic sympathetic nervous system, spinal cord and male genital ridge. Eur. J. Neurosci. 12, 994-1001. doi: 10.1046/j.1460-9568.2000.00993.x
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 994-1001
    • Harvey, R.J.1    Schmieden, V.2    Von Holst, A.3    Laube, B.4    Rohrer, H.5    Betz, H.6
  • 49
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • doi: 10.1038/nature10139
    • Hibbs, R. E., and Gouaux, E. (2011). Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 474, 54-60. doi: 10.1038/nature10139
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 50
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • doi: 10.1038/nature06717
    • Hilf, R. J., and Dutzler, R. (2008). X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452, 375-379. doi: 10.1038/nature06717
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 51
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • doi: 10.1038/nature07461
    • Hilf, R. J., and Dutzler, R. (2009). Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature 457, 115-118. doi: 10.1038/nature07461
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 52
    • 44449110466 scopus 로고    scopus 로고
    • Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin
    • doi: 10.1007/s10158-008-0069-3
    • Ihara, M., Okajima, T., Yamashita, A., Oda, T., Hirata, K., Nishiwaki, H., et al. (2008). Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin. Invert. Neurosci. 8, 71-81. doi: 10.1007/s10158-008-0069-3
    • (2008) Invert. Neurosci. , vol.8 , pp. 71-81
    • Ihara, M.1    Okajima, T.2    Yamashita, A.3    Oda, T.4    Hirata, K.5    Nishiwaki, H.6
  • 53
    • 56649102324 scopus 로고    scopus 로고
    • High tolerance for ionizable residues in the hydrophobic interior of proteins
    • doi: 10.1073/pnas.0805113105
    • Isom, D. G., Cannon, B. R., Castaneda, C. A., Robinson, A., and Garcia-Moreno, B. (2008). High tolerance for ionizable residues in the hydrophobic interior of proteins. Proc. Natl. Acad. Sci. U.S.A. 105, 17784-17788. doi: 10.1073/pnas.0805113105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 17784-17788
    • Isom, D.G.1    Cannon, B.R.2    Castaneda, C.A.3    Robinson, A.4    Garcia-Moreno, B.5
  • 54
    • 79955092337 scopus 로고    scopus 로고
    • Large shifts in pKa values of lysine residues buried inside a protein
    • doi: 10.1073/pnas.1010750108
    • Isom, D. G., Castaneda, C. A., Cannon, B. R., and Garcia-Moreno, B. (2011). Large shifts in pKa values of lysine residues buried inside a protein. Proc. Natl. Acad. Sci. U.S.A. 108, 5260-5265. doi: 10.1073/pnas.1010750108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 5260-5265
    • Isom, D.G.1    Castaneda, C.A.2    Cannon, B.R.3    Garcia-Moreno, B.4
  • 55
    • 0022628717 scopus 로고
    • Kinetics of unliganded acetylcholine receptor channel gating
    • doi: 10.1016/S0006-3495(86)83693-1
    • Jackson, M. B. (1986). Kinetics of unliganded acetylcholine receptor channel gating. Biophys. J. 49, 663-672. doi: 10.1016/S0006-3495(86)83693-1
    • (1986) Biophys. J. , vol.49 , pp. 663-672
    • Jackson, M.B.1
  • 56
    • 40749099893 scopus 로고    scopus 로고
    • A new class of anthelmintics effective against drug-resistant nematodes
    • doi: 10.1038/nature06722
    • Kaminsky, R., Ducray, P., Jung, M., Clover, R., Rufener, L., Bouvier, J., et al. (2008). A new class of anthelmintics effective against drug-resistant nematodes. Nature 452, 176-180. doi: 10.1038/nature06722
    • (2008) Nature , vol.452 , pp. 176-180
    • Kaminsky, R.1    Ducray, P.2    Jung, M.3    Clover, R.4    Rufener, L.5    Bouvier, J.6
  • 57
    • 0037448581 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in the GABA(A) receptor
    • doi: 10.1038/nature01280
    • Kash, T. L., Jenkins, A., Kelley, J. C., Trudell, J. R., and Harrison, N. L. (2003). Coupling of agonist binding to channel gating in the GABA(A) receptor. Nature 421, 272-275. doi: 10.1038/nature01280
    • (2003) Nature , vol.421 , pp. 272-275
    • Kash, T.L.1    Jenkins, A.2    Kelley, J.C.3    Trudell, J.R.4    Harrison, N.L.5
  • 58
    • 68449095532 scopus 로고    scopus 로고
    • Aplysia cys-loop glutamate-gated chloride channels reveal convergent evolution of ligand specificity
    • doi: 10.1007/s00239-009-9256-z
    • Kehoe, J., Buldakova, S., Acher, F., Dent, J., Bregestovski, P., and Bradley, J. (2009). Aplysia cys-loop glutamate-gated chloride channels reveal convergent evolution of ligand specificity. J. Mol. Evol. 69, 125-141. doi: 10.1007/s00239-009-9256-z
    • (2009) J. Mol. Evol. , vol.69 , pp. 125-141
    • Kehoe, J.1    Buldakova, S.2    Acher, F.3    Dent, J.4    Bregestovski, P.5    Bradley, J.6
  • 59
    • 84871927415 scopus 로고    scopus 로고
    • Structural basis of ligand recognition in 5-HT3 receptors
    • doi: 10.1038/embor.2012.189
    • Kesters, D., Thompson, A. J., Brams, M., Van Elk, R., Spurny, R., Geitmann, M., et al. (2013). Structural basis of ligand recognition in 5-HT3 receptors. EMBO Rep. 14, 49-56. doi: 10.1038/embor.2012.189
    • (2013) EMBO Rep. , vol.14 , pp. 49-56
    • Kesters, D.1    Thompson, A.J.2    Brams, M.3    Van Elk, R.4    Spurny, R.5    Geitmann, M.6
  • 60
    • 58849151840 scopus 로고    scopus 로고
    • Structural rearrangements in loop F of the GABA receptor signal ligand binding, not channel activation
    • doi: 10.1016/j.bpj.2008.09.011
    • Khatri, A., Sedelnikova, A., and Weiss, D. S. (2009). Structural rearrangements in loop F of the GABA receptor signal ligand binding, not channel activation. Biophys. J. 96, 45-55. doi: 10.1016/j.bpj.2008.09.011
    • (2009) Biophys. J. , vol.96 , pp. 45-55
    • Khatri, A.1    Sedelnikova, A.2    Weiss, D.S.3
  • 61
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins
    • doi: 10.1021/cb800314v
    • Koide, S., and Sidhu, S. S. (2009). The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins. ACS Chem. Biol. 4, 325-334. doi: 10.1021/cb800314v
    • (2009) ACS Chem. Biol. , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 62
    • 28444445585 scopus 로고    scopus 로고
    • GABA(A) receptor subtypes as targets for neuropsychiatric drug development
    • doi: 10.1016/j.pharmthera.2005.05.009
    • Korpi, E. R., and Sinkkonen, S. T. (2006). GABA(A) receptor subtypes as targets for neuropsychiatric drug development. Pharmacol. Ther. 109, 12-32. doi: 10.1016/j.pharmthera.2005.05.009
    • (2006) Pharmacol. Ther. , vol.109 , pp. 12-32
    • Korpi, E.R.1    Sinkkonen, S.T.2
  • 63
    • 0019775167 scopus 로고
    • Gaba agonists-development and interactions with the gaba receptor complex
    • doi: 10.1007/BF00235692
    • Krogsgaard-Larsen, P., and Falch, E. (1981). Gaba agonists-development and interactions with the gaba receptor complex. Mol. Cell. Biochem. 38, 129-146. doi: 10.1007/BF00235692
    • (1981) Mol. Cell. Biochem. , vol.38 , pp. 129-146
    • Krogsgaard-Larsen, P.1    Falch, E.2
  • 64
    • 84910491966 scopus 로고
    • Observations on the physiological action of extracts of the supra-renal bodies
    • Langley, J. N. (1901). Observations on the physiological action of extracts of the supra-renal bodies. J. Physiol. 27, 237-256.
    • (1901) J. Physiol. , vol.27 , pp. 237-256
    • Langley, J.N.1
  • 66
    • 8644263906 scopus 로고    scopus 로고
    • Invariant aspartic Acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding
    • doi: 10.1085/jgp.200409077
    • Lee, W. Y., and Sine, S. M. (2004). Invariant aspartic Acid in muscle nicotinic receptor contributes selectively to the kinetics of agonist binding. J. Gen. Physiol. 124, 555-567. doi: 10.1085/jgp.200409077
    • (2004) J. Gen. Physiol. , vol.124 , pp. 555-567
    • Lee, W.Y.1    Sine, S.M.2
  • 67
    • 0036890828 scopus 로고    scopus 로고
    • Nicotinic receptor subtypes and cognitive function
    • doi: 10.1002/neu.10151
    • Levin, E. D. (2002). Nicotinic receptor subtypes and cognitive function. J. Neurobiol. 53, 633-640. doi: 10.1002/neu.10151
    • (2002) J. Neurobiol. , vol.53 , pp. 633-640
    • Levin, E.D.1
  • 68
    • 0037174128 scopus 로고    scopus 로고
    • Selective elimination of glutamate activation and introduction of fluorescent proteins into a Caenorhabditis elegans chloride channel
    • doi: 10.1016/S0014-5793(02)03245-3
    • Li, P., Slimko, E. M., and Lester, H. A. (2002). Selective elimination of glutamate activation and introduction of fluorescent proteins into a Caenorhabditis elegans chloride channel. FEBS Lett. 528, 77-82. doi: 10.1016/S0014-5793(02)03245-3
    • (2002) FEBS Lett. , vol.528 , pp. 77-82
    • Li, P.1    Slimko, E.M.2    Lester, H.A.3
  • 69
    • 20844435484 scopus 로고    scopus 로고
    • A nicotinic acetylcholine receptor mutation conferring target-site resistance to imidacloprid in Nilaparvata lugens (brown planthopper)
    • doi: 10.1073/pnas.0502901102
    • Liu, Z., Williamson, M. S., Lansdell, S. J., Denholm, I., Han, Z., and Millar, N. S. (2005). A nicotinic acetylcholine receptor mutation conferring target-site resistance to imidacloprid in Nilaparvata lugens (brown planthopper). Proc. Natl. Acad. Sci. U.S.A. 102, 8420-8425. doi: 10.1073/pnas.0502901102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8420-8425
    • Liu, Z.1    Williamson, M.S.2    Lansdell, S.J.3    Denholm, I.4    Han, Z.5    Millar, N.S.6
  • 70
    • 0034613173 scopus 로고    scopus 로고
    • Molecular and neuronal substrate for the selective attenuation of anxiety
    • doi: 10.1126/science.290.5489.131
    • Low, K., Crestani, F., Keist, R., Benke, D., Brunig, I., Benson, J. A., et al. (2000). Molecular and neuronal substrate for the selective attenuation of anxiety. Science 290, 131-134. doi: 10.1126/science.290.5489.131
    • (2000) Science , vol.290 , pp. 131-134
    • Low, K.1    Crestani, F.2    Keist, R.3    Benke, D.4    Brunig, I.5    Benson, J.A.6
  • 71
    • 84870031999 scopus 로고    scopus 로고
    • 5-HT(3) receptors
    • doi: 10.1074/jbc.R112.406496
    • Lummis, S. C. (2012). 5-HT(3) receptors. J. Biol. Chem. 287, 40239-40245. doi: 10.1074/jbc.R112.406496
    • (2012) J. Biol. Chem. , vol.287 , pp. 40239-40245
    • Lummis, S.C.1
  • 72
    • 84863338048 scopus 로고    scopus 로고
    • Multiple tyrosine residues contribute to GABA binding in the GABA(C) receptor binding pocket
    • doi: 10.1021/cn200103n
    • Lummis, S. C., Harrison, N. J., Wang, J., Ashby, J. A., Millen, K. S., Beene, D. L., et al. (2012). Multiple tyrosine residues contribute to GABA binding in the GABA(C) receptor binding pocket. ACS Chem. Neurosci. 3, 186-192. doi: 10.1021/cn200103n
    • (2012) ACS Chem. Neurosci. , vol.3 , pp. 186-192
    • Lummis, S.C.1    Harrison, N.J.2    Wang, J.3    Ashby, J.A.4    Millen, K.S.5    Beene, D.L.6
  • 73
    • 25144465496 scopus 로고    scopus 로고
    • A cation-p binding interaction with a tyrosine in the binding site of the GABAC receptor
    • doi: 10.1016/j.chembiol.2005.06.012
    • Lummis, S. C., L., Beene, D., Harrison, N. J., Lester, H. A., and Dougherty, D. A. (2005). A cation-p binding interaction with a tyrosine in the binding site of the GABAC receptor. Chem. Biol. 12, 993-997. doi: 10.1016/j.chembiol.2005.06.012
    • (2005) Chem. Biol. , vol.12 , pp. 993-997
    • Lummis, S.C.L.1    Beene, D.2    Harrison, N.J.3    Lester, H.A.4    Dougherty, D.A.5
  • 74
    • 80052182729 scopus 로고    scopus 로고
    • Two amino acid residues contribute to a cation-p binding interaction in the binding site of an insect GABA receptor
    • doi: 10.1523/JNEUROSCI.1610-11.2011
    • Lummis, S. C., McGonigle, I., Ashby, J. A., and Dougherty, D. A. (2011). Two amino acid residues contribute to a cation-p binding interaction in the binding site of an insect GABA receptor. J. Neurosci. 31, 12371-12376. doi: 10.1523/JNEUROSCI.1610-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 12371-12376
    • Lummis, S.C.1    McGonigle, I.2    Ashby, J.A.3    Dougherty, D.A.4
  • 75
    • 58049120621 scopus 로고    scopus 로고
    • Native glycine receptor subtypes and their physiological roles
    • doi: 10.1016/j.neuropharm.2008.07.034
    • Lynch, J. W. (2009). Native glycine receptor subtypes and their physiological roles. Neuropharmacology 56, 303-309. doi: 10.1016/j.neuropharm.2008.07.034
    • (2009) Neuropharmacology , vol.56 , pp. 303-309
    • Lynch, J.W.1
  • 77
    • 33847364853 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptors: targets for commercially important insecticides
    • doi: 10.1007/s10158-006-0040-0
    • Millar, N. S., and Denholm, I. (2007). Nicotinic acetylcholine receptors: targets for commercially important insecticides. Invert. Neurosci. 7, 53-66. doi: 10.1007/s10158-006-0040-0
    • (2007) Invert. Neurosci. , vol.7 , pp. 53-66
    • Millar, N.S.1    Denholm, I.2
  • 78
    • 77950494200 scopus 로고    scopus 로고
    • Binding, activation and modulation of Cys-loop receptors
    • doi: 10.1016/j.tips.2009.12.005
    • Miller, P. S., and Smart, T. G. (2010). Binding, activation and modulation of Cys-loop receptors. Trends Pharmacol. Sci. 31, 161-174. doi: 10.1016/j.tips.2009.12.005
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 161-174
    • Miller, P.S.1    Smart, T.G.2
  • 79
    • 77952909252 scopus 로고    scopus 로고
    • Distinct activities of GABA agonists at synaptic- and extrasynaptic-type GABA(A) receptors
    • doi: 10.1113/jphysiol.2009.182444
    • Mortensen, M., Ebert, B., Wafford, K., and Smart, T. G. (2010). Distinct activities of GABA agonists at synaptic- and extrasynaptic-type GABA(A) receptors. J. Physiol. 588, 1251-1268. doi: 10.1113/jphysiol.2009.182444
    • (2010) J. Physiol. , vol.588 , pp. 1251-1268
    • Mortensen, M.1    Ebert, B.2    Wafford, K.3    Smart, T.G.4
  • 80
    • 0038277048 scopus 로고    scopus 로고
    • Different binding orientations for the same agonist at homologous receptors: a lock and key or a simple wedge?
    • doi: 10.1021/ja0348086
    • Mu, T. W., Lester, H. A., and Dougherty, D. A. (2003). Different binding orientations for the same agonist at homologous receptors: a lock and key or a simple wedge? J. Am. Chem. Soc. 125, 6850-6851. doi: 10.1021/ja0348086
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6850-6851
    • Mu, T.W.1    Lester, H.A.2    Dougherty, D.A.3
  • 81
    • 0037969585 scopus 로고    scopus 로고
    • The GABA(A) receptor alpha(1) subunit Pro(174)-Asp(191) segment is involved in GABA binding and channel gating
    • doi: 10.1074/jbc.M211905200
    • Newell, J. G., and Czajkowski, C. (2003). The GABA(A) receptor alpha(1) subunit Pro(174)-Asp(191) segment is involved in GABA binding and channel gating. J. Biol. Chem. 278, 13166-13172. doi: 10.1074/jbc.M211905200
    • (2003) J. Biol. Chem. , vol.278 , pp. 13166-13172
    • Newell, J.G.1    Czajkowski, C.2
  • 82
    • 84885651158 scopus 로고    scopus 로고
    • Structural insights into Cys-loop receptor function and ligand recognition
    • doi: 10.1016/j.bcp.2013.07.001
    • Nys, M., Kesters, D., and Ulens, C. (2013). Structural insights into Cys-loop receptor function and ligand recognition. Biochem. Pharmacol. 86, 1042-1053. doi: 10.1016/j.bcp.2013.07.001
    • (2013) Biochem. Pharmacol. , vol.86 , pp. 1042-1053
    • Nys, M.1    Kesters, D.2    Ulens, C.3
  • 83
    • 0026758178 scopus 로고
    • Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor
    • O'Leary, M. E., and White, M. M. (1992). Mutational analysis of ligand-induced activation of the Torpedo acetylcholine receptor. J. Biol. Chem. 267, 8360-8365.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8360-8365
    • O'Leary, M.E.1    White, M.M.2
  • 84
    • 54049137689 scopus 로고    scopus 로고
    • International Union of Pharmacology. LXX. Subtypes of gamma-aminobutyric acid(A) receptors: classification on the basis of subunit composition, pharmacology, and function. Update
    • doi: 10.1124/pr.108.00505
    • Olsen, R. W., and Sieghart, W. (2008). International Union of Pharmacology. LXX. Subtypes of gamma-aminobutyric acid(A) receptors: classification on the basis of subunit composition, pharmacology, and function. Update. Pharmacol. Rev. 60, 243-260. doi: 10.1124/pr.108.00505
    • (2008) Pharmacol. Rev. , vol.60 , pp. 243-260
    • Olsen, R.W.1    Sieghart, W.2
  • 85
    • 33846586497 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis of the GABA(A) receptor binding site residues reveals a novel cation-p interaction between GABA and beta 2Tyr97
    • doi: 10.1523/JNEUROSCI.4791-06.2007
    • Padgett, C. L., Hanek, A. P., Lester, H. A., Dougherty, D. A., and Lummis, S. C. (2007). Unnatural amino acid mutagenesis of the GABA(A) receptor binding site residues reveals a novel cation-p interaction between GABA and beta 2Tyr97. J. Neurosci. 27, 886-892. doi: 10.1523/JNEUROSCI.4791-06.2007
    • (2007) J. Neurosci. , vol.27 , pp. 886-892
    • Padgett, C.L.1    Hanek, A.P.2    Lester, H.A.3    Dougherty, D.A.4    Lummis, S.C.5
  • 86
    • 84888388626 scopus 로고    scopus 로고
    • Betaine acts on a ligand-gated ion channel in the nervous system of the nematode C. elegans
    • doi: 10.1038/nn.3575
    • Peden, A. S., Mac, P., Fei, Y. J., Castro, C., Jiang, G., Murfitt, K. J., et al. (2013). Betaine acts on a ligand-gated ion channel in the nervous system of the nematode C. elegans. Nat. Neurosci. 16, 1794-1801. doi: 10.1038/nn.3575
    • (2013) Nat. Neurosci. , vol.16 , pp. 1794-1801
    • Peden, A.S.1    Mac, P.2    Fei, Y.J.3    Castro, C.4    Jiang, G.5    Murfitt, K.J.6
  • 87
    • 84873937213 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 4-(Aminomethyl)-1-hydroxypyrazole analogues of muscimol as gamma-aminobutyric Acid(A) receptor agonists
    • doi: 10.1021/jm301473k
    • Petersen, J. G., Bergmann, R., Moller, H. A., Jorgensen, C. G., Nielsen, B., Kehler, J., et al. (2013). Synthesis and biological evaluation of 4-(Aminomethyl)-1-hydroxypyrazole analogues of muscimol as gamma-aminobutyric Acid(A) receptor agonists. J. Med. Chem. 56, 993-1006. doi: 10.1021/jm301473k
    • (2013) J. Med. Chem. , vol.56 , pp. 993-1006
    • Petersen, J.G.1    Bergmann, R.2    Moller, H.A.3    Jorgensen, C.G.4    Nielsen, B.5    Kehler, J.6
  • 88
    • 84872223512 scopus 로고    scopus 로고
    • Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences
    • doi: 10.1146/annurev-pharmtox-011112-140343
    • Pless, S. A., and Ahern, C. A. (2013). Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences. Annu. Rev. Pharmacol. Toxicol. 53, 211-229. doi: 10.1146/annurev-pharmtox-011112-140343
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 211-229
    • Pless, S.A.1    Ahern, C.A.2
  • 89
    • 79953018004 scopus 로고    scopus 로고
    • A cation-p interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists
    • doi: 10.1124/mol.110.069583
    • Pless, S. A., Hanek, A. P., Price, K. L., Lynch, J. W., Lester, H. A., Dougherty, D. A., et al. (2011). A cation-p interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists. Mol. Pharmacol. 79, 742-748. doi: 10.1124/mol.110.069583
    • (2011) Mol. Pharmacol. , vol.79 , pp. 742-748
    • Pless, S.A.1    Hanek, A.P.2    Price, K.L.3    Lynch, J.W.4    Lester, H.A.5    Dougherty, D.A.6
  • 90
    • 67650169910 scopus 로고    scopus 로고
    • Ligand-specific conformational changes in the alpha1 glycine receptor ligand-binding domain
    • doi: 10.1074/jbc.M809343200
    • Pless, S. A., and Lynch, J. W. (2009). Ligand-specific conformational changes in the alpha1 glycine receptor ligand-binding domain. J. Biol. Chem. 284, 15847-15856. doi: 10.1074/jbc.M809343200
    • (2009) J. Biol. Chem. , vol.284 , pp. 15847-15856
    • Pless, S.A.1    Lynch, J.W.2
  • 91
    • 58149166932 scopus 로고    scopus 로고
    • A cation-p interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue
    • doi: 10.1523/JNEUROSCI.2540-08.2008
    • Pless, S. A., Millen, K. S., Hanek, A. P., Lynch, J. W., Lester, H. A., Lummis, S. C., et al. (2008). A cation-p interaction in the binding site of the glycine receptor is mediated by a phenylalanine residue. J. Neurosci. 28, 10937-10942. doi: 10.1523/JNEUROSCI.2540-08.2008
    • (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
  • 92
    • 58549118250 scopus 로고    scopus 로고
    • Unliganded gating of acetylcholine receptor channels
    • doi: 10.1073/pnas.0809272106
    • Purohit, P., and Auerbach, A. (2009). Unliganded gating of acetylcholine receptor channels. Proc. Natl. Acad. Sci. U.S.A. 106, 115-120. doi: 10.1073/pnas.0809272106
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 115-120
    • Purohit, P.1    Auerbach, A.2
  • 93
    • 79954614551 scopus 로고    scopus 로고
    • Two neuronal nicotinic acetylcholine receptors, alpha4beta4 and alpha7, show differential agonist binding modes
    • doi: 10.1074/jbc.M110.206565
    • Puskar, N. L., Xiu, X., Lester, H. A., and Dougherty, D. A. (2011). Two neuronal nicotinic acetylcholine receptors, alpha4beta4 and alpha7, show differential agonist binding modes. J. Biol. Chem. 286, 14618-14627. doi: 10.1074/jbc.M110.206565
    • (2011) J. Biol. Chem. , vol.286 , pp. 14618-14627
    • Puskar, N.L.1    Xiu, X.2    Lester, H.A.3    Dougherty, D.A.4
  • 94
    • 14844332033 scopus 로고    scopus 로고
    • A family of acetylcholine-gated chloride channel subunits in Caenorhabditis elegans
    • doi: 10.1074/jbc.M412644200
    • Putrenko, I., Zakikhani, M., and Dent, J. A. (2005). A family of acetylcholine-gated chloride channel subunits in Caenorhabditis elegans. J. Biol. Chem. 280, 6392-6398. doi: 10.1074/jbc.M412644200
    • (2005) J. Biol. Chem. , vol.280 , pp. 6392-6398
    • Putrenko, I.1    Zakikhani, M.2    Dent, J.A.3
  • 95
    • 0034707063 scopus 로고    scopus 로고
    • MOD-1 is a serotonin-gated chloride channel that modulates locomotory behaviour in C. elegans
    • doi: 10.1038/35044083
    • Ranganathan, R., Cannon, S. C., and Horvitz, H. R. (2000). MOD-1 is a serotonin-gated chloride channel that modulates locomotory behaviour in C. elegans. Nature 408, 470-475. doi: 10.1038/35044083
    • (2000) Nature , vol.408 , pp. 470-475
    • Ranganathan, R.1    Cannon, S.C.2    Horvitz, H.R.3
  • 96
    • 4344594150 scopus 로고    scopus 로고
    • Molecular basis of the differential sensitivity of nematode and mammalian muscle to the anthelmintic agent levamisole
    • doi: 10.1074/jbc.M403096200
    • Rayes, D., De Rosa, M. J., Bartos, M., and Bouzat, C. (2004). Molecular basis of the differential sensitivity of nematode and mammalian muscle to the anthelmintic agent levamisole. J. Biol. Chem. 279, 36372-36381. doi: 10.1074/jbc.M403096200
    • (2004) J. Biol. Chem. , vol.279 , pp. 36372-36381
    • Rayes, D.1    De Rosa, M.J.2    Bartos, M.3    Bouzat, C.4
  • 97
    • 65949085351 scopus 로고    scopus 로고
    • Number and locations of agonist binding sites required to activate homomeric Cys-loop receptors
    • doi: 10.1523/JNEUROSCI.0627-09.2009
    • Rayes, D., De Rosa, M. J., Sine, S. M., and Bouzat, C. (2009). Number and locations of agonist binding sites required to activate homomeric Cys-loop receptors. J. Neurosci. 29, 6022-6032. doi: 10.1523/JNEUROSCI.0627-09.2009
    • (2009) J. Neurosci. , vol.29 , pp. 6022-6032
    • Rayes, D.1    De Rosa, M.J.2    Sine, S.M.3    Bouzat, C.4
  • 98
    • 0034669060 scopus 로고    scopus 로고
    • Anthelmintic actions on homomer-forming nicotinic acetylcholine receptor subunits: chicken alpha7 and ACR-16 from the nematode Caenorhabditis elegans
    • doi: 10.1016/S0306-4522(00)00279-7
    • Raymond, V., Mongan, N. P., and Sattelle, D. B. (2000). Anthelmintic actions on homomer-forming nicotinic acetylcholine receptor subunits: chicken alpha7 and ACR-16 from the nematode Caenorhabditis elegans. Neuroscience 101, 785-791. doi: 10.1016/S0306-4522(00)00279-7
    • (2000) Neuroscience , vol.101 , pp. 785-791
    • Raymond, V.1    Mongan, N.P.2    Sattelle, D.B.3
  • 99
    • 67650076325 scopus 로고    scopus 로고
    • Ligand-gated chloride channels are receptors for biogenic amines in C. elegans
    • doi: 10.1126/science.1169243
    • Ringstad, N., Abe, N., and Horvitz, H. R. (2009). Ligand-gated chloride channels are receptors for biogenic amines in C. elegans. Science 325, 96-100. doi: 10.1126/science.1169243
    • (2009) Science , vol.325 , pp. 96-100
    • Ringstad, N.1    Abe, N.2    Horvitz, H.R.3
  • 100
    • 0028557974 scopus 로고
    • The action of pyrantel as an agonist and an open channel blocker at acetylcholine receptors in isolated Ascaris suum muscle vesicles
    • doi: 10.1016/0014-2999(94)90784-6
    • Robertson, S. J., Pennington, A. J., Evans, A. M., and Martin, R. J. (1994). The action of pyrantel as an agonist and an open channel blocker at acetylcholine receptors in isolated Ascaris suum muscle vesicles. Eur. J. Pharmacol. 271, 273-282. doi: 10.1016/0014-2999(94)90784-6
    • (1994) Eur. J. Pharmacol. , vol.271 , pp. 273-282
    • Robertson, S.J.1    Pennington, A.J.2    Evans, A.M.3    Martin, R.J.4
  • 101
    • 0033592682 scopus 로고    scopus 로고
    • Benzodiazepine actions mediated by specific gamma-aminobutyric acid(A) receptor subtypes
    • doi: 10.1038/44579
    • Rudolph, U., Crestani, F., Benke, D., Brunig, I., Benson, J. A., Fritschy, J. M., et al. (1999). Benzodiazepine actions mediated by specific gamma-aminobutyric acid(A) receptor subtypes. Nature 401, 796-800. doi: 10.1038/44579
    • (1999) Nature , vol.401 , pp. 796-800
    • Rudolph, U.1    Crestani, F.2    Benke, D.3    Brunig, I.4    Benson, J.A.5    Fritschy, J.M.6
  • 102
    • 77958126455 scopus 로고    scopus 로고
    • Monepantel allosterically activates DEG-3/DES-2 channels of the gastrointestinal nematode Haemonchus contortus
    • doi: 10.1124/mol.110.066498
    • Rufener, L., Baur, R., Kaminsky, R., Maser, P., and Sigel, E. (2010). Monepantel allosterically activates DEG-3/DES-2 channels of the gastrointestinal nematode Haemonchus contortus. Mol. Pharmacol. 78, 895-902. doi: 10.1124/mol.110.066498
    • (2010) Mol. Pharmacol. , vol.78 , pp. 895-902
    • Rufener, L.1    Baur, R.2    Kaminsky, R.3    Maser, P.4    Sigel, E.5
  • 103
    • 20444375156 scopus 로고    scopus 로고
    • Nicotine upregulates its own receptors through enhanced intracellular maturation
    • doi: 10.1016/j.neuron.2005.03.029
    • Sallette, J., Pons, S., Devillers-Thiery, A., Soudant, M., Prado de Carvalho, L., Changeux, J. P., et al. (2005). Nicotine upregulates its own receptors through enhanced intracellular maturation. Neuron 46, 595-607. doi: 10.1016/j.neuron.2005.03.029
    • (2005) Neuron , vol.46 , pp. 595-607
    • Sallette, J.1    Pons, S.2    Devillers-Thiery, A.3    Soudant, M.4    Prado de Carvalho, L.5    Changeux, J.P.6
  • 104
    • 0033568859 scopus 로고    scopus 로고
    • The effects of acute nicotine on the metabolism of dopamine and the expression of Fos protein in striatal and limbic brain areas of rats during chronic nicotine infusion and its withdrawal
    • Salminen, O., Seppa, T., Gaddnas, H., and Ahtee, L. (1999). The effects of acute nicotine on the metabolism of dopamine and the expression of Fos protein in striatal and limbic brain areas of rats during chronic nicotine infusion and its withdrawal. J. Neurosci. 19, 8145-8151.
    • (1999) J. Neurosci. , vol.19 , pp. 8145-8151
    • Salminen, O.1    Seppa, T.2    Gaddnas, H.3    Ahtee, L.4
  • 105
    • 84892910277 scopus 로고    scopus 로고
    • Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation
    • doi: 10.1073/pnas.1314997111
    • Sauguet, L., Shahsavar, A., Poitevin, F., Huon, C., Menny, A., Nemecz, A., et al. (2014). Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation. Proc. Natl. Acad. Sci. U.S.A. 111, 966-971. doi: 10.1073/pnas.1314997111
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 966-971
    • Sauguet, L.1    Shahsavar, A.2    Poitevin, F.3    Huon, C.4    Menny, A.5    Nemecz, A.6
  • 106
    • 20944441090 scopus 로고    scopus 로고
    • A novel chloride channel in Drosophila melanogaster is inhibited by protons
    • doi: 10.1074/jbc.M411759200
    • Schnizler, K., Saeger, B., Pfeffer, C., Gerbaulet, A., Ebbinghaus-Kintscher, U., Methfessel, C., et al. (2005). A novel chloride channel in Drosophila melanogaster is inhibited by protons. J. Biol. Chem. 280, 16254-16262. doi: 10.1074/jbc.M411759200
    • (2005) J. Biol. Chem. , vol.280 , pp. 16254-16262
    • Schnizler, K.1    Saeger, B.2    Pfeffer, C.3    Gerbaulet, A.4    Ebbinghaus-Kintscher, U.5    Methfessel, C.6
  • 107
    • 12544249763 scopus 로고    scopus 로고
    • Mapping the rho(1) GABA(C) receptor agonist binding pocket - Constructing a complete model
    • doi: 10.1074/jbc.M409908200
    • Sedelnikova, A., Smith, C. D., Zakharkin, S. O., Davis, D., Weiss, D. S., and Chang, Y. C. (2005). Mapping the rho(1) GABA(C) receptor agonist binding pocket - Constructing a complete model. J. Biol. Chem. 280, 1535-1542. doi: 10.1074/jbc.M409908200
    • (2005) J. Biol. Chem. , vol.280 , pp. 1535-1542
    • Sedelnikova, A.1    Smith, C.D.2    Zakharkin, S.O.3    Davis, D.4    Weiss, D.S.5    Chang, Y.C.6
  • 108
    • 84862291650 scopus 로고    scopus 로고
    • Distinct properties of glycine receptor beta+/alpha- interface unambiguously characterizing heteromeric interface reconstituted in homomeric protein
    • doi: 10.1074/jbc.M111.337741
    • Shan, Q., Han, L., and Lynch, J. W. (2012). Distinct properties of glycine receptor beta+/alpha- interface unambiguously characterizing heteromeric interface reconstituted in homomeric protein. J. Biol. Chem. 287, 21244-21252. doi: 10.1074/jbc.M111.337741
    • (2012) J. Biol. Chem. , vol.287 , pp. 21244-21252
    • Shan, Q.1    Han, L.2    Lynch, J.W.3
  • 109
    • 45749146194 scopus 로고    scopus 로고
    • Individually monitoring ligand-induced changes in the structure of the GABA(A) receptor at benzodiazepine binding site and non-binding-site interfaces
    • doi: 10.1124/mol.108.044891
    • Sharkey, L. M., and Czajkowski, C. (2008). Individually monitoring ligand-induced changes in the structure of the GABA(A) receptor at benzodiazepine binding site and non-binding-site interfaces. Mol. Pharmacol. 74, 203-212. doi: 10.1124/mol.108.044891
    • (2008) Mol. Pharmacol. , vol.74 , pp. 203-212
    • Sharkey, L.M.1    Czajkowski, C.2
  • 110
    • 0036739004 scopus 로고    scopus 로고
    • Effects of mutations of a glutamine residue in loop D of the alpha7 nicotinic acetylcholine receptor on agonist profiles for neonicotinoid insecticides and related ligands
    • doi: 10.1038/sj.bjp.0704848
    • Shimomura, M., Okuda, H., Matsuda, K., Komai, K., Akamatsu, M., and Sattelle, D. B. (2002). Effects of mutations of a glutamine residue in loop D of the alpha7 nicotinic acetylcholine receptor on agonist profiles for neonicotinoid insecticides and related ligands. Br. J. Pharmacol. 137, 162-169. doi: 10.1038/sj.bjp.0704848
    • (2002) Br. J. Pharmacol. , vol.137 , pp. 162-169
    • Shimomura, M.1    Okuda, H.2    Matsuda, K.3    Komai, K.4    Akamatsu, M.5    Sattelle, D.B.6
  • 111
    • 84869992899 scopus 로고    scopus 로고
    • Structure, function, and modulation of GABA(A) receptors
    • doi: 10.1074/jbc.R112.386664
    • Sigel, E., and Steinmann, M. E. (2012). Structure, function, and modulation of GABA(A) receptors. J. Biol. Chem. 287, 40224-40231. doi: 10.1074/jbc.R112.386664
    • (2012) J. Biol. Chem. , vol.287 , pp. 40224-40231
    • Sigel, E.1    Steinmann, M.E.2
  • 112
    • 0025123090 scopus 로고
    • Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities
    • doi: 10.1085/jgp.96.2.395
    • Sine, S. M., Claudio, T., and Sigworth, F. J. (1990). Activation of Torpedo acetylcholine receptors expressed in mouse fibroblasts. Single channel current kinetics reveal distinct agonist binding affinities. J. Gen. Physiol. 96, 395-437. doi: 10.1085/jgp.96.2.395
    • (1990) J. Gen. Physiol. , vol.96 , pp. 395-437
    • Sine, S.M.1    Claudio, T.2    Sigworth, F.J.3
  • 113
    • 0028292368 scopus 로고
    • Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists
    • Sine, S. M., Quiram, P., Papanikolaou, F., Kreienkamp, H. J., and Taylor, P. (1994). Conserved tyrosines in the alpha subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists. J. Biol. Chem. 269, 8808-8816.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8808-8816
    • Sine, S.M.1    Quiram, P.2    Papanikolaou, F.3    Kreienkamp, H.J.4    Taylor, P.5
  • 114
    • 0036795364 scopus 로고    scopus 로고
    • Naturally occurring mutations at the acetylcholine receptor binding site independently alter ACh binding and channel gating
    • doi: 10.1085/jgp.20028568
    • Sine, S. M., Shen, X. M., Wang, H. L., Ohno, K., Lee, W. Y., Tsujino, A., et al. (2002). Naturally occurring mutations at the acetylcholine receptor binding site independently alter ACh binding and channel gating. J. Gen. Physiol. 120, 483-496. doi: 10.1085/jgp.20028568
    • (2002) J. Gen. Physiol. , vol.120 , pp. 483-496
    • Sine, S.M.1    Shen, X.M.2    Wang, H.L.3    Ohno, K.4    Lee, W.Y.5    Tsujino, A.6
  • 115
    • 0035902187 scopus 로고    scopus 로고
    • A glia-derived acetylcholine-binding protein that modulates synaptic transmission
    • doi: 10.1038/35077000
    • Smit, A. B., Syed, N. I., Schaap, D., van Minnen, J., Klumperman, J., Kits, K. S., et al. (2001). A glia-derived acetylcholine-binding protein that modulates synaptic transmission. Nature 411, 261-268. doi: 10.1038/35077000
    • (2001) Nature , vol.411 , pp. 261-268
    • Smit, A.B.1    Syed, N.I.2    Schaap, D.3    van Minnen, J.4    Klumperman, J.5    Kits, K.S.6
  • 116
    • 0034102071 scopus 로고    scopus 로고
    • The role of tryptophan residues in the 5-Hydroxytryptamine(3) receptor ligand binding domain
    • doi: 10.1074/jbc.275.8.5620
    • Spier, A. D., and Lummis, S. C. (2000). The role of tryptophan residues in the 5-Hydroxytryptamine(3) receptor ligand binding domain. J. Biol. Chem. 275, 5620-5625. doi: 10.1074/jbc.275.8.5620
    • (2000) J. Biol. Chem. , vol.275 , pp. 5620-5625
    • Spier, A.D.1    Lummis, S.C.2
  • 117
    • 84868116573 scopus 로고    scopus 로고
    • Pentameric ligand-gated ion channel ELIC is activated by GABA and modulated by benzodiazepines
    • doi: 10.1073/pnas.1208208109
    • Spurny, R., Ramerstorfer, J., Price, K., Brams, M., Ernst, M., Nury, H., et al. (2012). Pentameric ligand-gated ion channel ELIC is activated by GABA and modulated by benzodiazepines. Proc. Natl. Acad. Sci. U.S.A. 109, E3028-E3034. doi: 10.1073/pnas.1208208109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Spurny, R.1    Ramerstorfer, J.2    Price, K.3    Brams, M.4    Ernst, M.5    Nury, H.6
  • 118
    • 84878698690 scopus 로고    scopus 로고
    • Assembly of a pi-pi stack of ligands in the binding site of an acetylcholine-binding protein
    • doi: 10.1038/ncomms2900
    • Stornaiuolo, M., De Kloe, G. E., Rucktooa, P., Fish, A., van Elk, R., Edink, E. S., et al. (2013). Assembly of a pi-pi stack of ligands in the binding site of an acetylcholine-binding protein. Nat. Commun. 4:1875. doi: 10.1038/ncomms2900
    • (2013) Nat. Commun. , vol.4 , pp. 1875
    • Stornaiuolo, M.1    De Kloe, G.E.2    Rucktooa, P.3    Fish, A.4    van Elk, R.5    Edink, E.S.6
  • 119
    • 0027276929 scopus 로고
    • Differential expression of human nicotinic acetylcholine receptor alpha subunit variants in muscle and non-muscle tissues
    • doi: 10.1093/nar/21.2.233
    • Talib, S., Okarma, T. B., and Lebkowski, J. S. (1993). Differential expression of human nicotinic acetylcholine receptor alpha subunit variants in muscle and non-muscle tissues. Nucleic Acids Res. 21, 233-237. doi: 10.1093/nar/21.2.233
    • (1993) Nucleic Acids Res. , vol.21 , pp. 233-237
    • Talib, S.1    Okarma, T.B.2    Lebkowski, J.S.3
  • 120
    • 44949241532 scopus 로고    scopus 로고
    • Atomic interactions of neonicotinoid agonists with AChBP: molecular recognition of the distinctive electronegative pharmacophore
    • doi: 10.1073/pnas.0802197105
    • Talley, T. T., Harel, M., Hibbs, R. E., Radic, Z., Tomizawa, M., Casida, J. E., et al. (2008). Atomic interactions of neonicotinoid agonists with AChBP: molecular recognition of the distinctive electronegative pharmacophore. Proc. Natl. Acad. Sci. U.S.A. 105, 7606-7611. doi: 10.1073/pnas.0802197105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7606-7611
    • Talley, T.T.1    Harel, M.2    Hibbs, R.E.3    Radic, Z.4    Tomizawa, M.5    Casida, J.E.6
  • 121
    • 33646822242 scopus 로고    scopus 로고
    • Spectroscopic analysis of benzylidene anabaseine complexes with acetylcholine binding proteins as models for ligand-nicotinic receptor interactions
    • doi: 10.1021/bi060534y
    • Talley, T. T., Yalda, S., Ho, K. Y., Tor, Y., Soti, F. S., Kem, W. R., et al. (2006). Spectroscopic analysis of benzylidene anabaseine complexes with acetylcholine binding proteins as models for ligand-nicotinic receptor interactions. Biochemistry 45, 8894-8902. doi: 10.1021/bi060534y
    • (2006) Biochemistry , vol.45 , pp. 8894-8902
    • Talley, T.T.1    Yalda, S.2    Ho, K.Y.3    Tor, Y.4    Soti, F.S.5    Kem, W.R.6
  • 122
  • 123
    • 33745224113 scopus 로고    scopus 로고
    • Mutagenesis and molecular modeling reveal the importance of the 5-HT3 receptor F-loop
    • doi: 10.1074/jbc.M601265200
    • Thompson, A. J., Padgett, C. L., and Lummis, S. C. R. (2006). Mutagenesis and molecular modeling reveal the importance of the 5-HT3 receptor F-loop. J. Biol. Chem. 281, 16576-16582. doi: 10.1074/jbc.M601265200
    • (2006) J. Biol. Chem. , vol.281 , pp. 16576-16582
    • Thompson, A.J.1    Padgett, C.L.2    Lummis, S.C.R.3
  • 124
    • 0026004411 scopus 로고
    • Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor
    • doi: 10.1016/S0006-3495(91)82102-6
    • Tomaselli, G. F., McLaughlin, J. T., Jurman, M. E., Hawrot, E., and Yellen, G. (1991). Mutations affecting agonist sensitivity of the nicotinic acetylcholine receptor. Biophys. J. 60, 721-727. doi: 10.1016/S0006-3495(91)82102-6
    • (1991) Biophys. J. , vol.60 , pp. 721-727
    • Tomaselli, G.F.1    McLaughlin, J.T.2    Jurman, M.E.3    Hawrot, E.4    Yellen, G.5
  • 125
    • 13844280231 scopus 로고    scopus 로고
    • Neonicotinoid insecticide toxicology: mechanisms of selective action
    • doi: 10.1146/annurev.pharmtox.45.120403.095930
    • Tomizawa, M., and Casida, J. E. (2005). Neonicotinoid insecticide toxicology: mechanisms of selective action. Annu. Rev. Pharmacol. Toxicol. 45, 247-268. doi: 10.1146/annurev.pharmtox.45.120403.095930
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 247-268
    • Tomizawa, M.1    Casida, J.E.2
  • 126
    • 0025732113 scopus 로고
    • Kinetic properties of the glycine receptor main- and sub-conductance states of mouse spinal cord neurones in culture
    • Twyman, R. E., and Macdonald, R. L. (1991). Kinetic properties of the glycine receptor main- and sub-conductance states of mouse spinal cord neurones in culture. J. Physiol. 435, 303-331.
    • (1991) J. Physiol. , vol.435 , pp. 303-331
    • Twyman, R.E.1    Macdonald, R.L.2
  • 127
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • doi: 10.1016/j.jmb.2004.12.031
    • Unwin, N. (2005). Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J. Mol. Biol. 346, 967-989. doi: 10.1016/j.jmb.2004.12.031
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 128
    • 0026787189 scopus 로고
    • Distinct agonist- and antagonist-binding sites on the glycine receptor
    • doi: 10.1016/0896-6273(92)90186-H
    • Vandenberg, R. J., Handford, C. A., and Schofield, P. R. (1992). Distinct agonist- and antagonist-binding sites on the glycine receptor. Neuron 9, 491-496. doi: 10.1016/0896-6273(92)90186-H
    • (1992) Neuron , vol.9 , pp. 491-496
    • Vandenberg, R.J.1    Handford, C.A.2    Schofield, P.R.3
  • 129
    • 0035141668 scopus 로고    scopus 로고
    • Structure and dynamics of the GABA binding pocket: a narrowing cleft that constricts during activation
    • Wagner, D. A., and Czajkowski, C. (2001). Structure and dynamics of the GABA binding pocket: a narrowing cleft that constricts during activation. J. Neurosci. 21, 67-74.
    • (2001) J. Neurosci. , vol.21 , pp. 67-74
    • Wagner, D.A.1    Czajkowski, C.2
  • 130
    • 0026610272 scopus 로고
    • A single histidine in GABAA receptors is essential for benzodiazepine agonist binding
    • Wieland, H. A., Luddens, H., and Seeburg, P. H. (1992). A single histidine in GABAA receptors is essential for benzodiazepine agonist binding. J. Biol. Chem. 267, 1426-1429.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1426-1429
    • Wieland, H.A.1    Luddens, H.2    Seeburg, P.H.3
  • 131
    • 67649873076 scopus 로고    scopus 로고
    • Differential regulation of receptor activation and agonist selectivity by highly conserved tryptophans in the nicotinic acetylcholine receptor binding site
    • doi: 10.1124/jpet.109.151225
    • Williams, D. K., Stokes, C., Horenstein, N. A., and Papke, R. L. (2009). Differential regulation of receptor activation and agonist selectivity by highly conserved tryptophans in the nicotinic acetylcholine receptor binding site. J. Pharmacol. Exp. Ther. 330, 40-53. doi: 10.1124/jpet.109.151225
    • (2009) J. Pharmacol. Exp. Ther. , vol.330 , pp. 40-53
    • Williams, D.K.1    Stokes, C.2    Horenstein, N.A.3    Papke, R.L.4
  • 132
    • 70049086953 scopus 로고    scopus 로고
    • The nicotinic acetylcholine receptors of the parasitic nematode Ascaris suum: formation of two distinct drug targets by varying the relative expression levels of two subunits
    • doi: 10.1371/journal.ppat.1000517
    • Williamson, S. M., Robertson, A. P., Brown, L., Williams, T., Woods, D. J., Martin, R. J., et al. (2009). The nicotinic acetylcholine receptors of the parasitic nematode Ascaris suum: formation of two distinct drug targets by varying the relative expression levels of two subunits. PLoS Pathog. 5:e1000517. doi: 10.1371/journal.ppat.1000517
    • (2009) PLoS Pathog. , vol.5
    • Williamson, S.M.1    Robertson, A.P.2    Brown, L.3    Williams, T.4    Woods, D.J.5    Martin, R.J.6
  • 133
    • 63649149427 scopus 로고    scopus 로고
    • Nicotine binding to brain receptors requires a strong cation-p interaction
    • doi: 10.1038/nature07768
    • Xiu, X., Puskar, N. L., Shanata, J. A., Lester, H. A., and Dougherty, D. A. (2009). Nicotine binding to brain receptors requires a strong cation-p interaction. Nature 458, 534-537. doi: 10.1038/nature07768
    • (2009) Nature , vol.458 , pp. 534-537
    • Xiu, X.1    Puskar, N.L.2    Shanata, J.A.3    Lester, H.A.4    Dougherty, D.A.5
  • 134
    • 39049132185 scopus 로고    scopus 로고
    • 'Inhibitory ligand-gated ion channels as substrates for general anesthetic actions'
    • eds J. Schüttler and H. Schwilden (Berlin; Heidelberg: Springer)
    • Zeller, A., Jurd, R., Lambert, S., Arras, M., Drexler, B., Grashoff, C., et al. (2008). "Inhibitory ligand-gated ion channels as substrates for general anesthetic actions," in Modern Anesthetics, eds J. Schüttler and H. Schwilden (Berlin; Heidelberg: Springer), 31-51.
    • (2008) Modern Anesthetics , pp. 31-51
    • Zeller, A.1    Jurd, R.2    Lambert, S.3    Arras, M.4    Drexler, B.5    Grashoff, C.6
  • 135
    • 0037127296 scopus 로고    scopus 로고
    • Identification of two novel Drosophila melanogaster histamine-gated chloride channel subunits expressed in the eye
    • doi: 10.1074/jbc.M107635200
    • Zheng, Y., Hirschberg, B., Yuan, J., Wang, A. P., Hunt, D. C., Ludmerer, S. W., et al. (2002). Identification of two novel Drosophila melanogaster histamine-gated chloride channel subunits expressed in the eye. J. Biol. Chem. 277, 2000-2005. doi: 10.1074/jbc.M107635200
    • (2002) J. Biol. Chem. , vol.277 , pp. 2000-2005
    • Zheng, Y.1    Hirschberg, B.2    Yuan, J.3    Wang, A.P.4    Hunt, D.C.5    Ludmerer, S.W.6
  • 136
    • 0032514762 scopus 로고    scopus 로고
    • From ab initio quantum mechanics to molecular neurobiology: a cation-p binding site in the nicotinic receptor
    • doi: 10.1073/pnas.95.21.12088
    • Zhong, W., Gallivan, J. P., Zhang, Y., Li, L., Lester, H. A., and Dougherty, D. A. (1998). From ab initio quantum mechanics to molecular neurobiology: a cation-p binding site in the nicotinic receptor. Proc. Natl. Acad. Sci. U.S.A. 95, 12088-12093. doi: 10.1073/pnas.95.21.12088
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12088-12093
    • Zhong, W.1    Gallivan, J.P.2    Zhang, Y.3    Li, L.4    Lester, H.A.5    Dougherty, D.A.6
  • 137
    • 79959775185 scopus 로고    scopus 로고
    • Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC
    • doi: 10.1371/journal.pbio.1001101
    • Zimmermann, I., and Dutzler, R. (2011). Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC. PLoS Biol. 9:e1001101. doi: 10.1371/journal.pbio.1001101
    • (2011) PLoS Biol. , vol.9
    • Zimmermann, I.1    Dutzler, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.