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Volumn 593, Issue 1, 2015, Pages 97-110

Retour aux sources: Defining the structural basis of glutamate receptor activation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RECEPTOR STIMULATING AGENT; GLUTAMATE RECEPTOR;

EID: 84920125558     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2014.277921     Document Type: Article
Times cited : (13)

References (136)
  • 1
    • 0024464164 scopus 로고
    • Bacterial periplasmic binding protein tertiary structures
    • Adams MD & Oxender DL (1989). Bacterial periplasmic binding protein tertiary structures. J Biol Chem 264, 15739-15742.
    • (1989) J Biol Chem , vol.264 , pp. 15739-15742
    • Adams, M.D.1    Oxender, D.L.2
  • 2
    • 84920135930 scopus 로고
    • Concentration clamp technique
    • In, ed. Boulton A, Baker G & Walz W . Humana Press Inc.
    • Akaike N (1995). Concentration clamp technique. In Neuromethods, Patch-Clamp Applications and Protocols, ed. Boulton A, Baker G & Walz W, pp. 141-154. Humana Press Inc.
    • (1995) Neuromethods, Patch-Clamp Applications and Protocols , pp. 141-154
    • Akaike, N.1
  • 3
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core
    • Armstrong N & Gouaux E (2000). Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28, 165-181.
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 4
    • 33749059766 scopus 로고    scopus 로고
    • Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor
    • Armstrong N, Jasti J, Beich-Frandsen M & Gouaux E (2006). Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Cell 127, 85-97.
    • (2006) Cell , vol.127 , pp. 85-97
    • Armstrong, N.1    Jasti, J.2    Beich-Frandsen, M.3    Gouaux, E.4
  • 5
    • 0038625032 scopus 로고    scopus 로고
    • Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes
    • Armstrong N, Mayer M & Gouaux E (2003). Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes. Proc Natl Acad Sci U S A 100, 5736-5741.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5736-5741
    • Armstrong, N.1    Mayer, M.2    Gouaux, E.3
  • 6
    • 0032578635 scopus 로고    scopus 로고
    • Structure of a glutamate-receptor ligand-binding core in complex with kainate
    • Armstrong N, Sun Y, Chen GQ & Gouaux E (1998). Structure of a glutamate-receptor ligand-binding core in complex with kainate. Nature 395, 913-917.
    • (1998) Nature , vol.395 , pp. 913-917
    • Armstrong, N.1    Sun, Y.2    Chen, G.Q.3    Gouaux, E.4
  • 7
    • 0023948387 scopus 로고
    • Quisqualate- and kainate-activated channels in mouse central neurones in culture
    • Ascher P & Nowak L (1988). Quisqualate- and kainate-activated channels in mouse central neurones in culture. J Physiol 399, 227-245.
    • (1988) J Physiol , vol.399 , pp. 227-245
    • Ascher, P.1    Nowak, L.2
  • 9
    • 75349094219 scopus 로고    scopus 로고
    • Enhanced efficacy without further cleft closure: reevaluating twist as a source of agonist efficacy in AMPA receptors
    • Birdsey-Benson A, Gill A, Henderson LP & Madden DR (2010). Enhanced efficacy without further cleft closure: reevaluating twist as a source of agonist efficacy in AMPA receptors. J Neurosci 30, 1463-1470.
    • (2010) J Neurosci , vol.30 , pp. 1463-1470
    • Birdsey-Benson, A.1    Gill, A.2    Henderson, L.P.3    Madden, D.R.4
  • 10
    • 80055033154 scopus 로고    scopus 로고
    • NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers
    • Borschel WF, Murthy SE, Kasperek EM & Popescu GK (2011). NMDA receptor activation requires remodelling of intersubunit contacts within ligand-binding heterodimers. Nat Commun 2, 498.
    • (2011) Nat Commun , vol.2 , pp. 498
    • Borschel, W.F.1    Murthy, S.E.2    Kasperek, E.M.3    Popescu, G.K.4
  • 11
    • 0037088834 scopus 로고    scopus 로고
    • External anions and cations distinguish between AMPA and kainate receptor gating mechanisms
    • Bowie D (2002). External anions and cations distinguish between AMPA and kainate receptor gating mechanisms. J Physiol 539, 725-733.
    • (2002) J Physiol , vol.539 , pp. 725-733
    • Bowie, D.1
  • 12
    • 48849113877 scopus 로고    scopus 로고
    • Ionotropic glutamate receptors and CNS disorders
    • Bowie D (2008). Ionotropic glutamate receptors and CNS disorders. CNS Neurol Disord Drug Targets 7, 129-143.
    • (2008) CNS Neurol Disord Drug Targets , vol.7 , pp. 129-143
    • Bowie, D.1
  • 13
    • 73549084285 scopus 로고    scopus 로고
    • Ion-dependent gating of kainate receptors
    • Bowie D (2010). Ion-dependent gating of kainate receptors. J Physiol 588, 67-81.
    • (2010) J Physiol , vol.588 , pp. 67-81
    • Bowie, D.1
  • 14
    • 0037337142 scopus 로고    scopus 로고
    • Allosteric regulation and spatial distribution of kainate receptors bound to ancillary proteins
    • Bowie D, Garcia EP, Marshall J, Traynelis SF & Lange GD (2003). Allosteric regulation and spatial distribution of kainate receptors bound to ancillary proteins. J Physiol 547, 373-385.
    • (2003) J Physiol , vol.547 , pp. 373-385
    • Bowie, D.1    Garcia, E.P.2    Marshall, J.3    Traynelis, S.F.4    Lange, G.D.5
  • 15
    • 0036582716 scopus 로고    scopus 로고
    • Functional stoichiometry of glutamate receptor desensitization
    • Bowie D & Lange GD (2002). Functional stoichiometry of glutamate receptor desensitization. J Neurosci 22, 3392-3403.
    • (2002) J Neurosci , vol.22 , pp. 3392-3403
    • Bowie, D.1    Lange, G.D.2
  • 16
    • 0032531676 scopus 로고    scopus 로고
    • Activity-dependent modulation of glutamate receptors by polyamines
    • Bowie D, Lange GD & Mayer ML (1998). Activity-dependent modulation of glutamate receptors by polyamines. J Neurosci 18, 8175-8185.
    • (1998) J Neurosci , vol.18 , pp. 8175-8185
    • Bowie, D.1    Lange, G.D.2    Mayer, M.L.3
  • 17
    • 0031471216 scopus 로고    scopus 로고
    • Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen
    • Chen GQ & Gouaux E (1997). Overexpression of a glutamate receptor (GluR2) ligand binding domain in Escherichia coli: application of a novel protein folding screen. Proc Natl Acad Sci U S A 94, 13431-13436.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13431-13436
    • Chen, G.Q.1    Gouaux, E.2
  • 18
    • 84907261039 scopus 로고    scopus 로고
    • X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism
    • Chen L, Dürr KL & Gouaux E (2014). X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism. Science 345, 1021-1026.
    • (2014) Science , vol.345 , pp. 1021-1026
    • Chen, L.1    Dürr, K.L.2    Gouaux, E.3
  • 19
    • 0024829451 scopus 로고
    • Excitatory amino acid receptors in the vertebrate central nervous system
    • Collingridge GL & Lester RA (1989). Excitatory amino acid receptors in the vertebrate central nervous system. Pharmacol Rev 41, 143-210.
    • (1989) Pharmacol Rev , vol.41 , pp. 143-210
    • Collingridge, G.L.1    Lester, R.A.2
  • 21
    • 79952245139 scopus 로고    scopus 로고
    • Kainate receptors coming of age: milestones of two decades of research
    • Contractor A, Mulle C & Swanson GT (2011). Kainate receptors coming of age: milestones of two decades of research. Trends Neurosci 34, 154-163.
    • (2011) Trends Neurosci , vol.34 , pp. 154-163
    • Contractor, A.1    Mulle, C.2    Swanson, G.T.3
  • 22
    • 0023157215 scopus 로고
    • Multiple-conductance channels activated by excitatory amino acids in cerebellar neurons
    • Cull-Candy SG & Usowicz MM (1987). Multiple-conductance channels activated by excitatory amino acids in cerebellar neurons. Nature 325, 525-528.
    • (1987) Nature , vol.325 , pp. 525-528
    • Cull-Candy, S.G.1    Usowicz, M.M.2
  • 23
    • 0024327295 scopus 로고
    • On the multiple-conductance single channels activated by excitatory amino acids in large cerebellar neurones of the rat
    • Cull-Candy SG & Usowicz MM (1989). On the multiple-conductance single channels activated by excitatory amino acids in large cerebellar neurones of the rat. J Physiol 415, 555-582.
    • (1989) J Physiol , vol.415 , pp. 555-582
    • Cull-Candy, S.G.1    Usowicz, M.M.2
  • 24
    • 84881617618 scopus 로고    scopus 로고
    • Crosslinking the ligand-binding domain dimer interface locks kainate receptors out of the main open state
    • Daniels BA, Andrews ED, Aurousseau MR, Accardi MV & Bowie D (2013). Crosslinking the ligand-binding domain dimer interface locks kainate receptors out of the main open state. J Physiol 591, 3873-3885.
    • (2013) J Physiol , vol.591 , pp. 3873-3885
    • Daniels, B.A.1    Andrews, E.D.2    Aurousseau, M.R.3    Accardi, M.V.4    Bowie, D.5
  • 27
    • 79959268661 scopus 로고    scopus 로고
    • Atomistic mechanism for the activation and desensitization of an AMPA-subtype glutamate receptor
    • Dong H & Zhou HX (2011). Atomistic mechanism for the activation and desensitization of an AMPA-subtype glutamate receptor. Nat Commun 2, 354.
    • (2011) Nat Commun , vol.2 , pp. 354
    • Dong, H.1    Zhou, H.X.2
  • 29
    • 0025765017 scopus 로고
    • Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA
    • Egebjerg J, Bettler B, Hermans-Borgmeyer I & Heinemann S (1991). Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA. Nature 351, 745-748.
    • (1991) Nature , vol.351 , pp. 745-748
    • Egebjerg, J.1    Bettler, B.2    Hermans-Borgmeyer, I.3    Heinemann, S.4
  • 30
    • 66049109006 scopus 로고    scopus 로고
    • Functional characterization and in silico docking of full and partial GluK2 kainate receptor agonists
    • Fay AM, Corbeil CR, Brown P, Moitessier N & Bowie D (2009). Functional characterization and in silico docking of full and partial GluK2 kainate receptor agonists. Mol Pharmacol 75, 1096-1107.
    • (2009) Mol Pharmacol , vol.75 , pp. 1096-1107
    • Fay, A.M.1    Corbeil, C.R.2    Brown, P.3    Moitessier, N.4    Bowie, D.5
  • 31
    • 42249101227 scopus 로고    scopus 로고
    • NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists
    • Fenwick MK & Oswald RE (2008). NMR spectroscopy of the ligand-binding core of ionotropic glutamate receptor 2 bound to 5-substituted willardiine partial agonists. J Mol Biol 378, 673-685.
    • (2008) J Mol Biol , vol.378 , pp. 673-685
    • Fenwick, M.K.1    Oswald, R.E.2
  • 32
    • 0037442510 scopus 로고    scopus 로고
    • Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization
    • Fleck MW, Cornell E & Mah SJ (2003). Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization. J Neurosci 23, 1219-1227.
    • (2003) J Neurosci , vol.23 , pp. 1219-1227
    • Fleck, M.W.1    Cornell, E.2    Mah, S.J.3
  • 33
    • 67649771372 scopus 로고    scopus 로고
    • Full domain closure of the ligand-binding core of the ionotropic glutamate receptor iGluR5 induced by the high affinity agonist dysiherbaine and the functional antagonist 8,9-dideoxyneodysiherbaine
    • Frydenvang K, Lash LL, Naur P, Postila PA, Pickering DS, Smith CM, Gajhede M, Sasaki M, Sakai R, Pentikainen OT, Swanson GT & Kastrup JS (2009). Full domain closure of the ligand-binding core of the ionotropic glutamate receptor iGluR5 induced by the high affinity agonist dysiherbaine and the functional antagonist 8, 9-dideoxyneodysiherbaine. J Biol Chem 284, 14219-14229.
    • (2009) J Biol Chem , vol.284 , pp. 14219-14229
    • Frydenvang, K.1    Lash, L.L.2    Naur, P.3    Postila, P.A.4    Pickering, D.S.5    Smith, C.M.6    Gajhede, M.7    Sasaki, M.8    Sakai, R.9    Pentikainen, O.T.10    Swanson, G.T.11    Kastrup, J.S.12
  • 34
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa H & Gouaux E (2003). Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J 22, 2873-2885.
    • (2003) EMBO J , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 35
    • 0034988272 scopus 로고    scopus 로고
    • Pharmacological effects of AMPA receptor potentiators LY392098 and LY404187 on rat neuronal AMPA receptors in vitro
    • Gates M, Ogden A & Bleakman D (2001). Pharmacological effects of AMPA receptor potentiators LY392098 and LY404187 on rat neuronal AMPA receptors in vitro. Neuropharmacology 40, 984-991.
    • (2001) Neuropharmacology , vol.40 , pp. 984-991
    • Gates, M.1    Ogden, A.2    Bleakman, D.3
  • 36
    • 0442279279 scopus 로고    scopus 로고
    • Structure and function of AMPA receptors
    • Gouaux E (2004). Structure and function of AMPA receptors. J Physiol 554, 249-253.
    • (2004) J Physiol , vol.554 , pp. 249-253
    • Gouaux, E.1
  • 37
    • 0036968894 scopus 로고    scopus 로고
    • Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core
    • Hogner A, Kastrup JS, Jin R, Liljefors T, Mayer ML, Egebjerg J, Larsen IK & Gouaux E (2002). Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core. J Mol Biol 322, 93-109.
    • (2002) J Mol Biol , vol.322 , pp. 93-109
    • Hogner, A.1    Kastrup, J.S.2    Jin, R.3    Liljefors, T.4    Mayer, M.L.5    Egebjerg, J.6    Larsen, I.K.7    Gouaux, E.8
  • 39
    • 0028596211 scopus 로고
    • N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1
    • Hollmann M, Maron C & Heinemann S (1994). N-glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1. Neuron 13, 1331-1343.
    • (1994) Neuron , vol.13 , pp. 1331-1343
    • Hollmann, M.1    Maron, C.2    Heinemann, S.3
  • 40
    • 0024367836 scopus 로고
    • Cloning by functional expression of a member of the glutamate receptor family
    • Hollmann M, O'Shea-Greenfield A, Rogers SW & Heinemann S (1989). Cloning by functional expression of a member of the glutamate receptor family. Nature 342, 643-648.
    • (1989) Nature , vol.342 , pp. 643-648
    • Hollmann, M.1    O'Shea-Greenfield, A.2    Rogers, S.W.3    Heinemann, S.4
  • 41
    • 27444434374 scopus 로고    scopus 로고
    • A binding site tyrosine shapes desensitization kinetics and agonist potency at GluR2. A mutagenic, kinetic, and crystallographic study
    • Holm MM, Naur P, Vestergaard B, Geballe MT, Gajhede M, Kastrup JS, Traynelis SF & Egebjerg J (2005). A binding site tyrosine shapes desensitization kinetics and agonist potency at GluR2. A mutagenic, kinetic, and crystallographic study. J Biol Chem 280, 35469-35476.
    • (2005) J Biol Chem , vol.280 , pp. 35469-35476
    • Holm, M.M.1    Naur, P.2    Vestergaard, B.3    Geballe, M.T.4    Gajhede, M.5    Kastrup, J.S.6    Traynelis, S.F.7    Egebjerg, J.8
  • 42
    • 1242293631 scopus 로고    scopus 로고
    • Regulation of AMPA receptor gating by ligand binding core dimers
    • Horning MS & Mayer ML (2004). Regulation of AMPA receptor gating by ligand binding core dimers. Neuron 41, 379-388.
    • (2004) Neuron , vol.41 , pp. 379-388
    • Horning, M.S.1    Mayer, M.L.2
  • 43
    • 0030595368 scopus 로고    scopus 로고
    • The crystal structure of glutamine-binding protein from Escherichia coli
    • Hsiao CD, Sun YJ, Rose J & Wang BC (1996). The crystal structure of glutamine-binding protein from Escherichia coli. J Mol Biol 262, 225-242.
    • (1996) J Mol Biol , vol.262 , pp. 225-242
    • Hsiao, C.D.1    Sun, Y.J.2    Rose, J.3    Wang, B.C.4
  • 44
    • 0025040913 scopus 로고
    • Glutamate receptor channels in rat DRG neurons: activation by kainate and quisqualate and blockade of desensitization by Con A
    • Huettner JE (1990). Glutamate receptor channels in rat DRG neurons: activation by kainate and quisqualate and blockade of desensitization by Con A. Neuron 5, 255-266.
    • (1990) Neuron , vol.5 , pp. 255-266
    • Huettner, J.E.1
  • 45
    • 0141540782 scopus 로고    scopus 로고
    • Kainate receptors and synaptic transmission
    • Huettner JE (2003). Kainate receptors and synaptic transmission. Prog Neurobiol 70, 387-407.
    • (2003) Prog Neurobiol , vol.70 , pp. 387-407
    • Huettner, J.E.1
  • 46
    • 84920157296 scopus 로고    scopus 로고
    • Glutamate receptor pores
    • Huettner JE (2014). Glutamate receptor pores. J Physiol (in press; DOI: 10.1113/jphysiol.2014.272724).
    • (2014) J Physiol
    • Huettner, J.E.1
  • 47
    • 20444408992 scopus 로고    scopus 로고
    • Mechanism of partial agonist action at the NR1 subunit of NMDA receptors
    • Inanobe A, Furukawa H & Gouaux E (2005). Mechanism of partial agonist action at the NR1 subunit of NMDA receptors. Neuron 47, 71-84.
    • (2005) Neuron , vol.47 , pp. 71-84
    • Inanobe, A.1    Furukawa, H.2    Gouaux, E.3
  • 48
    • 79955089674 scopus 로고    scopus 로고
    • The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits
    • Jackson AC & Nicoll RA (2011). The expanding social network of ionotropic glutamate receptors: TARPs and other transmembrane auxiliary subunits. Neuron 70, 178-199.
    • (2011) Neuron , vol.70 , pp. 178-199
    • Jackson, A.C.1    Nicoll, R.A.2
  • 49
    • 0023145892 scopus 로고
    • Glutamate activates multiple single channel conductances in hippocampal neurons
    • Jahr CE & Stevens CF (1987). Glutamate activates multiple single channel conductances in hippocampal neurons. Nature 325, 522-525.
    • (1987) Nature , vol.325 , pp. 522-525
    • Jahr, C.E.1    Stevens, C.F.2
  • 50
    • 0043033172 scopus 로고    scopus 로고
    • Structural basis for partial agonist action at ionotropic glutamate receptors
    • Jin R, Banke TG, Mayer ML, Traynelis SF & Gouaux E (2003). Structural basis for partial agonist action at ionotropic glutamate receptors. Nat Neurosci 6, 803-810.
    • (2003) Nat Neurosci , vol.6 , pp. 803-810
    • Jin, R.1    Banke, T.G.2    Mayer, M.L.3    Traynelis, S.F.4    Gouaux, E.5
  • 51
    • 0037207136 scopus 로고    scopus 로고
    • Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate
    • Jin R, Horning M, Mayer ML & Gouaux E (2002). Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate. Biochemistry 41, 15635-15643.
    • (2002) Biochemistry , vol.41 , pp. 15635-15643
    • Jin, R.1    Horning, M.2    Mayer, M.L.3    Gouaux, E.4
  • 52
    • 0023091647 scopus 로고
    • Glycine potentiates the NMDA response in cultured mouse brain neurons
    • Johnson JW & Ascher P (1987). Glycine potentiates the NMDA response in cultured mouse brain neurons. Nature 325, 529-531.
    • (1987) Nature , vol.325 , pp. 529-531
    • Johnson, J.W.1    Ascher, P.2
  • 53
    • 0001941068 scopus 로고
    • Fast application of agonists to isolated membrane patches
    • In, ed. Sakmann B & Neher E . Plenum Press, New York.
    • Jonas P (1995). Fast application of agonists to isolated membrane patches. In Single-Channel Recording, ed. Sakmann B & Neher E, pp. 231-243. Plenum Press, New York.
    • (1995) Single-Channel Recording , pp. 231-243
    • Jonas, P.1
  • 55
    • 84901640125 scopus 로고    scopus 로고
    • Crystal structure of a heterotetrameric NMDA receptor ion channel
    • Karakas E & Furukawa H (2014). Crystal structure of a heterotetrameric NMDA receptor ion channel. Science 344, 992-997.
    • (2014) Science , vol.344 , pp. 992-997
    • Karakas, E.1    Furukawa, H.2
  • 56
    • 84903393500 scopus 로고    scopus 로고
    • Mechanical coupling maintains the fidelity of NMDA receptor-mediated currents
    • Kazi R, Dai J, Sweeney C, Zhou HX & Wollmuth LP (2014). Mechanical coupling maintains the fidelity of NMDA receptor-mediated currents. Nat Neurosci 17, 914-922.
    • (2014) Nat Neurosci , vol.17 , pp. 914-922
    • Kazi, R.1    Dai, J.2    Sweeney, C.3    Zhou, H.X.4    Wollmuth, L.P.5
  • 58
    • 0022652797 scopus 로고
    • Excitatory amino acid receptors in hippocampal neurons: kainate fails to desensitize them
    • Kiskin NI, Krishtal OA & Tsyndrenko A (1986). Excitatory amino acid receptors in hippocampal neurons: kainate fails to desensitize them. Neurosci Lett 63, 225-230.
    • (1986) Neurosci Lett , vol.63 , pp. 225-230
    • Kiskin, N.I.1    Krishtal, O.A.2    Tsyndrenko, A.3
  • 59
    • 0023754192 scopus 로고
    • Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes
    • Kleckner NW & Dingledine R (1988). Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes. Science 241, 835-837.
    • (1988) Science , vol.241 , pp. 835-837
    • Kleckner, N.W.1    Dingledine, R.2
  • 60
    • 0029583151 scopus 로고
    • Molecular dissection of the agonist binding site of an AMPA receptor
    • Kuusinen A, Arvola M & Keinanen K (1995). Molecular dissection of the agonist binding site of an AMPA receptor. EMBO J 14, 6327-6332.
    • (1995) EMBO J , vol.14 , pp. 6327-6332
    • Kuusinen, A.1    Arvola, M.2    Keinanen, K.3
  • 61
    • 35148826056 scopus 로고    scopus 로고
    • The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain
    • Lau AY & Roux B (2007). The free energy landscapes governing conformational changes in a glutamate receptor ligand-binding domain. Structure 15, 1203-1214.
    • (2007) Structure , vol.15 , pp. 1203-1214
    • Lau, A.Y.1    Roux, B.2
  • 62
    • 84904199124 scopus 로고    scopus 로고
    • NMDA receptor structures reveal subunit arrangement and pore architecture
    • Lee CH, Lu W, Michel JC, Goehring A, Du J, Song X & Gouaux E (2014). NMDA receptor structures reveal subunit arrangement and pore architecture. Nature 511, 191-197.
    • (2014) Nature , vol.511 , pp. 191-197
    • Lee, C.H.1    Lu, W.2    Michel, J.C.3    Goehring, A.4    Du, J.5    Song, X.6    Gouaux, E.7
  • 63
    • 84885732604 scopus 로고    scopus 로고
    • Kainate receptors in health and disease
    • Lerma J & Marques JM (2013). Kainate receptors in health and disease. Neuron 80, 292-311.
    • (2013) Neuron , vol.80 , pp. 292-311
    • Lerma, J.1    Marques, J.M.2
  • 64
    • 0027145163 scopus 로고
    • Functional kainate-selective glutamate receptors in cultured hippocampal neurons
    • Lerma J, Paternain AV, Naranjo JR & Mellström B (1993). Functional kainate-selective glutamate receptors in cultured hippocampal neurons. Proc Natl Acad Sci U S A 90, 11688-11692.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 11688-11692
    • Lerma, J.1    Paternain, A.V.2    Naranjo, J.R.3    Mellström, B.4
  • 65
    • 33645095476 scopus 로고    scopus 로고
    • Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond
    • Lipton SA (2006). Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond. Nat Rev Drug Discov 5, 160-170.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 160-170
    • Lipton, S.A.1
  • 66
    • 0025220595 scopus 로고
    • Mechanisms of blockade of excitatory amino acid receptor channels
    • MacDonald JF & Nowak LM (1990). Mechanisms of blockade of excitatory amino acid receptor channels. Trends Pharmacol Sci 11, 167-172.
    • (1990) Trends Pharmacol Sci , vol.11 , pp. 167-172
    • MacDonald, J.F.1    Nowak, L.M.2
  • 67
    • 79951548418 scopus 로고    scopus 로고
    • Cations but not anions regulate the responsiveness of kainate receptors
    • Maclean DM, Wong AY, Fay AM & Bowie D (2011). Cations but not anions regulate the responsiveness of kainate receptors. J Neurosci 31, 2136-2144.
    • (2011) J Neurosci , vol.31 , pp. 2136-2144
    • Maclean, D.M.1    Wong, A.Y.2    Fay, A.M.3    Bowie, D.4
  • 68
    • 0021067668 scopus 로고
    • Receptors for the excitatory amino acids in the mammalian central nervous system
    • McLennan H ( 1983). Receptors for the excitatory amino acids in the mammalian central nervous system. Prog Neurobiol 20, 251-271.
    • (1983) Prog Neurobiol , vol.20 , pp. 251-271
    • McLennan, H.1
  • 69
    • 0036483593 scopus 로고    scopus 로고
    • The structure and function of glutamate receptor ion channels
    • Madden DR (2002). The structure and function of glutamate receptor ion channels. Nat Rev Neurosci 3, 91-101.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 91-101
    • Madden, D.R.1
  • 70
    • 0029899637 scopus 로고    scopus 로고
    • A venus flytrap mechanism for activation and desensitization of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors
    • Mano I, Lamed Y & Teichberg VI (1996). A venus flytrap mechanism for activation and desensitization of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors. J Biol Chem 271, 15299-15302.
    • (1996) J Biol Chem , vol.271 , pp. 15299-15302
    • Mano, I.1    Lamed, Y.2    Teichberg, V.I.3
  • 71
    • 0026093312 scopus 로고
    • Sequence and expression of a metabotropic glutamate receptor
    • Masu M, Tanabe Y, Tsuchida K, Shigemoto R & Nakanishi S (1991). Sequence and expression of a metabotropic glutamate receptor. Nature 349, 760-765.
    • (1991) Nature , vol.349 , pp. 760-765
    • Masu, M.1    Tanabe, Y.2    Tsuchida, K.3    Shigemoto, R.4    Nakanishi, S.5
  • 72
    • 13844266202 scopus 로고    scopus 로고
    • Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity
    • Mayer ML (2005). Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity. Neuron 45, 539-552.
    • (2005) Neuron , vol.45 , pp. 539-552
    • Mayer, M.L.1
  • 73
    • 80054065551 scopus 로고    scopus 로고
    • Emerging models of glutamate receptor ion channel structure and function
    • Mayer ML (2011). Emerging models of glutamate receptor ion channel structure and function. Structure 19, 1370-1380.
    • (2011) Structure , vol.19 , pp. 1370-1380
    • Mayer, M.L.1
  • 74
    • 2342462388 scopus 로고    scopus 로고
    • Structure and function of glutamate receptor ion channels
    • Mayer ML & Armstrong N (2004). Structure and function of glutamate receptor ion channels. Annu Rev Physiol 66, 161-181.
    • (2004) Annu Rev Physiol , vol.66 , pp. 161-181
    • Mayer, M.L.1    Armstrong, N.2
  • 75
    • 0023125256 scopus 로고
    • The physiology of excitatory amino acids in the vertebrate central nervous system
    • Mayer ML & Westbrook GL (1987). The physiology of excitatory amino acids in the vertebrate central nervous system. Prog Neurobiol 28, 197-276.
    • (1987) Prog Neurobiol , vol.28 , pp. 197-276
    • Mayer, M.L.1    Westbrook, G.L.2
  • 77
    • 84856790671 scopus 로고    scopus 로고
    • Domain architecture of a calcium-permeable AMPA receptor in a ligand-free conformation
    • Midgett CR, Gill A & Madden DR (2012). Domain architecture of a calcium-permeable AMPA receptor in a ligand-free conformation. Front Mol Neurosci 4, 56.
    • (2012) Front Mol Neurosci , vol.4 , pp. 56
    • Midgett, C.R.1    Gill, A.2    Madden, D.R.3
  • 78
    • 50149084710 scopus 로고    scopus 로고
    • The quaternary structure of a calcium-permeable AMPA receptor: conservation of shape and symmetry across functionally distinct subunit assemblies
    • Midgett CR & Madden DR (2008). The quaternary structure of a calcium-permeable AMPA receptor: conservation of shape and symmetry across functionally distinct subunit assemblies. J Mol Biol 382, 578-584.
    • (2008) J Mol Biol , vol.382 , pp. 578-584
    • Midgett, C.R.1    Madden, D.R.2
  • 79
    • 34047216195 scopus 로고    scopus 로고
    • Targeting AMPA receptor gating processes with allosteric modulators and mutations
    • Mitchell NA & Fleck MW (2007). Targeting AMPA receptor gating processes with allosteric modulators and mutations. Biophys J 92, 2392-2402.
    • (2007) Biophys J , vol.92 , pp. 2392-2402
    • Mitchell, N.A.1    Fleck, M.W.2
  • 81
    • 78650974284 scopus 로고    scopus 로고
    • The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors
    • Nakagawa T (2010). The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors. Mol Neurobiol 42, 161-184.
    • (2010) Mol Neurobiol , vol.42 , pp. 161-184
    • Nakagawa, T.1
  • 82
    • 13444302564 scopus 로고    scopus 로고
    • Structure and different conformational states of native AMPA receptor complexes
    • Nakagawa T, Cheng Y, Ramm E, Sheng M & Walz T (2005). Structure and different conformational states of native AMPA receptor complexes. Nature 433, 545-549.
    • (2005) Nature , vol.433 , pp. 545-549
    • Nakagawa, T.1    Cheng, Y.2    Ramm, E.3    Sheng, M.4    Walz, T.5
  • 83
    • 32344443866 scopus 로고    scopus 로고
    • Three-dimensional structure of an AMPA receptor without associated stargazin/TARP proteins
    • Nakagawa T, Cheng Y, Sheng M & Walz T (2006). Three-dimensional structure of an AMPA receptor without associated stargazin/TARP proteins. Biol Chem 387, 179-187.
    • (2006) Biol Chem , vol.387 , pp. 179-187
    • Nakagawa, T.1    Cheng, Y.2    Sheng, M.3    Walz, T.4
  • 84
    • 0025221685 scopus 로고
    • A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties
    • Nakanishi N, Shneider NA & Axel R (1990). A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties. Neuron 5, 569-581.
    • (1990) Neuron , vol.5 , pp. 569-581
    • Nakanishi, N.1    Shneider, N.A.2    Axel, R.3
  • 85
    • 0026437728 scopus 로고
    • Molecular diversity of glutamate receptors and implications for brain function
    • Nakanishi S ( 1992). Molecular diversity of glutamate receptors and implications for brain function. Science 258, 597-603.
    • (1992) Science , vol.258 , pp. 597-603
    • Nakanishi, S.1
  • 86
    • 13444281913 scopus 로고    scopus 로고
    • Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid
    • Nanao MH, Green T, Stern-Bach Y, Heinemann SF & Choe S (2005). Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid. Proc Natl Acad Sci U S A 102, 1708-1713.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1708-1713
    • Nanao, M.H.1    Green, T.2    Stern-Bach, Y.3    Heinemann, S.F.4    Choe, S.5
  • 88
    • 79951985476 scopus 로고    scopus 로고
    • Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization
    • Nayeem N, Mayans O & Green T (2011). Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization. J Neurosci 31, 2916-2924.
    • (2011) J Neurosci , vol.31 , pp. 2916-2924
    • Nayeem, N.1    Mayans, O.2    Green, T.3
  • 91
    • 78649682240 scopus 로고    scopus 로고
    • Scalable rule-based modelling of allosteric proteins and biochemical networks
    • Ollivier JF, Shahrezaei V & Swain PS (2010). Scalable rule-based modelling of allosteric proteins and biochemical networks. PLoS Comput Biol 6, e1000975.
    • (2010) PLoS Comput Biol , vol.6 , pp. e1000975
    • Ollivier, J.F.1    Shahrezaei, V.2    Swain, P.S.3
  • 92
    • 0032032919 scopus 로고    scopus 로고
    • The macro- and microarchitectures of the ligand-binding domain of glutamate receptors
    • Paas Y (1998). The macro- and microarchitectures of the ligand-binding domain of glutamate receptors. Trends Neurosci 21, 117-125.
    • (1998) Trends Neurosci , vol.21 , pp. 117-125
    • Paas, Y.1
  • 93
    • 84878254691 scopus 로고    scopus 로고
    • NMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease
    • Paoletti P, Bellone C & Zhou Q (2013). NMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease. Nat Rev Neurosci 14, 383-400.
    • (2013) Nat Rev Neurosci , vol.14 , pp. 383-400
    • Paoletti, P.1    Bellone, C.2    Zhou, Q.3
  • 94
    • 0025456905 scopus 로고
    • Structure-activity relationships for amino acid transmitter candidates acting at N-methyl-d-aspartate and quisqualate receptors
    • Patneau DK & Mayer ML (1990). Structure-activity relationships for amino acid transmitter candidates acting at N-methyl-d-aspartate and quisqualate receptors. J Neurosci 10, 2385-2399.
    • (1990) J Neurosci , vol.10 , pp. 2385-2399
    • Patneau, D.K.1    Mayer, M.L.2
  • 95
    • 0025852165 scopus 로고
    • Kinetic analysis of interactions between kainate and AMPA: evidence for activation of a single receptor in mouse hippocampal neurons
    • Patneau DK & Mayer ML (1991). Kinetic analysis of interactions between kainate and AMPA: evidence for activation of a single receptor in mouse hippocampal neurons. Neuron 6, 785-798.
    • (1991) Neuron , vol.6 , pp. 785-798
    • Patneau, D.K.1    Mayer, M.L.2
  • 96
    • 0026556811 scopus 로고
    • Activation and desensitization of AMPA/kainate receptors by novel derivatives of willardiine
    • Patneau DK, Mayer ML, Jane DE & Watkins JC (1992). Activation and desensitization of AMPA/kainate receptors by novel derivatives of willardiine. J Neurosci 12, 595-606.
    • (1992) J Neurosci , vol.12 , pp. 595-606
    • Patneau, D.K.1    Mayer, M.L.2    Jane, D.E.3    Watkins, J.C.4
  • 97
    • 0027228511 scopus 로고
    • Hippocampal neurons exhibit cyclothiazide-sensitive rapidly desensitizing responses to kainate
    • Patneau DK, Vyklicky L Jr & Mayer ML (1993). Hippocampal neurons exhibit cyclothiazide-sensitive rapidly desensitizing responses to kainate. J Neurosci 13, 3496-3509.
    • (1993) J Neurosci , vol.13 , pp. 3496-3509
    • Patneau, D.K.1    Vyklicky Jr, L.2    Mayer, M.L.3
  • 99
    • 33847769253 scopus 로고    scopus 로고
    • Structure and mechanism of kainate receptor modulation by anions
    • Plested AJ & Mayer ML (2007). Structure and mechanism of kainate receptor modulation by anions. Neuron 53, 829-841.
    • (2007) Neuron , vol.53 , pp. 829-841
    • Plested, A.J.1    Mayer, M.L.2
  • 100
    • 44649169115 scopus 로고    scopus 로고
    • Molecular basis of kainate receptor modulation by sodium
    • Plested AJ, Vijayan R, Biggin PC & Mayer ML (2008). Molecular basis of kainate receptor modulation by sodium. Neuron 58, 720-735.
    • (2008) Neuron , vol.58 , pp. 720-735
    • Plested, A.J.1    Vijayan, R.2    Biggin, P.C.3    Mayer, M.L.4
  • 101
    • 33845416936 scopus 로고    scopus 로고
    • Block of kainate receptor desensitization uncovers a key trafficking checkpoint
    • Priel A, Selak S, Lerma J & Stern-Bach Y (2006). Block of kainate receptor desensitization uncovers a key trafficking checkpoint. Neuron 52, 1037-1046.
    • (2006) Neuron , vol.52 , pp. 1037-1046
    • Priel, A.1    Selak, S.2    Lerma, J.3    Stern-Bach, Y.4
  • 103
    • 0036950527 scopus 로고    scopus 로고
    • Channel gating of NMDA receptors
    • Qian A & Johnson JW (2002). Channel gating of NMDA receptors. Physiol Behav 77, 577-582.
    • (2002) Physiol Behav , vol.77 , pp. 577-582
    • Qian, A.1    Johnson, J.W.2
  • 104
    • 0025716317 scopus 로고
    • Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria
    • discussion 351-342.
    • Quiocho FA (1990). Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Philos Trans R Soc Lond B Biol Sci 326, 341-351; discussion 351-342.
    • (1990) Philos Trans R Soc Lond B Biol Sci , vol.326 , pp. 341-351
    • Quiocho, F.A.1
  • 105
    • 84897024230 scopus 로고    scopus 로고
    • Tethered ligands reveal glutamate receptor desensitization depends on subunit occupancy
    • Reiner A & Isacoff EY (2014). Tethered ligands reveal glutamate receptor desensitization depends on subunit occupancy. Nat Chem Biol 10, 273-280.
    • (2014) Nat Chem Biol , vol.10 , pp. 273-280
    • Reiner, A.1    Isacoff, E.Y.2
  • 106
    • 17644377289 scopus 로고    scopus 로고
    • AMPA receptor binding cleft mutations that alter affinity, efficacy, and recovery from desensitization
    • Robert A, Armstrong N, Gouaux JE & Howe JR (2005). AMPA receptor binding cleft mutations that alter affinity, efficacy, and recovery from desensitization. J Neurosci 25, 3752-3762.
    • (2005) J Neurosci , vol.25 , pp. 3752-3762
    • Robert, A.1    Armstrong, N.2    Gouaux, J.E.3    Howe, J.R.4
  • 107
    • 0037320716 scopus 로고    scopus 로고
    • How AMPA receptor desensitization depends on receptor occupancy
    • Robert A & Howe JR (2003). How AMPA receptor desensitization depends on receptor occupancy. J Neurosci 23, 847-858.
    • (2003) J Neurosci , vol.23 , pp. 847-858
    • Robert, A.1    Howe, J.R.2
  • 108
    • 0035426114 scopus 로고    scopus 로고
    • Subunit interactions and AMPA receptor desensitization
    • Robert A, Irizarry SN, Hughes TE & Howe JR (2001). Subunit interactions and AMPA receptor desensitization. J Neurosci 21, 5574-5586.
    • (2001) J Neurosci , vol.21 , pp. 5574-5586
    • Robert, A.1    Irizarry, S.N.2    Hughes, T.E.3    Howe, J.R.4
  • 109
    • 0035923431 scopus 로고    scopus 로고
    • First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers
    • Safferling M, Tichelaar W, Kummerle G, Jouppila A, Kuusinen A, Keinanen K & Madden DR (2001). First images of a glutamate receptor ion channel: oligomeric state and molecular dimensions of GluRB homomers. Biochemistry 40, 13948-13953.
    • (2001) Biochemistry , vol.40 , pp. 13948-13953
    • Safferling, M.1    Tichelaar, W.2    Kummerle, G.3    Jouppila, A.4    Kuusinen, A.5    Keinanen, K.6    Madden, D.R.7
  • 110
    • 0019215162 scopus 로고
    • Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist
    • Sakmann B, Patlak J & Neher E (1980). Single acetylcholine-activated channels show burst-kinetics in presence of desensitizing concentrations of agonist. Nature 286, 71-73.
    • (1980) Nature , vol.286 , pp. 71-73
    • Sakmann, B.1    Patlak, J.2    Neher, E.3
  • 111
    • 42949123365 scopus 로고    scopus 로고
    • Targeting the glutamatergic system to develop novel, improved therapeutics for mood disorders
    • Sanacora G, Zarate CA, Krystal JH & Manji HK (2008). Targeting the glutamatergic system to develop novel, improved therapeutics for mood disorders. Nat Rev Drug Discov 7, 426-437.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 426-437
    • Sanacora, G.1    Zarate, C.A.2    Krystal, J.H.3    Manji, H.K.4
  • 114
    • 0027234701 scopus 로고
    • The TINS/TiPS Lecture. The molecular biology of mammalian glutamate receptor channels
    • Seeburg PH (1993). The TINS/TiPS Lecture. The molecular biology of mammalian glutamate receptor channels. Trends Neurosci 16, 359-365.
    • (1993) Trends Neurosci , vol.16 , pp. 359-365
    • Seeburg, P.H.1
  • 115
    • 84920165039 scopus 로고    scopus 로고
    • Structure and gating of tetrameric glutamate receptors
    • Sobolevsky AI (2013). Structure and gating of tetrameric glutamate receptors. J Physiol (in press; DOI: 10.1113/jphysiol.2013.264911).
    • (2013) J Physiol
    • Sobolevsky, A.I.1
  • 116
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky AI, Rosconi MP & Gouaux E (2009). X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756.
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 117
    • 0028559605 scopus 로고
    • Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
    • Stern-Bach Y, Bettler B, Hartley M, Sheppard PO, O'Hara PJ & Heinemann SF (1994). Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins. Neuron 13, 1345-1357.
    • (1994) Neuron , vol.13 , pp. 1345-1357
    • Stern-Bach, Y.1    Bettler, B.2    Hartley, M.3    Sheppard, P.O.4    O'Hara, P.J.5    Heinemann, S.F.6
  • 118
    • 0032191104 scopus 로고    scopus 로고
    • A point mutation in the glutamate binding site blocks desensitization of AMPA receptors
    • Stern-Bach Y, Russo S, Neuman M & Rosenmund C (1998). A point mutation in the glutamate binding site blocks desensitization of AMPA receptors. Neuron 21, 907-918.
    • (1998) Neuron , vol.21 , pp. 907-918
    • Stern-Bach, Y.1    Russo, S.2    Neuman, M.3    Rosenmund, C.4
  • 120
    • 0032562651 scopus 로고    scopus 로고
    • The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: comparisons with other amino acid binding proteins
    • Sun YJ, Rose J, Wang BC & Hsiao CD (1998). The structure of glutamine-binding protein complexed with glutamine at 1.94 Å resolution: comparisons with other amino acid binding proteins. J Mol Biol 278, 219-229.
    • (1998) J Mol Biol , vol.278 , pp. 219-229
    • Sun, Y.J.1    Rose, J.2    Wang, B.C.3    Hsiao, C.D.4
  • 122
    • 0024580689 scopus 로고
    • Quisqualate activates a rapidly inactivating high conductance ionic channel in hippocampal neurons
    • Tang CM, Dichter M & Morad M (1989). Quisqualate activates a rapidly inactivating high conductance ionic channel in hippocampal neurons. Science 243, 1474-1477.
    • (1989) Science , vol.243 , pp. 1474-1477
    • Tang, C.M.1    Dichter, M.2    Morad, M.3
  • 123
    • 7444240214 scopus 로고    scopus 로고
    • The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly
    • Tichelaar W, Safferling M, Keinanen K, Stark H & Madden DR (2004). The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly. J Mol Biol 344, 435-442.
    • (2004) J Mol Biol , vol.344 , pp. 435-442
    • Tichelaar, W.1    Safferling, M.2    Keinanen, K.3    Stark, H.4    Madden, D.R.5
  • 126
    • 0025006846 scopus 로고
    • Modulation of N-methyl-d-aspartic acid receptor desensitization by glycine in mouse cultured hippocampal neurones
    • Vyklicky L Jr, Benveniste M & Mayer ML (1990). Modulation of N-methyl-d-aspartic acid receptor desensitization by glycine in mouse cultured hippocampal neurones. J Physiol 428, 313-331.
    • (1990) J Physiol , vol.428 , pp. 313-331
    • Vyklicky Jr, L.1    Benveniste, M.2    Mayer, M.L.3
  • 127
    • 0026351573 scopus 로고
    • Modulation of excitatory synaptic transmission by drugs that reduce desensitization at AMPA/kainate receptors
    • Vyklicky L Jr., Patneau DK & Mayer ML (1991). Modulation of excitatory synaptic transmission by drugs that reduce desensitization at AMPA/kainate receptors. Neuron 7, 971-984.
    • (1991) Neuron , vol.7 , pp. 971-984
    • Vyklicky Jr, L.1    Patneau, D.K.2    Mayer, M.L.3
  • 130
    • 33744973079 scopus 로고    scopus 로고
    • External ions are coactivators of kainate receptors
    • Wong AY, Fay AM & Bowie D (2006). External ions are coactivators of kainate receptors. J Neurosci 26, 5750-5755.
    • (2006) J Neurosci , vol.26 , pp. 5750-5755
    • Wong, A.Y.1    Fay, A.M.2    Bowie, D.3
  • 131
    • 34250806504 scopus 로고    scopus 로고
    • - dipole couples agonist binding to kainate receptor activation
    • - dipole couples agonist binding to kainate receptor activation. J Neurosci 27, 6800-6809.
    • (2007) J Neurosci , vol.27 , pp. 6800-6809
    • Wong, A.Y.1    MacLean, D.M.2    Bowie, D.3
  • 132
    • 84907261409 scopus 로고    scopus 로고
    • Structure of an agonist-bound ionotropic glutamate receptor
    • Yelshanskaya MV, Li M & Sobolevsky AI (2014). Structure of an agonist-bound ionotropic glutamate receptor. Science 345, 1070-1074.
    • (2014) Science , vol.345 , pp. 1070-1074
    • Yelshanskaya, M.V.1    Li, M.2    Sobolevsky, A.I.3
  • 133
    • 0037404640 scopus 로고    scopus 로고
    • The δ2 glutamate receptor: 10 years later
    • Yuzaki M (2003). The δ2 glutamate receptor: 10 years later. Neurosci Res 46, 11-22.
    • (2003) Neurosci Res , vol.46 , pp. 11-22
    • Yuzaki, M.1
  • 134
    • 84864719369 scopus 로고    scopus 로고
    • The ins and outs of GluD2-why and how Purkinje cells use the special glutamate receptor
    • Yuzaki M (2012). The ins and outs of GluD2-why and how Purkinje cells use the special glutamate receptor. Cerebellum 11, 438-439.
    • (2012) Cerebellum , vol.11 , pp. 438-439
    • Yuzaki, M.1
  • 135
    • 38549125923 scopus 로고    scopus 로고
    • Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating
    • Zhang W, Cho Y, Lolis E & Howe JR (2008). Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating. J Neurosci 28, 932-943.
    • (2008) J Neurosci , vol.28 , pp. 932-943
    • Zhang, W.1    Cho, Y.2    Lolis, E.3    Howe, J.R.4
  • 136
    • 33749176816 scopus 로고    scopus 로고
    • Interface interactions modulating desensitization of the kainate-selective ionotropic glutamate receptor subunit GluR6
    • Zhang Y, Nayeem N, Nanao MH & Green T (2006). Interface interactions modulating desensitization of the kainate-selective ionotropic glutamate receptor subunit GluR6. J Neurosci 26, 10033-10042.
    • (2006) J Neurosci , vol.26 , pp. 10033-10042
    • Zhang, Y.1    Nayeem, N.2    Nanao, M.H.3    Green, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.