메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Radial symmetry in a chimeric glutamate receptor pore

Author keywords

[No Author keywords available]

Indexed keywords

AC RECEPTOR SUBUNIT; B D RECPTOR SUBUNIT; IONOTROPIC RECEPTOR; KAINIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR SUBUNIT GLUK2; N METHYL DEXTRO ASPARTIC ACID RECEPTOR SUBUNIT GLUN1; N METHYL DEXTRO ASPARTIC ACID RECEPTOR SUBUNIT GLUN2B; RECEPTOR SUBUNIT; UNCLASSIFIED DRUG; COMPLEMENTARY DNA; DOCOSAHEXAENOIC ACID;

EID: 84896830227     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4349     Document Type: Article
Times cited : (16)

References (56)
  • 1
    • 77952363301 scopus 로고    scopus 로고
    • Glutamate receptor ion channels: Structure, regulation, and function
    • Traynelis, S. F. et al. Glutamate receptor ion channels: structure, regulation, and function. Pharmacol. Rev. 62, 405-496 (2010).
    • (2010) Pharmacol. Rev. , vol.62 , pp. 405-496
    • Traynelis, S.F.1
  • 2
    • 80054065551 scopus 로고    scopus 로고
    • Emerging models of glutamate receptor ion channel structure and function
    • Mayer, M. L. Emerging models of glutamate receptor ion channel structure and function. Structure 19, 1370-1380 (2011).
    • (2011) Structure , vol.19 , pp. 1370-1380
    • Mayer M., .L.1
  • 3
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky, A. I., Rosconi, M. P. & Gouaux, E. X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462, 745-756 (2009).
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 5
    • 0037442813 scopus 로고    scopus 로고
    • Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits
    • Schorge, S. & Colquhoun, D. Studies of NMDA receptor function and stoichiometry with truncated and tandem subunits. J. Neurosci. 23, 1151-1158 (2003). (Pubitemid 36258894)
    • (2003) Journal of Neuroscience , vol.23 , Issue.4 , pp. 1151-1158
    • Schorge, S.1    Colquhoun, D.2
  • 6
    • 81155142109 scopus 로고    scopus 로고
    • The transmembrane domain C of AMPA receptors is critically involved in receptor function and modulation
    • Terhag, J., Gottschling, K. & Hollmann, M. The transmembrane domain C of AMPA receptors is critically involved in receptor function and modulation. Front. Mol. Neurosci. 3, 117 (2010).
    • (2010) Front. Mol. Neurosci. , vol.3 , pp. 117
    • Terhag, J.1    Gottschling, K.2    Hollmann, M.3
  • 7
    • 84878485837 scopus 로고    scopus 로고
    • A eukaryotic specific transmembrane segment is required for tetramerization in AMPA receptors
    • Salussolia, C. L. et al. A eukaryotic specific transmembrane segment is required for tetramerization in AMPA receptors. J. Neurosci. 33, 9840-9845 (2013).
    • (2013) J. Neurosci. , vol.33 , pp. 9840-9845
    • Salussolia, C.L.1
  • 8
    • 0036924208 scopus 로고    scopus 로고
    • Staggering of subunits in NMDAR channels
    • Sobolevsky, A. I., Rooney, L. & Wollmuth, L. P. Staggering of subunits in NMDAR channels. Biophys. J. 83, 3304-3314 (2002). (Pubitemid 36041948)
    • (2002) Biophysical Journal , vol.83 , Issue.6 , pp. 3304-3314
    • Sobolevsky, A.I.1    Rooney, L.2    Wollmuth, L.P.3
  • 9
    • 1242293628 scopus 로고    scopus 로고
    • The Outer Pore of the Glutamate Receptor Channel Has 2-Fold Rotational Symmetry
    • DOI 10.1016/S0896-6273(04)00008-X
    • Sobolevsky, A. I., Yelshansky, M. V. & Wollmuth, L. P. The outer pore of the glutamate receptor channel has 2-fold rotational symmetry. Neuron 41, 367-378 (2004). (Pubitemid 38221041)
    • (2004) Neuron , vol.41 , Issue.3 , pp. 367-378
    • Sobolevsky, A.I.1    Yelshansky, M.V.2    Wollmuth, L.P.3
  • 10
    • 79959268661 scopus 로고    scopus 로고
    • Atomistic mechanism for the activation and desensitization of an AMPA-subtype glutamate receptor
    • Dong, H. & Zhou, H. X. Atomistic mechanism for the activation and desensitization of an AMPA-subtype glutamate receptor. Nat. Commun. 2, 354 (2011).
    • (2011) Nat. Commun. , vol.2 , pp. 354
    • Dong, H.1    Zhou, H.X.2
  • 11
    • 84880445751 scopus 로고    scopus 로고
    • Asynchronous movements prior to pore opening in NMDA receptors
    • Kazi, R. et al. Asynchronous movements prior to pore opening in NMDA receptors. J. Neurosci. 33, 12052-12066 (2013).
    • (2013) J. Neurosci. , vol.33 , pp. 12052-12066
    • Kazi, R.1
  • 12
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh, J., Gamal El-Din, T. M., Scheuer, T., Zheng, N. & Catterall, W. A. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature 486, 135-139 (2012).
    • (2012) Nature , vol.486 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 13
    • 84883246984 scopus 로고    scopus 로고
    • Q/R site interactions with the M3 helix in GluK2 kainate receptor channels revealed by thermodynamic mutant cycles
    • Lopez, M. N., Wilding, T. J. & Huettner, J. E. Q/R site interactions with the M3 helix in GluK2 kainate receptor channels revealed by thermodynamic mutant cycles. J. Gen. Physiol. 142, 225-239 (2013).
    • (2013) J. Gen. Physiol. , vol.142 , pp. 225-239
    • Lopez, M.N.1    Wilding, T.J.2    Huettner, J.E.3
  • 14
    • 84862777495 scopus 로고    scopus 로고
    • A single GluN2 subunit residue controls NMDA receptor channel properties via intersubunit interaction
    • Siegler Retchless, B., Gao, W. & Johnson, J. W. A single GluN2 subunit residue controls NMDA receptor channel properties via intersubunit interaction. Nat. Neurosci. 15, 406-413 (2012).
    • (2012) Nat. Neurosci. , vol.15 , pp. 406-413
    • Siegler Retchless, B.1    Gao, W.2    Johnson, J.W.3
  • 15
    • 77957235696 scopus 로고    scopus 로고
    • Control of assembly and function of glutamate receptors by the amino-terminal domain
    • Hansen, K. B., Furukawa, H. & Traynelis, S. F. Control of assembly and function of glutamate receptors by the amino-terminal domain. Mol. Pharmacol. 78, 535-549 (2010).
    • (2010) Mol. Pharmacol. , vol.78 , pp. 535-549
    • Hansen, K.B.1    Furukawa, H.2    Traynelis, S.F.3
  • 16
    • 53149132407 scopus 로고    scopus 로고
    • Different structural requirements for functional ion pore transplantation suggest different gating mechanisms of NMDA and kainate receptors
    • Villmann, C. et al. Different structural requirements for functional ion pore transplantation suggest different gating mechanisms of NMDA and kainate receptors. J. Neurochem. 107, 453-465 (2008).
    • (2008) J. Neurochem. , vol.107 , pp. 453-465
    • Villmann, C.1
  • 18
    • 84859502370 scopus 로고    scopus 로고
    • An alternating GluN1-2- 1-2 subunit arrangement in mature NMDA receptors
    • Riou, M., Stroebel, D., Edwardson, J. M. & Paoletti, P. An alternating GluN1-2- 1-2 subunit arrangement in mature NMDA receptors. PLoS One 7, e35134 (2012).
    • (2012) PLoS One , vol.7
    • Riou, M.1    Stroebel, D.2    Edwardson, J.M.3    Paoletti, P.4
  • 19
    • 84881232191 scopus 로고    scopus 로고
    • A-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements
    • Balasuriya, D. et al. a-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements. J. Biol. Chem. 288, 21987-21998 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 21987-21998
    • Balasuriya, D.1
  • 20
    • 0023091647 scopus 로고
    • Glycine potentiates the NMDA response in cultured mouse brain neurons
    • DOI 10.1038/325529a0
    • Johnson, J. W. & Ascher, P. Glycine potentiates the NMDA response in cultured mouse brain neurons. Nature 325, 529-531 (1987). (Pubitemid 17056733)
    • (1987) Nature , vol.325 , Issue.6104 , pp. 529-531
    • Johnson, J.W.1    Ascher, P.2
  • 21
    • 0023754192 scopus 로고
    • Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes
    • Kleckner, N. W. & Dingledine, R. Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes. Science 241, 835-837 (1988).
    • (1988) Science , vol.241 , pp. 835-837
    • Kleckner, N.W.1    Dingledine, R.2
  • 22
    • 0029082204 scopus 로고
    • Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block
    • Bowie, D. & Mayer, M. L. Inward rectification of both AMPA and kainate subtype glutamate receptors generated by polyamine-mediated ion channel block. Neuron 15, 453-462 (1995).
    • (1995) Neuron , vol.15 , pp. 453-462
    • Bowie, D.1    Mayer, M.L.2
  • 23
    • 26844541625 scopus 로고    scopus 로고
    • Q/R site editing controls kainate receptor inhibition by membrane fatty acids
    • DOI 10.1523/JNEUROSCI.2826-05.2005
    • Wilding, T. J., Zhou, Y. & Huettner, J. E. Q/R site editing controls kainate receptor inhibition by membrane fatty acids. J. Neurosci. 25, 9470-9478 (2005). (Pubitemid 41464761)
    • (2005) Journal of Neuroscience , vol.25 , Issue.41 , pp. 9470-9478
    • Wilding, T.J.1    Zhou, Y.2    Huettner, J.E.3
  • 24
    • 0026570085 scopus 로고
    • Potentiation of NMDA receptor currents by arachidonic acid
    • Miller, B., Sarantis, M., Traynelis, S. F. & Attwell, D. Potentiation of NMDA receptor currents by arachidonic acid. Nature 355, 722-725 (1992).
    • (1992) Nature , vol.355 , pp. 722-725
    • Miller, B.1    Sarantis, M.2    Traynelis, S.F.3    Attwell, D.4
  • 25
    • 0028210975 scopus 로고
    • Facilitatory effect of docosahexaenoic acid on N-methyl-D-aspartate response in pyramidal neurones of rat cerebral cortex
    • Nishikawa, M., Kimura, S. & Akaike, N. Facilitatory effect of docosahexaenoic acid on N-methyl-D-aspartate response in pyramidal neurones of rat cerebral cortex. J. Physiol. 475, 83-93 (1994). (Pubitemid 24081939)
    • (1994) Journal of Physiology , vol.475 , Issue.1 , pp. 83-93
    • Nishikawa, M.1    Kimura, S.2    Akaike, N.3
  • 26
    • 0034114521 scopus 로고    scopus 로고
    • Mutation of a glutamate receptor motif reveals its role in gating and δ2 receptor channel properties
    • DOI 10.1038/73877
    • Kohda, K., Wang, Y. & Yuzaki, M. Mutation of a glutamate receptor motif reveals its role in gating and delta2 receptor channel properties. Nat. Neurosci. 3, 315-322 (2000). (Pubitemid 30185480)
    • (2000) Nature Neuroscience , vol.3 , Issue.4 , pp. 315-322
    • Kohda, K.1    Wang, Y.2    Yuzaki, M.3
  • 27
    • 47949104957 scopus 로고    scopus 로고
    • The NR1 M3 domain mediates allosteric coupling in the N-methyl-D-aspartate receptor
    • Blanke, M. L. & VanDongen, A. M. The NR1 M3 domain mediates allosteric coupling in the N-methyl-D-aspartate receptor. Mol. Pharmacol. 74, 454-465 (2008).
    • (2008) Mol. Pharmacol. , vol.74 , pp. 454-465
    • Blanke, M.L.1    Vandongen, A.M.2
  • 28
    • 2542553538 scopus 로고    scopus 로고
    • Effects of the lurcher mutation on GluR1 desensitation and activation kinetics
    • DOI 10.1523/JNEUROSCI.0660-04.2004
    • Klein, R. M. & Howe, J. R. Effects of the lurcher mutation on GluR1 desensitization and activation kinetics. J. Neurosci. 24, 4941-4951 (2004). (Pubitemid 38697827)
    • (2004) Journal of Neuroscience , vol.24 , Issue.21 , pp. 4941-4951
    • Klein, R.M.1    Howe, J.R.2
  • 29
    • 0028916586 scopus 로고
    • In vitro pharmacology of ACEA-1021 and ACEA-1031: Systemically active quinoxalinediones with high affinity and selectivity for N-methyl-D-aspartate receptor glycine sites
    • Woodward, R. M., Huettner, J. E., Guastella, J., Keana, J. F. & Weber, E. In vitro pharmacology of ACEA-1021 and ACEA-1031: systemically active quinoxalinediones with high affinity and selectivity for N-methyl-D-aspartate receptor glycine sites. Mol. Pharmacol. 47, 568-581 (1995).
    • (1995) Mol. Pharmacol. , vol.47 , pp. 568-581
    • Woodward, R.M.1    Huettner, J.E.2    Guastella, J.3    Keana, J.F.4    Weber, E.5
  • 30
    • 0024518502 scopus 로고
    • Indole-2-carboxylic acid: A competitive antagonist of potentiation by glycine at the NMDA receptor
    • Huettner, J. E. Indole-2-carboxylic acid: a competitive antagonist of potentiation by glycine at the NMDA receptor. Science 243, 1611-1613 (1989). (Pubitemid 19090513)
    • (1989) Science , vol.243 , Issue.4898 , pp. 1611-1613
    • Huettner, J.E.1
  • 31
    • 0025191432 scopus 로고
    • Structure-activity relationships in the development of excitatory amino acid receptor agonists and competitive antagonists
    • DOI 10.1016/0165-6147(90)90038-A
    • Watkins, J. C., Krogsgaard-Larsen, P. & Honoré, T. Structure-activity relationships in the development of excitatory amino acid receptor agonists and competitive antagonists. Trends Pharmacol. Sci. 11, 25-33 (1990). (Pubitemid 20023917)
    • (1990) Trends in Pharmacological Sciences , vol.11 , Issue.1 , pp. 25-33
    • Watkins, J.C.1    Krogsgaard-Larsen, P.2    Honore, T.3
  • 32
    • 0025974234 scopus 로고
    • Kinetic analysis of antagonist action at N-methyl-D-aspartic acid receptors. Two binding sites each for glutamate and glycine
    • Benveniste, M. & Mayer, M. L. Kinetic analysis of antagonist action at N-methyl-D-aspartic acid receptors. Two binding sites each for glutamate and glycine. Biophys. J. 59, 560-573 (1991).
    • (1991) Biophys. J. , vol.59 , pp. 560-573
    • Benveniste, M.1    Mayer, M.L.2
  • 33
    • 0025944430 scopus 로고
    • Activation kinetics reveal the number of glutamate and glycine binding sites on the N-methyl-D-aspartate receptor
    • Clements, J. D. & Westbrook, G. L. Activation kinetics reveal the number of glutamate and glycine binding sites on the N-methyl-D-aspartate receptor. Neuron 7, 605-613 (1991).
    • (1991) Neuron , vol.7 , pp. 605-613
    • Clements, J.D.1    Westbrook, G.L.2
  • 34
    • 0037312558 scopus 로고    scopus 로고
    • Activation of NR1/NR2B NMDA receptors
    • DOI 10.1038/nn1000
    • Banke, T. G. & Traynelis, S. F. Activation of NR1/NR2B NMDA receptors. Nat. Neurosci. 6, 144-152 (2003). (Pubitemid 36182783)
    • (2003) Nature Neuroscience , vol.6 , Issue.2 , pp. 144-152
    • Banke, T.G.1    Traynelis, S.F.2
  • 35
    • 0037407919 scopus 로고    scopus 로고
    • Modal gating of NMDA receptors and the shape of their synaptic response
    • Popescu, G. & Auerbach, A. Modal gating of NMDA receptors and the shape of their synaptic response. Nat. Neurosci. 6, 476-483 (2003). (Pubitemid 36514695)
    • (2003) Nature Neuroscience , vol.6 , Issue.5 , pp. 476-483
    • Popescu, G.1    Auerbach, A.2
  • 36
    • 29244456432 scopus 로고    scopus 로고
    • Maximum likelihood fitting of single channel NMDA activity with a mechanism composed of independent dimers of subunits
    • DOI 10.1113/jphysiol.2005.095349
    • Schorge, S., Elenes, S. & Colquhoun, D. Maximum likelihood fitting of single channel NMDA activity with a mechanism composed of independent dimers of subunits. J Physiol. 569, 395-418 (2005). (Pubitemid 41830110)
    • (2005) Journal of Physiology , vol.569 , Issue.2 , pp. 395-418
    • Schorge, S.1    Elenes, S.2    Colquhoun, D.3
  • 37
    • 0032486422 scopus 로고    scopus 로고
    • The tetrameric structure of a glutamate receptor channel
    • DOI 10.1126/science.280.5369.1596
    • Rosenmund, C., Stern-Bach, Y. & Stevens, C. F. The tetrameric structure of a glutamate receptor channel. Science 280, 1596-1599 (1998). (Pubitemid 28277703)
    • (1998) Science , vol.280 , Issue.5369 , pp. 1596-1599
    • Rosenmund, C.1    Stern-Bach, Y.2    Stevens, C.F.3
  • 38
    • 0033623299 scopus 로고    scopus 로고
    • Concentration-dependent substate behavior of native AMPA receptors
    • Smith, T. C. & Howe, J. R. Concentration-dependent substate behavior of native AMPA receptors. Nat. Neurosci. 3, 992-997 (2000).
    • (2000) Nat. Neurosci. , vol.3 , pp. 992-997
    • Smith, T.C.1    Howe, J.R.2
  • 39
    • 81855193749 scopus 로고    scopus 로고
    • Distinct functional roles of subunits within the heteromeric kainate receptor
    • Fisher, J. L. & Mott, D. D. Distinct functional roles of subunits within the heteromeric kainate receptor. J. Neurosci. 31, 17113-17122 (2011).
    • (2011) J. Neurosci. , vol.31 , pp. 17113-17122
    • Fisher, J.L.1    Mott, D.D.2
  • 40
    • 0025082936 scopus 로고
    • A kinetic analysis of the modulation of N-methyl-D-aspartic acid receptors by glycine in mouse cultured hippocampal neurones
    • Benveniste, M., Clements, J., Vyklický, Jr L. & Mayer, M. L. A kinetic analysis of the modulation of N-methyl-D-aspartic acid receptors by glycine in mouse cultured hippocampal neurones. J Physiol. 428, 333-357 (1990). (Pubitemid 20313660)
    • (1990) Journal of Physiology , vol.428 , pp. 333-357
    • Benveniste, M.1    Clements, J.2    Vyklicky Jr., L.3    Mayer, M.L.4
  • 41
    • 84866320347 scopus 로고    scopus 로고
    • Probing the activation sequence of NMDA receptors with lurcher mutations
    • Murthy, S. E., Shogan, T., Page, J. C., Kasperek, E. M. & Popescu, G. K. Probing the activation sequence of NMDA receptors with lurcher mutations. J. Gen. Physiol. 140, 267-277 (2012).
    • (2012) J. Gen. Physiol. , vol.140 , pp. 267-277
    • Murthy, S.E.1    Shogan, T.2    Page, J.C.3    Kasperek, E.M.4    Popescu, G.K.5
  • 42
    • 0028559605 scopus 로고
    • Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
    • Stern-Bach, Y. et al. Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins. Neuron 13, 1345-1357 (1994).
    • (1994) Neuron , vol.13 , pp. 1345-1357
    • Stern-Bach, Y.1
  • 43
    • 0034884750 scopus 로고    scopus 로고
    • Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions
    • DOI 10.1016/S0896-6273(01)00333-6
    • Ayalon, G. & Stern-Bach, Y. Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions. Neuron 31, 103-113 (2001). (Pubitemid 32757092)
    • (2001) Neuron , vol.31 , Issue.1 , pp. 103-113
    • Ayalon, G.1    Stern-Bach, Y.2
  • 44
    • 84861944383 scopus 로고    scopus 로고
    • Coupled control of desensitization and gating by the ligand binding domain of glutamate receptors
    • Carbone, A. L. & Plested, A. J. Coupled control of desensitization and gating by the ligand binding domain of glutamate receptors. Neuron 74, 845-857 (2012).
    • (2012) Neuron , vol.74 , pp. 845-857
    • Carbone, A.L.1    Plested, A.J.2
  • 45
    • 66649086928 scopus 로고    scopus 로고
    • Mechanism of differential control of NMDA receptor activity by NR2 subunits
    • Gielen, M., Siegler Retchless, B., Mony, L., Johnson, J. W. & Paoletti, P. Mechanism of differential control of NMDA receptor activity by NR2 subunits. Nature 459, 703-707 (2009).
    • (2009) Nature , vol.459 , pp. 703-707
    • Gielen, M.1    Siegler Retchless, B.2    Mony, L.3    Johnson, J.W.4    Paoletti, P.5
  • 46
    • 70349610345 scopus 로고    scopus 로고
    • Control of NMDA receptor function by the NR2 subunit amino-terminal domain
    • Yuan, H., Hansen, K. B., Vance, K. M., Ogden, K. K. & Traynelis, S. F. Control of NMDA receptor function by the NR2 subunit amino-terminal domain. J. Neurosci. 29, 12045-12058 (2009).
    • (2009) J. Neurosci. , vol.29 , pp. 12045-12058
    • Yuan, H.1    Hansen, K.B.2    Vance, K.M.3    Ogden, K.K.4    Traynelis, S.F.5
  • 47
    • 0030777076 scopus 로고    scopus 로고
    • Identification of amino acid residues that control functional behavior in GluR5 and GluR6 kainate receptors
    • DOI 10.1016/S0896-6273(00)80972-1
    • Swanson, G. T., Gereau, 4th R. W., Green, T. & Heinemann, S. F. Identification of amino acid residues that control functional behavior in GluR5 and GluR6 kainate receptors. Neuron 19, 913-926 (1997). (Pubitemid 27471395)
    • (1997) Neuron , vol.19 , Issue.4 , pp. 913-926
    • Swanson, G.T.1    Gereau IV, R.W.2    Green, T.3    Heinemann, S.F.4
  • 48
    • 0032403241 scopus 로고    scopus 로고
    • Inhibition of rat neuronal kainate receptors by cis-unsaturated fatty acids
    • Wilding, T. J., Chai, Y. H. & Huettner, J. E. Inhibition of rat neuronal kainate receptors by cis-unsaturated fatty acids. J. Physiol. 513, 331-339 (1998). (Pubitemid 28562952)
    • (1998) Journal of Physiology , vol.513 , Issue.2 , pp. 331-339
    • Wilding, T.J.1    Chai, Y.H.2    Huettner, J.E.3
  • 49
    • 48749087539 scopus 로고    scopus 로고
    • Amino acid substitutions in the pore helix of GluR6 control inhibition by membrane fatty acids
    • Wilding, T. J., Fulling, E., Zhou, Y. & Huettner, J. E. Amino acid substitutions in the pore helix of GluR6 control inhibition by membrane fatty acids. J. Gen. Physiol. 132, 85-99 (2008).
    • (2008) J. Gen. Physiol. , vol.132 , pp. 85-99
    • Wilding, T.J.1    Fulling, E.2    Zhou, Y.3    Huettner, J.E.4
  • 50
    • 0028353272 scopus 로고
    • Arachidonic acid depresses non-NMDA receptor currents
    • Kovalchuk, Y., Miller, B., Sarantis, M. & Attwell, D. Arachidonic acid depresses non-NMDA receptor currents. Brain Res. 643, 287-295 (1994). (Pubitemid 24115103)
    • (1994) Brain Research , vol.643 , Issue.1-2 , pp. 287-295
    • Kovalchuk, Y.1    Miller, B.2    Sarantis, M.3    Attwell, D.4
  • 51
    • 0032404197 scopus 로고    scopus 로고
    • Opposite modulation of NMDA receptors by lysophospholipids and arachidonic acid: Common features with mechanosensitivity
    • Casado, M. & Ascher, P. Opposite modulation of NMDA receptors by lysophospholipids and arachidonic acid: common features with mechanosensitivity. J. Physiol. 513, 317-330 (1998). (Pubitemid 28562951)
    • (1998) Journal of Physiology , vol.513 , Issue.2 , pp. 317-330
    • Casado, M.1    Ascher, P.2
  • 52
    • 79960417429 scopus 로고    scopus 로고
    • Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors
    • Karakas, E., Simorowski, N. & Furukawa, H. Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors. Nature 475, 249-253 (2011).
    • (2011) Nature , vol.475 , pp. 249-253
    • Karakas, E.1    Simorowski, N.2    Furukawa, H.3
  • 53
    • 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. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28, 165-181 (2000).
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 54
    • 84878156213 scopus 로고    scopus 로고
    • An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions
    • Dai, J. & Zhou, H. X. An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions. Biophys. J. 104, 2170-2181 (2013).
    • (2013) Biophys. J. , vol.104 , pp. 2170-2181
    • Dai, J.1    Zhou, H.X.2
  • 55
    • 0033209590 scopus 로고    scopus 로고
    • Enzyme-free cloning: A rapid method to clone PCR products independent of vector restriction enzyme sites
    • Tillett, D. & Neilan, B. A. Enzyme-free cloning: a rapid method to clone PCR products independent of vector restriction enzyme sites. Nucleic Acids Res. 27, e26 (1999).
    • (1999) Nucleic Acids Res. , vol.27
    • Tillett, D.1    Neilan, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.