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Volumn 53, Issue 38, 2014, Pages 6041-6051

Agonist and antagonist binding in human glycine receptors

Author keywords

[No Author keywords available]

Indexed keywords

GLYCINE RECEPTOR;

EID: 84907462413     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500815f     Document Type: Article
Times cited : (35)

References (69)
  • 1
    • 0034973097 scopus 로고    scopus 로고
    • The glycinergic inhibitory response
    • Legendre, P. (2001) The glycinergic inhibitory response Cell. Mol. Life Sci. 58, 760-793
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 760-793
    • Legendre, P.1
  • 2
    • 4644265039 scopus 로고    scopus 로고
    • Molecular structure and function of the glycine receptor chloride channel
    • Lynch, J. W. (2004) Molecular structure and function of the glycine receptor chloride channel Physiol. Rev. 84, 1051-1095
    • (2004) Physiol. Rev. , vol.84 , pp. 1051-1095
    • Lynch, J.W.1
  • 3
    • 30944455443 scopus 로고    scopus 로고
    • Glycine receptors: A new therapeutic target in pain pathways
    • Lynch, J. and Callister, R. (2006) Glycine receptors: A new therapeutic target in pain pathways Curr. Opin. Invest. Drugs 7, 48-53
    • (2006) Curr. Opin. Invest. Drugs , vol.7 , pp. 48-53
    • Lynch, J.1    Callister, R.2
  • 5
    • 84892181483 scopus 로고    scopus 로고
    • The impact of human hyperekplexia mutations on glycine receptor structure and function
    • Bode, A. and Lynch, J. (2014) The impact of human hyperekplexia mutations on glycine receptor structure and function Mol. Brain 7, 2
    • (2014) Mol. Brain , vol.7 , pp. 2
    • Bode, A.1    Lynch, J.2
  • 6
    • 0001202076 scopus 로고
    • Conserved quaternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer
    • Langosch, D., Thomas, L., and Betz, H. (1988) Conserved quaternary structure of ligand-gated ion channels: The postsynaptic glycine receptor is a pentamer Proc. Natl. Acad. Sci. U.S.A. 85, 7394-7398
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7394-7398
    • Langosch, D.1    Thomas, L.2    Betz, H.3
  • 7
    • 0028840995 scopus 로고
    • Distribution patterns of mRNAs encoding glycine receptor channels in the developing rat spinal cord
    • Watanabe, E. and Akagi, H. (1995) Distribution patterns of mRNAs encoding glycine receptor channels in the developing rat spinal cord Neurosci. Res. 23, 377-382
    • (1995) Neurosci. Res. , vol.23 , pp. 377-382
    • Watanabe, E.1    Akagi, H.2
  • 8
    • 73549120879 scopus 로고    scopus 로고
    • What single-channel analysis tells us of the activation mechanism of ligand-gated channels: The case of the glycine receptor
    • Sivilotti, L. G. (2010) What single-channel analysis tells us of the activation mechanism of ligand-gated channels: The case of the glycine receptor J. Physiol. 588, 45-58
    • (2010) J. Physiol. , vol.588 , pp. 45-58
    • Sivilotti, L.G.1
  • 10
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. (1995) Acetylcholine receptor channel imaged in the open state Nature 373, 37-43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 11
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution
    • Unwin, N. (2005) Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution J. Mol. Biol. 346, 967-989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 14
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc, K., van Dijk, W. J., Klassen, R. V., Schuurmans, M., van Der Oost, J., Smit, A. B., and Sixma, T. K. (2001) Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors Nature 411, 269-276
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    Van Dijk, W.J.2    Klassen, R.V.3    Schuurmans, M.4    Van Der Oost, J.5    Smit, A.B.6    Sixma, T.K.7
  • 15
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • Celie, P. H., van Rossum-Fikkert, S. H., 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
    • (2004) Neuron , vol.41 , pp. 907-914
    • Celie, P.H.1    Van Rossum-Fikkert, S.H.2    Van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 16
    • 27144473613 scopus 로고    scopus 로고
    • Structures of the Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • Hansen, S. B., Sulzenbacher, G., Huxford, T., Marchot, P., Taylor, P., and Bourne, Y. (2005) Structures of the Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations EMBO J. 1-12
    • (2005) EMBO J. , pp. 1-12
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 17
    • 26944443142 scopus 로고    scopus 로고
    • Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels
    • Tasneem, A., Iyer, L., Jakobsson, E., and Aravind, L. (2005) Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels Genome Biol. 6, R4
    • (2005) Genome Biol. , vol.6 , pp. 4
    • Tasneem, A.1    Iyer, L.2    Jakobsson, E.3    Aravind, L.4
  • 18
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet, N., Nury, H., Baaden, M., Le Poupon, C., Changeux, J.-P., Delarue, M., and Corringer, P.-J. (2009) X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation Nature 457, 111-114
    • (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    Corringer, P.-J.7
  • 19
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf, R. J. C. and Dutzler, R. (2008) X-ray structure of a prokaryotic pentameric ligand-gated ion channel Nature 452, 375-379
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.C.1    Dutzler, R.2
  • 20
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • Hilf, R. J. C. and Dutzler, R. (2009) Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel Nature 457, 115-118
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.C.1    Dutzler, R.2
  • 21
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel
    • Bouzat, C., Gumilar, F., Spitzmaul, G., Wang, H. L., Rayes, D., Hansen, S. B., Taylor, P., and Sine, S. M. (2004) Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel Nature 430, 269-276
    • (2004) Nature , vol.430 , pp. 269-276
    • Bouzat, C.1    Gumilar, F.2    Spitzmaul, G.3    Wang, H.L.4    Rayes, D.5    Hansen, S.B.6    Taylor, P.7    Sine, S.M.8
  • 22
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • Hibbs, R. and Gouaux, E. (2011) Principles of activation and permeation in an anion-selective Cys-loop receptor Nature 474, 54-60
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.1    Gouaux, E.2
  • 23
    • 84881437750 scopus 로고    scopus 로고
    • Gating of pentameric ligand-gated ion channels: Structural insights and ambiguities
    • daCosta, C. J. B. and Baenziger, J. E. (2013) Gating of pentameric ligand-gated ion channels: Structural insights and ambiguities Structure 21, 1271-1283
    • (2013) Structure , vol.21 , pp. 1271-1283
    • Dacosta, C.J.B.1    Baenziger, J.E.2
  • 24
    • 10044248233 scopus 로고    scopus 로고
    • Single-channel behavior of heteromeric α1β glycine receptors: An attempt to detect a conformational change before the channel opens
    • Burzomato, V., Beato, M., Groot-Kormelink, P. J., Colquhoun, D., and Sivilotti, L. G. (2004) Single-channel behavior of heteromeric α1β glycine receptors: An attempt to detect a conformational change before the channel opens J. Neurosci. 24, 10924-10940
    • (2004) J. Neurosci. , vol.24 , pp. 10924-10940
    • Burzomato, V.1    Beato, M.2    Groot-Kormelink, P.J.3    Colquhoun, D.4    Sivilotti, L.G.5
  • 25
    • 79951621335 scopus 로고    scopus 로고
    • The long activations of α2 glycine channels can be described by a mechanism with reaction intermediates ("flip")
    • Krashia, P., Lape, R., Lodesani, F., Colquhoun, D., and Sivilotti, L. G. (2011) The long activations of α2 glycine channels can be described by a mechanism with reaction intermediates ("flip") J. Gen. Physiol. 137, 197-216
    • (2011) J. Gen. Physiol. , vol.137 , pp. 197-216
    • Krashia, P.1    Lape, R.2    Lodesani, F.3    Colquhoun, D.4    Sivilotti, L.G.5
  • 26
    • 49649102025 scopus 로고    scopus 로고
    • On the nature of partial agonism in the nicotinic receptor superfamily
    • Lape, R., Colquhoun, D., and Sivilotti, L. G. (2008) On the nature of partial agonism in the nicotinic receptor superfamily Nature 454, 722-727
    • (2008) Nature , vol.454 , pp. 722-727
    • Lape, R.1    Colquhoun, D.2    Sivilotti, L.G.3
  • 27
    • 67349279395 scopus 로고    scopus 로고
    • Detection and trapping of intermediate states priming nicotinic receptor channel opening
    • Mukhtasimova, N., Lee, W. Y., Wang, H.-L., and Sine, S. M. (2009) Detection and trapping of intermediate states priming nicotinic receptor channel opening Nature 459, 451-454
    • (2009) Nature , vol.459 , pp. 451-454
    • Mukhtasimova, N.1    Lee, W.Y.2    Wang, H.-L.3    Sine, S.M.4
  • 28
    • 79953658296 scopus 로고    scopus 로고
    • Blockade of neuronal α7-nAChR by α-conotoxin ImI explained by computational scanning and energy calculations
    • Yu, R., Craik, D. J., and Kaas, Q. (2011) Blockade of neuronal α7-nAChR by α-conotoxin ImI explained by computational scanning and energy calculations PLoS Comput. Biol. 7, e1002011
    • (2011) PLoS Comput. Biol. , vol.7 , pp. 1002011
    • Yu, R.1    Craik, D.J.2    Kaas, Q.3
  • 29
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE: A multiple sequence alignment method with reduced time and space complexity
    • Edgar, R. C. (2004) MUSCLE: A multiple sequence alignment method with reduced time and space complexity BMC Bioinf. 5, 113
    • (2004) BMC Bioinf. , vol.5 , pp. 113
    • Edgar, R.C.1
  • 30
    • 80053635399 scopus 로고    scopus 로고
    • Chloride ions in the pore of Gly and GABA channels shape the time course and voltage dependence of agonist currents
    • Moroni, M., Biro, I., Giugliano, M., Vijayan, R., Biggin, P. C., Beato, M., and Svililotti, L. (2011) Chloride ions in the pore of Gly and GABA channels shape the time course and voltage dependence of agonist currents J. Neurosci. 31, 14095-14106
    • (2011) J. Neurosci. , vol.31 , pp. 14095-14106
    • Moroni, M.1    Biro, I.2    Giugliano, M.3    Vijayan, R.4    Biggin, P.C.5    Beato, M.6    Svililotti, L.7
  • 32
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen, M.-Y. and Sali, A. (2006) Statistical potential for assessment and prediction of protein structures Protein Sci. 15, 2507-2524
    • (2006) Protein Sci. , vol.15 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2
  • 34
    • 79953684899 scopus 로고    scopus 로고
    • A structural and mutagenic blueprint for molecular recognition of strychnine and d -tubocurarine by different cys-loop receptors
    • Brams, M., Pandya, A., Kuzmin, D., van Elk, R., Krijnen, L., Yakel, J. L., Tsetlin, V., Smit, A. B., and Ulens, C. (2011) A structural and mutagenic blueprint for molecular recognition of strychnine and d -tubocurarine by different cys-loop receptors PLoS Biol. 9, e1001034
    • (2011) PLoS Biol. , vol.9 , pp. 1001034
    • Brams, M.1    Pandya, A.2    Kuzmin, D.3    Van Elk, R.4    Krijnen, L.5    Yakel, J.L.6    Tsetlin, V.7    Smit, A.B.8    Ulens, C.9
  • 37
    • 33645858780 scopus 로고
    • Transferable intermolecular potential functions for water, alcohols, and ethers, application to liquid water
    • Jorgensen, W. L. (1981) Transferable intermolecular potential functions for water, alcohols, and ethers, application to liquid water J. Am. Chem. Soc. 103, 335-340
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 335-340
    • Jorgensen, W.L.1
  • 39
  • 40
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 41
    • 14644414132 scopus 로고    scopus 로고
    • The β subunit determines the ligand binding properties of synaptic glycine receptors
    • Grudzinska, J., Schemm, R., Haeger, S., Nicke, A., Schmalzing, G., Betz, H., and Laube, B. (2005) The β subunit determines the ligand binding properties of synaptic glycine receptors Neuron 45, 727-739
    • (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    Laube, B.7
  • 42
    • 79953018004 scopus 로고    scopus 로고
    • A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists
    • Pless, S. A., Hanek, A. P., Price, K. L., Lynch, J. W., Lester, H. A., Dougherty, D. A., and Lummis, S. C. R. (2011) A cation-π interaction at a phenylalanine residue in the glycine receptor binding site is conserved for different agonists Mol. Pharmacol. 79, 742-748
    • (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    Lummis, S.C.R.7
  • 43
    • 0032692626 scopus 로고    scopus 로고
    • Identification of a new ligand binding domain in the α1 subunit of the inhibitory glycine receptor
    • Vafa, B., Lewis, T. M., Cunningham, A. M., Jacques, P., Lynch, J. W., and Schofield, P. R. (1999) Identification of a new ligand binding domain in the α1 subunit of the inhibitory glycine receptor J. Neurochem. 73, 2158-2166
    • (1999) J. Neurochem. , vol.73 , pp. 2158-2166
    • Vafa, B.1    Lewis, T.M.2    Cunningham, A.M.3    Jacques, P.4    Lynch, J.W.5    Schofield, P.R.6
  • 44
    • 0026787189 scopus 로고
    • Distinct agonist- and antagonist-binding sites on the glycine receptor
    • 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
    • (1992) Neuron , vol.9 , pp. 491-496
    • Vandenberg, R.J.1    Handford, C.A.2    Schofield, P.R.3
  • 45
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun, D. (1998) Binding, gating, affinity and efficacy: The interpretation of structure-activity relationships for agonists and of the effects of mutating receptors Br. J. Pharmacol. 125, 923-947
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 923-947
    • Colquhoun, D.1
  • 46
    • 0037196236 scopus 로고    scopus 로고
    • Achieving optimal expression for single channel recording: A plasmid ratio approach to the expression of α1 glycine receptors in HEK293 cells
    • Groot-Kormelink, P. J., Beato, M., Finotti, C., Harvey, R. J., and Sivilotti, L. G. (2002) Achieving optimal expression for single channel recording: A plasmid ratio approach to the expression of α1 glycine receptors in HEK293 cells J. Neurosci. Methods 113, 207-214
    • (2002) J. Neurosci. Methods , vol.113 , pp. 207-214
    • Groot-Kormelink, P.J.1    Beato, M.2    Finotti, C.3    Harvey, R.J.4    Sivilotti, L.G.5
  • 47
    • 58149264819 scopus 로고    scopus 로고
    • High intracellular chloride slows the decay of glycinergic currents
    • Pitt, S. J., Sivilotti, L. G., and Beato, M. (2008) High intracellular chloride slows the decay of glycinergic currents J. Neurosci. 28, 11454-11467
    • (2008) J. Neurosci. , vol.28 , pp. 11454-11467
    • Pitt, S.J.1    Sivilotti, L.G.2    Beato, M.3
  • 48
    • 0019185036 scopus 로고
    • A receptor for protons in the nerve cell membrane
    • Krishtal, O. A. and Pidoplichko, V. I. (1980) A receptor for protons in the nerve cell membrane Neuroscience 5, 2325-2327
    • (1980) Neuroscience , vol.5 , pp. 2325-2327
    • Krishtal, O.A.1    Pidoplichko, V.I.2
  • 49
    • 0036154304 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2
    • Arinaminpathy, Y., Sansom, M. S. P., and Biggin, P. C. (2002) Molecular dynamics simulations of the ligand-binding domain of the ionotropic glutamate receptor GluR2 Biophys. J. 82, 676-683
    • (2002) Biophys. J. , vol.82 , pp. 676-683
    • Arinaminpathy, Y.1    Sansom, M.S.P.2    Biggin, P.C.3
  • 50
    • 84885728224 scopus 로고    scopus 로고
    • Using molecular dynamics to elucidate the structural basis for function in pLGICs
    • Akabas, M. H. (2013) Using molecular dynamics to elucidate the structural basis for function in pLGICs Proc. Natl. Acad. Sci. U.S.A. 110, 16700-16701
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 16700-16701
    • Akabas, M.H.1
  • 53
    • 84870013769 scopus 로고    scopus 로고
    • Energetics and ion permeation characteristics in a glutamate-gated chloride (GluCl) receptor channel
    • Cheng, M. H. and Coalson, R. D. (2012) Energetics and ion permeation characteristics in a glutamate-gated chloride (GluCl) receptor channel J. Phys. Chem. B 116, 13637-13643
    • (2012) J. Phys. Chem. B , vol.116 , pp. 13637-13643
    • Cheng, M.H.1    Coalson, R.D.2
  • 54
    • 84881394637 scopus 로고    scopus 로고
    • Stabilization of the GluCl ligand-gated ion channel in the presence and absence of ivermectin
    • Yoluk, O., Bromstrup, T., Bertaccini, E. J., Trudell, J. R., and Lindahl, E. (2013) Stabilization of the GluCl ligand-gated ion channel in the presence and absence of ivermectin Biophys. J. 105, 640-647
    • (2013) Biophys. J. , vol.105 , pp. 640-647
    • Yoluk, O.1    Bromstrup, T.2    Bertaccini, E.J.3    Trudell, J.R.4    Lindahl, E.5
  • 55
    • 79959652664 scopus 로고    scopus 로고
    • Microsecond simulations indicate that ethanol binds between subunits and could stabilize an open-state model of a glycine receptor
    • Murail, S., Wallner, B., Trudell, J. R., Bertaccini, E., and Lindahl, E. (2011) Microsecond simulations indicate that ethanol binds between subunits and could stabilize an open-state model of a glycine receptor Biophys. J. 100, 1642-1650
    • (2011) Biophys. J. , vol.100 , pp. 1642-1650
    • Murail, S.1    Wallner, B.2    Trudell, J.R.3    Bertaccini, E.4    Lindahl, E.5
  • 56
  • 58
    • 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. R., 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.R.6    Dougherty, D.A.7
  • 60
    • 34247187356 scopus 로고    scopus 로고
    • Analysis of ligand-bound water molecules in high resolution crystal structures of protein-ligand complexes
    • Lu, Y., Wang, R., Yang, C.-Y., and Wang, S. (2007) Analysis of ligand-bound water molecules in high resolution crystal structures of protein-ligand complexes J. Chem. Inf. Model. 47, 668-675
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 668-675
    • Lu, Y.1    Wang, R.2    Yang, C.-Y.3    Wang, S.4
  • 61
    • 84857748866 scopus 로고    scopus 로고
    • Rapid and Accurate Prediction and Scoring of Water Molecules in Protein Binding Sites
    • Ross, G. A., Morris, G. M., and Biggin, P. C. (2012) Rapid and Accurate Prediction and Scoring of Water Molecules in Protein Binding Sites PLoS One 7, e32036
    • (2012) PLoS One , vol.7 , pp. 32036
    • Ross, G.A.1    Morris, G.M.2    Biggin, P.C.3
  • 64
    • 80054695668 scopus 로고    scopus 로고
    • Isoflurane alters the structure and dynamics of GLIC
    • Willenbring, D., Liu, Lu. T., Mowrey, D., Xu, Y., and Tang, P. (2011) Isoflurane alters the structure and dynamics of GLIC Biophys. J. 101, 1905-1912
    • (2011) Biophys. J. , vol.101 , pp. 1905-1912
    • Willenbring, D.1    Liu Lu., T.2    Mowrey, D.3    Xu, Y.4    Tang, P.5
  • 65
    • 84864007947 scopus 로고    scopus 로고
    • Molecular mechanisms of Cys-loop ion channel receptor modulation by ivermectin
    • Lynagh, T. and Lynch, J. (2012) Molecular mechanisms of Cys-loop ion channel receptor modulation by ivermectin Front. Mol. Neurosci. 5, 60
    • (2012) Front. Mol. Neurosci. , vol.5 , pp. 60
    • Lynagh, T.1    Lynch, J.2
  • 66
    • 0036830645 scopus 로고    scopus 로고
    • Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism
    • Chang, Y. and Weiss, D. S. (2002) Site-specific fluorescence reveals distinct structural changes with GABA receptor activation and antagonism Nat. Neurosci. 5, 1163-1168
    • (2002) Nat. Neurosci. , vol.5 , pp. 1163-1168
    • Chang, Y.1    Weiss, D.S.2
  • 67
    • 67650169910 scopus 로고    scopus 로고
    • Ligand-specific conformational changes in the α1 glycine receptor ligand-binding domain
    • Pless, S. A. and Lynch, J. W. (2009) Ligand-specific conformational changes in the α1 glycine receptor ligand-binding domain J. Biol. Chem. 284, 15847-15856
    • (2009) J. Biol. Chem. , vol.284 , pp. 15847-15856
    • Pless, S.A.1    Lynch, J.W.2
  • 68
    • 84874774558 scopus 로고    scopus 로고
    • Fluorescence-based high-throughput functional profiling of ligand-gated ion channels at the level of single cells
    • Talwar, S., Lynch, J. W., and Gilbert, D. F. (2013) Fluorescence-based high-throughput functional profiling of ligand-gated ion channels at the level of single cells PLoS One 8, e58479
    • (2013) PLoS One , vol.8 , pp. 58479
    • Talwar, S.1    Lynch, J.W.2    Gilbert, D.F.3
  • 69
    • 84885435090 scopus 로고    scopus 로고
    • Open-Channel Structures of the Human Glycine Receptor α1 Full-Length Transmembrane Domain
    • Mowrey, D. D., Cui, T., Jia, Y., Ma, D., Makhov, A. M., Zhang, P., Tang, P., and Xu, Y. (2013) Open-Channel Structures of the Human Glycine Receptor α1 Full-Length Transmembrane Domain Structure 21, 1897-1904
    • (2013) Structure , vol.21 , pp. 1897-1904
    • Mowrey, D.D.1    Cui, T.2    Jia, Y.3    Ma, D.4    Makhov, A.M.5    Zhang, P.6    Tang, P.7    Xu, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.