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Volumn 20, Issue 4, 2013, Pages 477-485

Allosteric signaling and dynamics of the clamshell-like NMDA receptor GluN1 N-terminal domain

Author keywords

[No Author keywords available]

Indexed keywords

GLUN1 PROTEIN; GLUN2 PROTEIN; GLUTAMIC ACID; GLYCINE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; UNCLASSIFIED DRUG;

EID: 84876183319     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2522     Document Type: Article
Times cited : (58)

References (57)
  • 1
    • 33544461370 scopus 로고    scopus 로고
    • The Venus fytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors
    • Felder, C.B., Graul, R.C., Lee, A.Y., Merkle, H.P. & Sadee, W. The Venus fytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors. AAPS PharmSci 1, E2 (1999).
    • (1999) AAPS PharmSci , vol.1
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 2
    • 20344362178 scopus 로고    scopus 로고
    • Amino acid recognition by Venus fytrap domains is encoded in an 8-residue motif
    • Acher, F.C. & Bertrand, H.O. Amino acid recognition by Venus fytrap domains is encoded in an 8-residue motif. Biopolymers 80, 357-366 (2005).
    • (2005) Biopolymers , vol.80 , pp. 357-366
    • Acher, F.C.1    Bertrand, H.O.2
  • 3
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specifcity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F.A. & Ledvina, P.S. Atomic structure and specifcity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 20, 17-25 (1996).
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 4
    • 0033576612 scopus 로고    scopus 로고
    • Functional characterization of a potassium-selective prokaryotic glutamate receptor
    • Chen, G.Q., Cui, C., Mayer, M.L. & Gouaux, E. Functional characterization of a potassium-selective prokaryotic glutamate receptor. Nature 402, 817-821 (1999).
    • (1999) Nature , vol.402 , pp. 817-821
    • Chen, G.Q.1    Cui, C.2    Mayer, M.L.3    Gouaux, E.4
  • 6
    • 78149497839 scopus 로고    scopus 로고
    • The complexity of their activation mechanism opens new possibilities for the modulation of mGlu and GABAB class C G protein-coupled receptors
    • Rondard, P., Goudet, C., Kniazeff, J., Pin, J.P. & Prezeau, L. The complexity of their activation mechanism opens new possibilities for the modulation of mGlu and GABAB class C G protein-coupled receptors. Neuropharmacology 60, 82-92 (2011).
    • (2011) Neuropharmacology , vol.60 , pp. 82-92
    • Rondard, P.1    Goudet, C.2    Kniazeff, J.3    Pin, J.P.4    Prezeau, L.5
  • 7
    • 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
  • 8
    • 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
  • 9
    • 77952362034 scopus 로고    scopus 로고
    • Domain organization and function in GluK2 subtype kainate receptors
    • Das, U., Kumar, J., Mayer, M.L. & Plested, A.J. Domain organization and function in GluK2 subtype kainate receptors. Proc. Natl. Acad. Sci. USA 107, 8463-8468 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8463-8468
    • Das, U.1    Kumar, J.2    Mayer, M.L.3    Plested, A.J.4
  • 10
    • 33645321641 scopus 로고    scopus 로고
    • Glutamate receptors at atomic resolution
    • Mayer, M.L. Glutamate receptors at atomic resolution. Nature 440, 456-462 (2006).
    • (2006) Nature , vol.440 , pp. 456-462
    • Mayer, M.L.1
  • 11
    • 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
  • 12
    • 17644417156 scopus 로고    scopus 로고
    • Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specifc receptor assembly
    • Ayalon, G., Segev, E., Elgavish, S. & Stern-Bach, Y. Two regions in the N-terminal domain of ionotropic glutamate receptor 3 form the subunit oligomerization interfaces that control subtype-specifc receptor assembly. J. Biol. Chem. 280, 15053-15060 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 15053-15060
    • Ayalon, G.1    Segev, E.2    Elgavish, S.3    Stern-Bach, Y.4
  • 13
    • 67649565613 scopus 로고    scopus 로고
    • Crystal structure and association behaviour of the GluR2 amino-terminal domain
    • Jin, R. et al. Crystal structure and association behaviour of the GluR2 amino-terminal domain. EMBO J. 28, 1812-1823 (2009).
    • (2009) EMBO J. , vol.28 , pp. 1812-1823
    • Jin, R.1
  • 14
    • 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
  • 15
    • 79952280700 scopus 로고    scopus 로고
    • Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers
    • Rossmann, M. et al. Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers. EMBO J. 30, 959-971 (2011).
    • (2011) EMBO J. , vol.30 , pp. 959-971
    • Rossmann, M.1
  • 16
    • 79960652046 scopus 로고    scopus 로고
    • Structure and assembly mechanism for heteromeric kainate receptors
    • Kumar, J., Schuck, P. & Mayer, M.L. Structure and assembly mechanism for heteromeric kainate receptors. Neuron 71, 319-331 (2011).
    • (2011) Neuron , vol.71 , pp. 319-331
    • Kumar, J.1    Schuck, P.2    Mayer, M.L.3
  • 17
    • 79954630544 scopus 로고    scopus 로고
    • Molecular basis of NMDA receptor functional diversity
    • Paoletti, P. Molecular basis of NMDA receptor functional diversity. Eur. J. Neurosci. 33, 1351-1365 (2011).
    • (2011) Eur. J. Neurosci. , vol.33 , pp. 1351-1365
    • Paoletti, P.1
  • 18
    • 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
  • 19
    • 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
  • 20
    • 72449151659 scopus 로고    scopus 로고
    • Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit
    • Karakas, E., Simorowski, N. & Furukawa, H. Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit. EMBO J. 28, 3910-3920 (2009).
    • (2009) EMBO J. , vol.28 , pp. 3910-3920
    • Karakas, E.1    Simorowski, N.2    Furukawa, H.3
  • 21
    • 79952399129 scopus 로고    scopus 로고
    • Separation of domain contacts is required for heterotetrameric assembly of functional NMDA receptors
    • Farina, A.N. et al. Separation of domain contacts is required for heterotetrameric assembly of functional NMDA receptors. J. Neurosci. 31, 3565-3579 (2011).
    • (2011) J. Neurosci. , vol.31 , pp. 3565-3579
    • Farina, A.N.1
  • 22
    • 78149495223 scopus 로고    scopus 로고
    • Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain
    • Stroebel, D., Carvalho, S. & Paoletti, P. Functional evidence for a twisted conformation of the NMDA receptor GluN2A subunit N-terminal domain. Neuropharmacology 60, 151-158 (2011).
    • (2011) Neuropharmacology , vol.60 , pp. 151-158
    • Stroebel, D.1    Carvalho, S.2    Paoletti, P.3
  • 23
    • 0025162702 scopus 로고
    • A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specifcity. Sugar-binding and crystallographic studies
    • Vermersch, P.S., Tesmer, J.J., Lemon, D.D. & Quiocho, F.A. A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specifcity. Sugar-binding and crystallographic studies. J. Biol. Chem. 265, 16592-16603 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 16592-16603
    • Vermersch, P.S.1    Tesmer, J.J.2    Lemon, D.D.3    Quiocho, F.A.4
  • 24
    • 0034863015 scopus 로고    scopus 로고
    • Manipulation of ligand binding affnity by exploitation of conformational coupling
    • Marvin, J.S. & Hellinga, H.W. Manipulation of ligand binding affnity by exploitation of conformational coupling. Nat. Struct. Biol. 8, 795-798 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 795-798
    • Marvin, J.S.1    Hellinga, H.W.2
  • 25
    • 0141446029 scopus 로고    scopus 로고
    • Insights into the conformational equilibria of maltose-binding protein by analysis of high affnity mutants
    • Telmer, P.G. & Shilton, B.H. Insights into the conformational equilibria of maltose-binding protein by analysis of high affnity mutants. J. Biol. Chem. 278, 34555-34567 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 34555-34567
    • Telmer, P.G.1    Shilton, B.H.2
  • 26
    • 0242331659 scopus 로고    scopus 로고
    • The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fuorescence spectroscopy
    • Millet, O., Hudson, R.P. & Kay, L.E. The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fuorescence spectroscopy. Proc. Natl. Acad. Sci. USA 100, 12700-12705 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12700-12705
    • Millet, O.1    Hudson, R.P.2    Kay, L.E.3
  • 27
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • Dwyer, M.A. & Hellinga, H.W. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr. Opin. Struct. Biol. 14, 495-504 (2004).
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 28
    • 0027427564 scopus 로고
    • Nonuniform probability of glutamate release at a hippocampal synapse
    • Rosenmund, C., Clements, J.D. & Westbrook, G.L. Nonuniform probability of glutamate release at a hippocampal synapse. Science 262, 754-757 (1993).
    • (1993) Science , vol.262 , pp. 754-757
    • Rosenmund, C.1    Clements, J.D.2    Westbrook, G.L.3
  • 29
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specifcity: Crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa, H. & Gouaux, E. Mechanisms of activation, inhibition and specifcity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22, 2873-2885 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 30
    • 0028034803 scopus 로고
    • Identifcation of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor
    • Sullivan, J.M. et al. Identifcation of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor. Neuron 13, 929-936 (1994).
    • (1994) Neuron , vol.13 , pp. 929-936
    • Sullivan, J.M.1
  • 31
    • 70350324907 scopus 로고    scopus 로고
    • Allosteric modulators of NR2B-containing NMDA receptors: Molecular mechanisms and therapeutic potential
    • Mony, L., Kew, J.N., Gunthorpe, M.J. & Paoletti, P. Allosteric modulators of NR2B-containing NMDA receptors: molecular mechanisms and therapeutic potential. Br. J. Pharmacol. 157, 1301-1317 (2009).
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 1301-1317
    • Mony, L.1    Kew, J.N.2    Gunthorpe, M.J.3    Paoletti, P.4
  • 32
    • 37549045649 scopus 로고    scopus 로고
    • Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition
    • Gielen, M. et al. Structural rearrangements of NR1/NR2A NMDA receptors during allosteric inhibition. Neuron 57, 80-93 (2008).
    • (2008) Neuron , vol.57 , pp. 80-93
    • Gielen, M.1
  • 33
    • 79961020657 scopus 로고    scopus 로고
    • Molecular basis of positive allosteric modulation of GluN2B NMDA receptors by polyamines
    • Mony, L., Zhu, S., Carvalho, S. & Paoletti, P. Molecular basis of positive allosteric modulation of GluN2B NMDA receptors by polyamines. EMBO J. 30, 3134-3146 (2011).
    • (2011) EMBO J. , vol.30 , pp. 3134-3146
    • Mony, L.1    Zhu, S.2    Carvalho, S.3    Paoletti, P.4
  • 34
    • 0027525324 scopus 로고
    • Ifenprodil discriminates subtypes of the N-methyl-d-aspartate receptor: Selectivity and mechanisms at recombinant heteromeric receptors
    • Williams, K. Ifenprodil discriminates subtypes of the N-methyl-d-aspartate receptor: selectivity and mechanisms at recombinant heteromeric receptors. Mol. Pharmacol. 44, 851-859 (1993).
    • (1993) Mol. Pharmacol. , vol.44 , pp. 851-859
    • Williams, K.1
  • 36
    • 12144271737 scopus 로고    scopus 로고
    • Protons trap NR1/NR2B NMDA receptors in a nonconducting state
    • Banke, T.G., Dravid, S.M. & Traynelis, S.F. Protons trap NR1/NR2B NMDA receptors in a nonconducting state. J. Neurosci. 25, 42-51 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 42-51
    • Banke, T.G.1    Dravid, S.M.2    Traynelis, S.F.3
  • 37
    • 79955525364 scopus 로고    scopus 로고
    • Amino terminal domains of the NMDA receptor are organized as local heterodimers
    • Lee, C.H. & Gouaux, E. Amino terminal domains of the NMDA receptor are organized as local heterodimers. PLoS ONE 6, e19180 (2011).
    • (2011) PLoS ONE , vol.6
    • Lee, C.H.1    Gouaux, E.2
  • 38
    • 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. Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor. Cell 127, 85-97 (2006).
    • (2006) Cell , vol.127 , pp. 85-97
    • Armstrong, N.1    Jasti, J.2    Beich-Frandsen, M.3    Gouaux, E.4
  • 39
    • 0034867583 scopus 로고    scopus 로고
    • Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A
    • Zheng, F. et al. Allosteric interaction between the amino terminal domain and the ligand binding domain of NR2A. Nat. Neurosci. 4, 894-901 (2001).
    • (2001) Nat. Neurosci. , vol.4 , pp. 894-901
    • Zheng, F.1
  • 40
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • Bahar, I. & Rader, A.J. Coarse-grained normal mode analysis in structural biology. Curr. Opin. Struct. Biol. 15, 586-592 (2005).
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 41
    • 22244438519 scopus 로고    scopus 로고
    • Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism
    • Taly, A. et al. Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism. Biophys. J. 88, 3954-3965 (2005).
    • (2005) Biophys. J. , vol.88 , pp. 3954-3965
    • Taly, A.1
  • 42
    • 84860540831 scopus 로고    scopus 로고
    • Tightening of the ATP-binding sites induces the opening of P2X receptor channels
    • Jiang, R. et al. Tightening of the ATP-binding sites induces the opening of P2X receptor channels. EMBO J. 31, 2134-2143 (2012).
    • (2012) EMBO J. , vol.31 , pp. 2134-2143
    • Jiang, R.1
  • 43
    • 84868571307 scopus 로고    scopus 로고
    • Comparative dynamics of NMDA-and AMPA-glutamate receptor N-terminal domains
    • Dutta, A., Shrivastava, I.H., Sukumaran, M., Greger, I.H. & Bahar, I. Comparative dynamics of NMDA-and AMPA-glutamate receptor N-terminal domains. Structure 20, 1838-1849 (2012).
    • (2012) Structure , vol.20 , pp. 1838-1849
    • Dutta, A.1    Shrivastava, I.H.2    Sukumaran, M.3    Greger, I.H.4    Bahar, I.5
  • 44
    • 84863885062 scopus 로고    scopus 로고
    • Mapping the binding of GluN2B-selective NMDA receptor negative allosteric modulators
    • Burger, P.B. et al. Mapping the binding of GluN2B-selective NMDA receptor negative allosteric modulators. 82, 344-359. Mol. Pharmacol. (2012).
    • (2012) Mol. Pharmacol. , vol.82 , pp. 344-359
    • Burger, P.B.1
  • 45
    • 78549248799 scopus 로고    scopus 로고
    • Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains
    • Kumar, J. & Mayer, M.L. Crystal structures of the glutamate receptor ion channel GluK3 and GluK5 amino-terminal domains. J. Mol. Biol. 404, 680-696 (2010).
    • (2010) J. Mol. Biol. , vol.404 , pp. 680-696
    • Kumar, J.1    Mayer, M.L.2
  • 46
    • 75349094219 scopus 로고    scopus 로고
    • Enhanced effcacy without further cleft closure: Reevaluating twist as a source of agonist effcacy in AMPA receptors
    • Birdsey-Benson, A., Gill, A., Henderson, L.P. & Madden, D.R. Enhanced effcacy without further cleft closure: reevaluating twist as a source of agonist effcacy in AMPA receptors. J. Neurosci. 30, 1463-1470 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 1463-1470
    • Birdsey-Benson, A.1    Gill, A.2    Henderson, L.P.3    Madden, D.R.4
  • 47
    • 67349285101 scopus 로고    scopus 로고
    • The N-terminal domain of GluR6-subtype glutamate receptor ion channels
    • Kumar, J., Schuck, P., Jin, R. & Mayer, M.L. The N-terminal domain of GluR6-subtype glutamate receptor ion channels. Nat. Struct. Mol. Biol. 16, 631-638 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 631-638
    • Kumar, J.1    Schuck, P.2    Jin, R.3    Mayer, M.L.4
  • 48
    • 70149087712 scopus 로고    scopus 로고
    • Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate Receptors
    • Clayton, A. et al. Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate Receptors. J. Mol. Biol. 392, 1125-1132 (2009).
    • (2009) J. Mol. Biol. , vol.392 , pp. 1125-1132
    • Clayton, A.1
  • 49
    • 79952281882 scopus 로고    scopus 로고
    • Dynamics and allosteric potential of the AMPA receptor N-terminal domain
    • Sukumaran, M. et al. Dynamics and allosteric potential of the AMPA receptor N-terminal domain. EMBO J. 30, 972-982 (2011).
    • (2011) EMBO J. , vol.30 , pp. 972-982
    • Sukumaran, M.1
  • 50
    • 81055140191 scopus 로고    scopus 로고
    • Intrinsic motions in the N-terminal domain of an ionotropic glutamate receptor detected by fuorescence correlation spectroscopy
    • Jensen, M.H., Sukumaran, M., Johnson, C.M., Greger, I.H. & Neuweiler, H. Intrinsic motions in the N-terminal domain of an ionotropic glutamate receptor detected by fuorescence correlation spectroscopy. J. Mol. Biol. 414, 96-105 (2011).
    • (2011) J. Mol. Biol. , vol.414 , pp. 96-105
    • Jensen, M.H.1    Sukumaran, M.2    Johnson, C.M.3    Greger, I.H.4    Neuweiler, H.5
  • 51
    • 70349320394 scopus 로고    scopus 로고
    • AMPA receptor ligand binding domain mobility revealed by functional cross linking
    • Plested, A.J. & Mayer, M.L. AMPA receptor ligand binding domain mobility revealed by functional cross linking. J. Neurosci. 29, 11912-11923 (2009).
    • (2009) J. Neurosci. , vol.29 , pp. 11912-11923
    • Plested, A.J.1    Mayer, M.L.2
  • 52
    • 0035924573 scopus 로고    scopus 로고
    • Intersubunit cooperativity in the NMDA receptor
    • Regalado, M.P., Villarroel, A. & Lerma, J. Intersubunit cooperativity in the NMDA receptor. Neuron 32, 1085-1096 (2001).
    • (2001) Neuron , vol.32 , pp. 1085-1096
    • Regalado, M.P.1    Villarroel, A.2    Lerma, J.3
  • 54
    • 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
  • 55
    • 0033635736 scopus 로고    scopus 로고
    • EphB receptors interact with NMDA receptors and regulate excitatory synapse formation
    • Dalva, M.B. et al. EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. Cell 103, 945-956 (2000).
    • (2000) Cell , vol.103 , pp. 945-956
    • Dalva, M.B.1
  • 56
    • 33846809197 scopus 로고    scopus 로고
    • Paraneoplastic anti-N-methyl-d-aspartate receptor encephalitis associated with ovarian teratoma
    • Dalmau, J. et al. Paraneoplastic anti-N-methyl-d-aspartate receptor encephalitis associated with ovarian teratoma. Ann. Neurol. 61, 25-36 (2007).
    • (2007) Ann. Neurol. , vol.61 , pp. 25-36
    • Dalmau, J.1
  • 57
    • 55549135314 scopus 로고    scopus 로고
    • Anti-NMDA-receptor encephalitis: Case series and analysis of the effects of antibodies
    • Dalmau, J. et al. Anti-NMDA-receptor encephalitis: case series and analysis of the effects of antibodies. Lancet Neurol. 7, 1091-1098 (2008).
    • (2008) Lancet Neurol. , vol.7 , pp. 1091-1098
    • Dalmau, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.