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Volumn 48, Issue 4, 2011, Pages 308-320

Mechanisms underlying NMDA receptor synaptic/extrasynaptic distribution and function

Author keywords

Extrasynaptic; Lateral diffusion; Neurodegenerative disease; NMDA receptor; Phosphorylation; Signaling

Indexed keywords

CALPAIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR;

EID: 79961168563     PISSN: 10447431     EISSN: 10959327     Source Type: Journal    
DOI: 10.1016/j.mcn.2011.05.001     Document Type: Review
Times cited : (159)

References (235)
  • 2
    • 0035369919 scopus 로고    scopus 로고
    • NMDA receptor regulation by Src kinase signalling in excitatory synaptic transmission and plasticity
    • Ali D.W., Salter M.W. NMDA receptor regulation by Src kinase signalling in excitatory synaptic transmission and plasticity. Curr. Opin. Neurobiol. 2001, 11:336-342.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 336-342
    • Ali, D.W.1    Salter, M.W.2
  • 3
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors
    • Allison D.W., Gelfand V.I., Spector I., Craig A.M. Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J. Neurosci. 1998, 18:2423-2436.
    • (1998) J. Neurosci. , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 4
    • 21244447454 scopus 로고    scopus 로고
    • Neuronal vulnerability in mouse models of Huntington's disease: membrane channel protein changes
    • Ariano M.A., Wagle N., Grissell A.E. Neuronal vulnerability in mouse models of Huntington's disease: membrane channel protein changes. J. Neurosci. Res. 2005, 80:634-645.
    • (2005) J. Neurosci. Res. , vol.80 , pp. 634-645
    • Ariano, M.A.1    Wagle, N.2    Grissell, A.E.3
  • 5
    • 0042536473 scopus 로고    scopus 로고
    • Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity
    • Arundine M., Tymianski M. Molecular mechanisms of calcium-dependent neurodegeneration in excitotoxicity. Cell Calcium 2003, 34:325-337.
    • (2003) Cell Calcium , vol.34 , pp. 325-337
    • Arundine, M.1    Tymianski, M.2
  • 7
    • 0037130451 scopus 로고    scopus 로고
    • Subunit-specific NMDA receptor trafficking to synapses
    • Barria A., Malinow R. Subunit-specific NMDA receptor trafficking to synapses. Neuron 2002, 35:345-353.
    • (2002) Neuron , vol.35 , pp. 345-353
    • Barria, A.1    Malinow, R.2
  • 8
    • 68049124955 scopus 로고    scopus 로고
    • Neuroligin1: a cell adhesion molecule that recruits PSD-95 and NMDA receptors by distinct mechanisms during synaptogenesis
    • Barrow S.L., Constable J.R., Clark E., El-Sabeawy F., McAllister A.K., Washbourne P. Neuroligin1: a cell adhesion molecule that recruits PSD-95 and NMDA receptors by distinct mechanisms during synaptogenesis. Neural Dev. 2009, 4:17.
    • (2009) Neural Dev. , vol.4 , pp. 17
    • Barrow, S.L.1    Constable, J.R.2    Clark, E.3    El-Sabeawy, F.4    McAllister, A.K.5    Washbourne, P.6
  • 9
    • 33847162742 scopus 로고    scopus 로고
    • The interaction between Stargazin and PSD-95 regulates AMPA receptor surface trafficking
    • Bats C., Groc L., Choquet D. The interaction between Stargazin and PSD-95 regulates AMPA receptor surface trafficking. Neuron 2007, 53:719-734.
    • (2007) Neuron , vol.53 , pp. 719-734
    • Bats, C.1    Groc, L.2    Choquet, D.3
  • 10
    • 0022446150 scopus 로고
    • Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid
    • Beal M.F., Kowall N.W., Ellison D.W., Mazurek M.F., Swartz K.J., Martin J.B. Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature 1986, 321:168-171.
    • (1986) Nature , vol.321 , pp. 168-171
    • Beal, M.F.1    Kowall, N.W.2    Ellison, D.W.3    Mazurek, M.F.4    Swartz, K.J.5    Martin, J.B.6
  • 11
    • 0025122066 scopus 로고
    • Homocysteic acid lesions in rat striatum spare somatostatin-neuropeptide Y (NADPH-diaphorase) neurons
    • Beal M.F., Kowall N.W., Swartz K.J., Ferrante R.J. Homocysteic acid lesions in rat striatum spare somatostatin-neuropeptide Y (NADPH-diaphorase) neurons. Neurosci. Lett. 1990, 108:36-42.
    • (1990) Neurosci. Lett. , vol.108 , pp. 36-42
    • Beal, M.F.1    Kowall, N.W.2    Swartz, K.J.3    Ferrante, R.J.4
  • 13
    • 34548218356 scopus 로고    scopus 로고
    • Rapid bidirectional switching of synaptic NMDA receptors
    • Bellone C., Nicoll R.A. Rapid bidirectional switching of synaptic NMDA receptors. Neuron 2007, 55:779-785.
    • (2007) Neuron , vol.55 , pp. 779-785
    • Bellone, C.1    Nicoll, R.A.2
  • 14
    • 0034714267 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of NR2 subunits of N-methyl-d-aspartate receptors protects from calpain-mediated truncation of their C-terminal domains
    • Bi R., Rong Y., Bernard A., Khrestchatisky M., Baudry M. Src-mediated tyrosine phosphorylation of NR2 subunits of N-methyl-d-aspartate receptors protects from calpain-mediated truncation of their C-terminal domains. J. Biol. Chem. 2000, 275:26477-26483.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26477-26483
    • Bi, R.1    Rong, Y.2    Bernard, A.3    Khrestchatisky, M.4    Baudry, M.5
  • 15
    • 0037168123 scopus 로고    scopus 로고
    • Dynamics and regulation of clathrin coats at specialized endocytic zones of dendrites and spines
    • Blanpied T.A., Scott D.B., Ehlers M.D. Dynamics and regulation of clathrin coats at specialized endocytic zones of dendrites and spines. Neuron 2002, 36:435-449.
    • (2002) Neuron , vol.36 , pp. 435-449
    • Blanpied, T.A.1    Scott, D.B.2    Ehlers, M.D.3
  • 16
    • 0027476024 scopus 로고
    • A synaptic model of memory: long-term potentiation in the hippocampus
    • Bliss T.V., Collingridge G.L. A synaptic model of memory: long-term potentiation in the hippocampus. Nature 1993, 361:31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.1    Collingridge, G.L.2
  • 17
    • 0035955643 scopus 로고    scopus 로고
    • Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin
    • Bockers T.M., Mameza M.G., Kreutz M.R., Bockmann J., Weise C., Buck F., Richter D., Gundelfinger E.D., Kreienkamp H.J. Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin. J. Biol. Chem. 2001, 276:40104-40112.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40104-40112
    • Bockers, T.M.1    Mameza, M.G.2    Kreutz, M.R.3    Bockmann, J.4    Weise, C.5    Buck, F.6    Richter, D.7    Gundelfinger, E.D.8    Kreienkamp, H.J.9
  • 18
    • 78649417803 scopus 로고    scopus 로고
    • Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid-ss production
    • Bordji K., Becerril-Ortega J., Nicole O., Buisson A. Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid-ss production. J. Neurosci. 2010, 30:15927-15942.
    • (2010) J. Neurosci. , vol.30 , pp. 15927-15942
    • Bordji, K.1    Becerril-Ortega, J.2    Nicole, O.3    Buisson, A.4
  • 21
    • 0036828497 scopus 로고    scopus 로고
    • NMDA-receptor trafficking and targeting: implications for synaptic transmission and plasticity
    • Carroll R.C., Zukin R.S. NMDA-receptor trafficking and targeting: implications for synaptic transmission and plasticity. Trends Neurosci. 2002, 25:571-577.
    • (2002) Trends Neurosci. , vol.25 , pp. 571-577
    • Carroll, R.C.1    Zukin, R.S.2
  • 22
    • 0034659742 scopus 로고    scopus 로고
    • Prolonged synaptic currents and glutamate spillover at the parallel fiber to stellate cell synapse
    • Carter A.G., Regehr W.G. Prolonged synaptic currents and glutamate spillover at the parallel fiber to stellate cell synapse. J. Neurosci. 2000, 20:4423-4434.
    • (2000) J. Neurosci. , vol.20 , pp. 4423-4434
    • Carter, A.G.1    Regehr, W.G.2
  • 24
    • 77957147338 scopus 로고    scopus 로고
    • Genetic mouse models of Huntington's disease: focus on electrophysiological mechanisms
    • Cepeda C., Cummings D.M., Andre V.M., Holley S.M., Levine M.S. Genetic mouse models of Huntington's disease: focus on electrophysiological mechanisms. ASN Neuro 2010, 2:e00033.
    • (2010) ASN Neuro , vol.2
    • Cepeda, C.1    Cummings, D.M.2    Andre, V.M.3    Holley, S.M.4    Levine, M.S.5
  • 25
    • 0035902139 scopus 로고    scopus 로고
    • Integrins mediate functional pre- and postsynaptic maturation at a hippocampal synapse
    • Chavis P., Westbrook G. Integrins mediate functional pre- and postsynaptic maturation at a hippocampal synapse. Nature 2001, 411:317-321.
    • (2001) Nature , vol.411 , pp. 317-321
    • Chavis, P.1    Westbrook, G.2
  • 26
    • 34547664721 scopus 로고    scopus 로고
    • Regulation of NMDA receptors by phosphorylation
    • Chen B.S., Roche K.W. Regulation of NMDA receptors by phosphorylation. Neuropharmacology 2007, 53:362-368.
    • (2007) Neuropharmacology , vol.53 , pp. 362-368
    • Chen, B.S.1    Roche, K.W.2
  • 27
    • 33745034018 scopus 로고    scopus 로고
    • The chemical biology of clinically tolerated NMDA receptor antagonists
    • Chen H.S., Lipton S.A. The chemical biology of clinically tolerated NMDA receptor antagonists. J. Neurochem. 2006, 97:1611-1626.
    • (2006) J. Neurochem. , vol.97 , pp. 1611-1626
    • Chen, H.S.1    Lipton, S.A.2
  • 28
    • 0032543788 scopus 로고    scopus 로고
    • Neuroprotective concentrations of the N-methyl-d-aspartate open-channel blocker memantine are effective without cytoplasmic vacuolation following post-ischemic administration and do not block maze learning or long-term potentiation
    • Chen H.S., Wang Y.F., Rayudu P.V., Edgecomb P., Neill J.C., Segal M.M., Lipton S.A., Jensen F.E. Neuroprotective concentrations of the N-methyl-d-aspartate open-channel blocker memantine are effective without cytoplasmic vacuolation following post-ischemic administration and do not block maze learning or long-term potentiation. Neuroscience 1998, 86:1121-1132.
    • (1998) Neuroscience , vol.86 , pp. 1121-1132
    • Chen, H.S.1    Wang, Y.F.2    Rayudu, P.V.3    Edgecomb, P.4    Neill, J.C.5    Segal, M.M.6    Lipton, S.A.7    Jensen, F.E.8
  • 29
    • 0037088916 scopus 로고    scopus 로고
    • Synaptically released glutamate activates extrasynaptic NMDA receptors on cells in the ganglion cell layer of rat retina
    • Chen S., Diamond J.S. Synaptically released glutamate activates extrasynaptic NMDA receptors on cells in the ganglion cell layer of rat retina. J. Neurosci. 2002, 22:2165-2173.
    • (2002) J. Neurosci. , vol.22 , pp. 2165-2173
    • Chen, S.1    Diamond, J.S.2
  • 30
    • 34548445136 scopus 로고    scopus 로고
    • Neuronal morphogenesis is regulated by the interplay between cyclin-dependent kinase 5 and the ubiquitin ligase mind bomb 1
    • Choe E.A., Liao L., Zhou J.Y., Cheng D., Duong D.M., Jin P., Tsai L.H., Peng J. Neuronal morphogenesis is regulated by the interplay between cyclin-dependent kinase 5 and the ubiquitin ligase mind bomb 1. J. Neurosci. 2007, 27:9503-9512.
    • (2007) J. Neurosci. , vol.27 , pp. 9503-9512
    • Choe, E.A.1    Liao, L.2    Zhou, J.Y.3    Cheng, D.4    Duong, D.M.5    Jin, P.6    Tsai, L.H.7    Peng, J.8
  • 31
    • 0042386445 scopus 로고    scopus 로고
    • Lipid- and protein-mediated multimerization of PSD-95: implications for receptor clustering and assembly of synaptic protein networks
    • Christopherson K.S., Sweeney N.T., Craven S.E., Kang R., El-Husseini Ael D., Bredt D.S. Lipid- and protein-mediated multimerization of PSD-95: implications for receptor clustering and assembly of synaptic protein networks. J. Cell Sci. 2003, 116:3213-3219.
    • (2003) J. Cell Sci. , vol.116 , pp. 3213-3219
    • Christopherson, K.S.1    Sweeney, N.T.2    Craven, S.E.3    Kang, R.4    El-Husseini Ael, D.5    Bredt, D.S.6
  • 32
    • 8544232133 scopus 로고    scopus 로고
    • Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand
    • Chung H.J., Huang Y.H., Lau L.F., Huganir R.L. Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand. J. Neurosci. 2004, 24:10248-10259.
    • (2004) J. Neurosci. , vol.24 , pp. 10248-10259
    • Chung, H.J.1    Huang, Y.H.2    Lau, L.F.3    Huganir, R.L.4
  • 33
    • 42349091996 scopus 로고    scopus 로고
    • Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy
    • Cingolani L.A., Goda Y. Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy. Nat. Rev. Neurosci. 2008, 9:344-356.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 344-356
    • Cingolani, L.A.1    Goda, Y.2
  • 35
    • 0036618260 scopus 로고    scopus 로고
    • Activity-dependent recruitment of extrasynaptic NMDA receptor activation at an AMPA receptor-only synapse
    • Clark B.A., Cull-Candy S.G. Activity-dependent recruitment of extrasynaptic NMDA receptor activation at an AMPA receptor-only synapse. J. Neurosci. 2002, 22:4428-4436.
    • (2002) J. Neurosci. , vol.22 , pp. 4428-4436
    • Clark, B.A.1    Cull-Candy, S.G.2
  • 37
    • 0033103971 scopus 로고    scopus 로고
    • Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs
    • Craven S.E., El-Husseini A.E., Bredt D.S. Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs. Neuron 1999, 22:497-509.
    • (1999) Neuron , vol.22 , pp. 497-509
    • Craven, S.E.1    El-Husseini, A.E.2    Bredt, D.S.3
  • 38
    • 0035879068 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase mediates activity-regulated synaptic targeting of NMDA receptors
    • Crump F.T., Dillman K.S., Craig A.M. cAMP-dependent protein kinase mediates activity-regulated synaptic targeting of NMDA receptors. J. Neurosci. 2001, 21:5079-5088.
    • (2001) J. Neurosci. , vol.21 , pp. 5079-5088
    • Crump, F.T.1    Dillman, K.S.2    Craig, A.M.3
  • 39
    • 0035369112 scopus 로고    scopus 로고
    • NMDA receptor subunits: diversity, development and disease
    • Cull-Candy S., Brickley S., Farrant M. NMDA receptor subunits: diversity, development and disease. Curr. Opin. Neurobiol. 2001, 11:327-335.
    • (2001) Curr. Opin. Neurobiol. , vol.11 , pp. 327-335
    • Cull-Candy, S.1    Brickley, S.2    Farrant, M.3
  • 40
    • 16544376850 scopus 로고    scopus 로고
    • Role of distinct NMDA receptor subtypes at central synapses
    • Cull-Candy S.G., Leszkiewicz D.N. Role of distinct NMDA receptor subtypes at central synapses. Sci STKE 2004, re16.
    • (2004) Sci STKE
    • Cull-Candy, S.G.1    Leszkiewicz, D.N.2
  • 41
    • 0033635736 scopus 로고    scopus 로고
    • EphB receptors interact with NMDA receptors and regulate excitatory synapse formation
    • Dalva M.B., Takasu M.A., Lin M.Z., Shamah S.M., Hu L., Gale N.W., Greenberg M.E. EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. Cell 2000, 103:945-956.
    • (2000) Cell , vol.103 , pp. 945-956
    • Dalva, M.B.1    Takasu, M.A.2    Lin, M.Z.3    Shamah, S.M.4    Hu, L.5    Gale, N.W.6    Greenberg, M.E.7
  • 42
    • 0001788650 scopus 로고    scopus 로고
    • Neuroprotective and symptomatological action of memantine relevant for Alzheimer's disease-a unified glutamatergic hypothesis on the mechanism of action
    • Danysz W., Parsons C.G., Mobius H.J., Stoffler A., Quack G. Neuroprotective and symptomatological action of memantine relevant for Alzheimer's disease-a unified glutamatergic hypothesis on the mechanism of action. Neurotox. Res. 2000, 2:85-97.
    • (2000) Neurotox. Res. , vol.2 , pp. 85-97
    • Danysz, W.1    Parsons, C.G.2    Mobius, H.J.3    Stoffler, A.4    Quack, G.5
  • 45
    • 34249672242 scopus 로고    scopus 로고
    • Abeta oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine
    • De Felice F.G., Velasco P.T., Lambert M.P., Viola K., Fernandez S.J., Ferreira S.T., Klein W.L. Abeta oligomers induce neuronal oxidative stress through an N-methyl-d-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine. J. Biol. Chem. 2007, 282:11590-11601.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11590-11601
    • De Felice, F.G.1    Velasco, P.T.2    Lambert, M.P.3    Viola, K.4    Fernandez, S.J.5    Ferreira, S.T.6    Klein, W.L.7
  • 48
    • 10944267003 scopus 로고    scopus 로고
    • Interactions of postsynaptic density-95 and the NMDA receptor 2 subunit control calpain-mediated cleavage of the NMDA receptor
    • Dong Y.N., Waxman E.A., Lynch D.R. Interactions of postsynaptic density-95 and the NMDA receptor 2 subunit control calpain-mediated cleavage of the NMDA receptor. J. Neurosci. 2004, 24:11035-11045.
    • (2004) J. Neurosci. , vol.24 , pp. 11035-11045
    • Dong, Y.N.1    Waxman, E.A.2    Lynch, D.R.3
  • 49
    • 33748696770 scopus 로고    scopus 로고
    • Developmental and cell-selective variations in N-methyl-d-aspartate receptor degradation by calpain
    • Dong Y.N., Wu H.Y., Hsu F.C., Coulter D.A., Lynch D.R. Developmental and cell-selective variations in N-methyl-d-aspartate receptor degradation by calpain. J. Neurochem. 2006, 99:206-217.
    • (2006) J. Neurochem. , vol.99 , pp. 206-217
    • Dong, Y.N.1    Wu, H.Y.2    Hsu, F.C.3    Coulter, D.A.4    Lynch, D.R.5
  • 51
    • 0033974271 scopus 로고    scopus 로고
    • Alterations in subunit expression, composition, and phosphorylation of striatal N-methyl-d-aspartate glutamate receptors in a rat 6-hydroxydopamine model of Parkinson's disease
    • Dunah A.W., Wang Y., Yasuda R.P., Kameyama K., Huganir R.L., Wolfe B.B., Standaert D.G. Alterations in subunit expression, composition, and phosphorylation of striatal N-methyl-d-aspartate glutamate receptors in a rat 6-hydroxydopamine model of Parkinson's disease. Mol. Pharmacol. 2000, 57:342-352.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 342-352
    • Dunah, A.W.1    Wang, Y.2    Yasuda, R.P.3    Kameyama, K.4    Huganir, R.L.5    Wolfe, B.B.6    Standaert, D.G.7
  • 52
    • 0034705447 scopus 로고    scopus 로고
    • Alpha-actinin-2 in rat striatum: localization and interaction with NMDA glutamate receptor subunits
    • Dunah A.W., Wyszynski M., Martin D.M., Sheng M., Standaert D.G. alpha-actinin-2 in rat striatum: localization and interaction with NMDA glutamate receptor subunits. Brain Res. Mol. Brain Res. 2000, 79:77-87.
    • (2000) Brain Res. Mol. Brain Res. , vol.79 , pp. 77-87
    • Dunah, A.W.1    Wyszynski, M.2    Martin, D.M.3    Sheng, M.4    Standaert, D.G.5
  • 53
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers M.D. Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nat. Neurosci. 2003, 6:231-242.
    • (2003) Nat. Neurosci. , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 54
    • 0031972719 scopus 로고    scopus 로고
    • Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments
    • Ehlers M.D., Fung E.T., O'Brien R.J., Huganir R.L. Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. J. Neurosci. 1998, 18:720-730.
    • (1998) J. Neurosci. , vol.18 , pp. 720-730
    • Ehlers, M.D.1    Fung, E.T.2    O'Brien, R.J.3    Huganir, R.L.4
  • 55
    • 0029147928 scopus 로고
    • Regulated subcellular distribution of the NR1 subunit of the NMDA receptor
    • Ehlers M.D., Tingley W.G., Huganir R.L. Regulated subcellular distribution of the NR1 subunit of the NMDA receptor. Science 1995, 269:1734-1737.
    • (1995) Science , vol.269 , pp. 1734-1737
    • Ehlers, M.D.1    Tingley, W.G.2    Huganir, R.L.3
  • 56
    • 0034627757 scopus 로고    scopus 로고
    • Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
    • El-Husseini A.E., Craven S.E., Chetkovich D.M., Firestein B.L., Schnell E., Aoki C., Bredt D.S. Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J. Cell Biol. 2000, 148:159-172.
    • (2000) J. Cell Biol. , vol.148 , pp. 159-172
    • El-Husseini, A.E.1    Craven, S.E.2    Chetkovich, D.M.3    Firestein, B.L.4    Schnell, E.5    Aoki, C.6    Bredt, D.S.7
  • 58
    • 0036779578 scopus 로고    scopus 로고
    • Protein palmitoylation: a regulator of neuronal development and function
    • el-Husseini Ael D., Bredt D.S. Protein palmitoylation: a regulator of neuronal development and function. Nat. Rev. Neurosci. 2002, 3:791-802.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 791-802
    • el-Husseini Ael, D.1    Bredt, D.S.2
  • 59
  • 60
    • 69749091508 scopus 로고    scopus 로고
    • Interaction of postsynaptic density protein-95 with NMDA receptors influences excitotoxicity in the yeast artificial chromosome mouse model of Huntington's disease
    • Fan J., Cowan C.M., Zhang L.Y., Hayden M.R., Raymond L.A. Interaction of postsynaptic density protein-95 with NMDA receptors influences excitotoxicity in the yeast artificial chromosome mouse model of Huntington's disease. J. Neurosci. 2009, 29:10928-10938.
    • (2009) J. Neurosci. , vol.29 , pp. 10928-10938
    • Fan, J.1    Cowan, C.M.2    Zhang, L.Y.3    Hayden, M.R.4    Raymond, L.A.5
  • 61
    • 34147112751 scopus 로고    scopus 로고
    • Altered NMDA receptor trafficking in a yeast artificial chromosome transgenic mouse model of Huntington's disease
    • Fan M.M., Fernandes H.B., Zhang L.Y., Hayden M.R., Raymond L.A. Altered NMDA receptor trafficking in a yeast artificial chromosome transgenic mouse model of Huntington's disease. J. Neurosci. 2007, 27:3768-3779.
    • (2007) J. Neurosci. , vol.27 , pp. 3768-3779
    • Fan, M.M.1    Fernandes, H.B.2    Zhang, L.Y.3    Hayden, M.R.4    Raymond, L.A.5
  • 62
    • 37249083913 scopus 로고    scopus 로고
    • Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease
    • Fernandes H.B., Baimbridge K.G., Church J., Hayden M.R., Raymond L.A. Mitochondrial sensitivity and altered calcium handling underlie enhanced NMDA-induced apoptosis in YAC128 model of Huntington's disease. J. Neurosci. 2007, 27:13614-13623.
    • (2007) J. Neurosci. , vol.27 , pp. 13614-13623
    • Fernandes, H.B.1    Baimbridge, K.G.2    Church, J.3    Hayden, M.R.4    Raymond, L.A.5
  • 63
    • 0030909728 scopus 로고    scopus 로고
    • NR2A subunit expression shortens NMDA receptor synaptic currents in developing neocortex
    • Flint A.C., Maisch U.S., Weishaupt J.H., Kriegstein A.R., Monyer H. NR2A subunit expression shortens NMDA receptor synaptic currents in developing neocortex. J. Neurosci. 1997, 17:2469-2476.
    • (1997) J. Neurosci. , vol.17 , pp. 2469-2476
    • Flint, A.C.1    Maisch, U.S.2    Weishaupt, J.H.3    Kriegstein, A.R.4    Monyer, H.5
  • 64
    • 0037088921 scopus 로고    scopus 로고
    • Rapid synaptic remodeling by protein kinase C: reciprocal translocation of NMDA receptors and calcium/calmodulin-dependent kinase II
    • Fong D.K., Rao A., Crump F.T., Craig A.M. Rapid synaptic remodeling by protein kinase C: reciprocal translocation of NMDA receptors and calcium/calmodulin-dependent kinase II. J. Neurosci. 2002, 22:2153-2164.
    • (2002) J. Neurosci. , vol.22 , pp. 2153-2164
    • Fong, D.K.1    Rao, A.2    Crump, F.T.3    Craig, A.M.4
  • 66
    • 33751367170 scopus 로고    scopus 로고
    • Calcium-calmodulin-dependent protein kinase II phosphorylation modulates PSD-95 binding to NMDA receptors
    • Gardoni F., Polli F., Cattabeni F., Di Luca M. Calcium-calmodulin-dependent protein kinase II phosphorylation modulates PSD-95 binding to NMDA receptors. Eur. J. Neurosci. 2006, 24:2694-2704.
    • (2006) Eur. J. Neurosci. , vol.24 , pp. 2694-2704
    • Gardoni, F.1    Polli, F.2    Cattabeni, F.3    Di Luca, M.4
  • 67
    • 37249023297 scopus 로고    scopus 로고
    • Excitotoxicity and focal cerebral ischemia induce truncation of the NR2A and NR2B subunits of the NMDA receptor and cleavage of the scaffolding protein PSD-95
    • Gascon S., Sobrado M., Roda J.M., Rodriguez-Pena A., Diaz-Guerra M. Excitotoxicity and focal cerebral ischemia induce truncation of the NR2A and NR2B subunits of the NMDA receptor and cleavage of the scaffolding protein PSD-95. Mol. Psychiatry 2008, 13:99-114.
    • (2008) Mol. Psychiatry , vol.13 , pp. 99-114
    • Gascon, S.1    Sobrado, M.2    Roda, J.M.3    Rodriguez-Pena, A.4    Diaz-Guerra, M.5
  • 68
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 2002, 82:373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 69
    • 27844539808 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the N-methyl-d-aspartate receptor is enhanced in synaptic membrane fractions of the adult rat hippocampus
    • Goebel S.M., Alvestad R.M., Coultrap S.J., Browning M.D. Tyrosine phosphorylation of the N-methyl-d-aspartate receptor is enhanced in synaptic membrane fractions of the adult rat hippocampus. Brain Res. Mol. Brain Res. 2005, 142:65-79.
    • (2005) Brain Res. Mol. Brain Res. , vol.142 , pp. 65-79
    • Goebel, S.M.1    Alvestad, R.M.2    Coultrap, S.J.3    Browning, M.D.4
  • 70
    • 60349088785 scopus 로고    scopus 로고
    • Phospho-regulation of synaptic and extrasynaptic N-methyl-d-aspartate receptors in adult hippocampal slices
    • Goebel-Goody S.M., Davies K.D., Alvestad Linger R.M., Freund R.K., Browning M.D. Phospho-regulation of synaptic and extrasynaptic N-methyl-d-aspartate receptors in adult hippocampal slices. Neuroscience 2009, 158:1446-1459.
    • (2009) Neuroscience , vol.158 , pp. 1446-1459
    • Goebel-Goody, S.M.1    Davies, K.D.2    Alvestad Linger, R.M.3    Freund, R.K.4    Browning, M.D.5
  • 72
    • 0021982117 scopus 로고
    • Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease
    • Graveland G.A., Williams R.S., DiFiglia M. Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington's disease. Science 1985, 227:770-773.
    • (1985) Science , vol.227 , pp. 770-773
    • Graveland, G.A.1    Williams, R.S.2    DiFiglia, M.3
  • 73
    • 58149463218 scopus 로고    scopus 로고
    • Surface trafficking of N-methyl-d-aspartate receptors: physiological and pathological perspectives
    • Groc L., Bard L., Choquet D. Surface trafficking of N-methyl-d-aspartate receptors: physiological and pathological perspectives. Neuroscience 2009, 158:4-18.
    • (2009) Neuroscience , vol.158 , pp. 4-18
    • Groc, L.1    Bard, L.2    Choquet, D.3
  • 74
    • 33748920372 scopus 로고    scopus 로고
    • AMPA and NMDA glutamate receptor trafficking: multiple roads for reaching and leaving the synapse
    • Groc L., Choquet D. AMPA and NMDA glutamate receptor trafficking: multiple roads for reaching and leaving the synapse. Cell Tissue Res. 2006, 326:423-438.
    • (2006) Cell Tissue Res. , vol.326 , pp. 423-438
    • Groc, L.1    Choquet, D.2
  • 75
    • 34548855036 scopus 로고    scopus 로고
    • NMDA receptor surface trafficking and synaptic subunit composition are developmentally regulated by the extracellular matrix protein Reelin
    • Groc L., Choquet D., Stephenson F.A., Verrier D., Manzoni O.J., Chavis P. NMDA receptor surface trafficking and synaptic subunit composition are developmentally regulated by the extracellular matrix protein Reelin. J. Neurosci. 2007, 27:10165-10175.
    • (2007) J. Neurosci. , vol.27 , pp. 10165-10175
    • Groc, L.1    Choquet, D.2    Stephenson, F.A.3    Verrier, D.4    Manzoni, O.J.5    Chavis, P.6
  • 79
    • 0036139881 scopus 로고    scopus 로고
    • LTP leads to rapid surface expression of NMDA but not AMPA receptors in adult rat CA1
    • Grosshans D.R., Clayton D.A., Coultrap S.J., Browning M.D. LTP leads to rapid surface expression of NMDA but not AMPA receptors in adult rat CA1. Nat. Neurosci. 2002, 5:27-33.
    • (2002) Nat. Neurosci. , vol.5 , pp. 27-33
    • Grosshans, D.R.1    Clayton, D.A.2    Coultrap, S.J.3    Browning, M.D.4
  • 80
    • 0037223301 scopus 로고    scopus 로고
    • KIF17 dynamics and regulation of NR2B trafficking in hippocampal neurons
    • Guillaud L., Setou M., Hirokawa N. KIF17 dynamics and regulation of NR2B trafficking in hippocampal neurons. J. Neurosci. 2003, 23:131-140.
    • (2003) J. Neurosci. , vol.23 , pp. 131-140
    • Guillaud, L.1    Setou, M.2    Hirokawa, N.3
  • 81
    • 0032742620 scopus 로고    scopus 로고
    • Hypoxia-ischemia in perinatal rat brain induces the formation of a low molecular weight isoform of striatal enriched tyrosine phosphatase (STEP)
    • Gurd J.W., Bissoon N., Nguyen T.H., Lombroso P.J., Rider C.C., Beesley P.W., Vannucci S.J. Hypoxia-ischemia in perinatal rat brain induces the formation of a low molecular weight isoform of striatal enriched tyrosine phosphatase (STEP). J. Neurochem. 1999, 73:1990-1994.
    • (1999) J. Neurochem. , vol.73 , pp. 1990-1994
    • Gurd, J.W.1    Bissoon, N.2    Nguyen, T.H.3    Lombroso, P.J.4    Rider, C.C.5    Beesley, P.W.6    Vannucci, S.J.7
  • 83
    • 1542360582 scopus 로고    scopus 로고
    • Effect of a selective glutamate antagonist on l-DOPA-induced dyskinesias in drug-naive parkinsonian monkeys
    • Hadj Tahar A., Gregoire L., Darre A., Belanger N., Meltzer L., Bedard P.J. Effect of a selective glutamate antagonist on l-DOPA-induced dyskinesias in drug-naive parkinsonian monkeys. Neurobiol. Dis. 2004, 15:171-176.
    • (2004) Neurobiol. Dis. , vol.15 , pp. 171-176
    • Hadj Tahar, A.1    Gregoire, L.2    Darre, A.3    Belanger, N.4    Meltzer, L.5    Bedard, P.J.6
  • 85
    • 77956917231 scopus 로고    scopus 로고
    • Synaptic versus extrasynaptic NMDA receptor signalling: implications for neurodegenerative disorders
    • Hardingham G.E., Bading H. Synaptic versus extrasynaptic NMDA receptor signalling: implications for neurodegenerative disorders. Nat. Rev. Neurosci. 2010, 11:682-696.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 682-696
    • Hardingham, G.E.1    Bading, H.2
  • 86
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • Hardingham G.E., Fukunaga Y., Bading H. Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways. Nat. Neurosci. 2002, 5:405-414.
    • (2002) Nat. Neurosci. , vol.5 , pp. 405-414
    • Hardingham, G.E.1    Fukunaga, Y.2    Bading, H.3
  • 87
    • 0041656292 scopus 로고    scopus 로고
    • The hunt for huntingtin function: interaction partners tell many different stories
    • Harjes P., Wanker E.E. The hunt for huntingtin function: interaction partners tell many different stories. Trends Biochem. Sci. 2003, 28:425-433.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 425-433
    • Harjes, P.1    Wanker, E.E.2
  • 88
    • 35348900781 scopus 로고    scopus 로고
    • Extrasynaptic and synaptic NMDA receptors form stable and uniform pools in rat hippocampal slices
    • Harris A.Z., Pettit D.L. Extrasynaptic and synaptic NMDA receptors form stable and uniform pools in rat hippocampal slices. J. Physiol. 2007, 584:509-519.
    • (2007) J. Physiol. , vol.584 , pp. 509-519
    • Harris, A.Z.1    Pettit, D.L.2
  • 89
    • 39149086059 scopus 로고    scopus 로고
    • Recruiting extrasynaptic NMDA receptors augments synaptic signaling
    • Harris A.Z., Pettit D.L. Recruiting extrasynaptic NMDA receptors augments synaptic signaling. J. Neurophysiol. 2008, 99:524-533.
    • (2008) J. Neurophysiol. , vol.99 , pp. 524-533
    • Harris, A.Z.1    Pettit, D.L.2
  • 91
    • 70350207200 scopus 로고    scopus 로고
    • Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking
    • Hayashi T., Thomas G.M., Huganir R.L. Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking. Neuron 2009, 64:213-226.
    • (2009) Neuron , vol.64 , pp. 213-226
    • Hayashi, T.1    Thomas, G.M.2    Huganir, R.L.3
  • 92
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • HDCRG
    • HDCRG A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993, 72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 93
    • 0346433978 scopus 로고    scopus 로고
    • Activity-dependent redistribution and essential role of cortactin in dendritic spine morphogenesis
    • Hering H., Sheng M. Activity-dependent redistribution and essential role of cortactin in dendritic spine morphogenesis. J. Neurosci. 2003, 23:11759-11769.
    • (2003) J. Neurosci. , vol.23 , pp. 11759-11769
    • Hering, H.1    Sheng, M.2
  • 94
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2001, 2:195-201.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 95
    • 25844522857 scopus 로고    scopus 로고
    • Modulation of neuronal protein trafficking and function by palmitoylation
    • Huang K., El-Husseini A. Modulation of neuronal protein trafficking and function by palmitoylation. Curr. Opin. Neurobiol. 2005, 15:527-535.
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 527-535
    • Huang, K.1    El-Husseini, A.2
  • 97
    • 0037155199 scopus 로고    scopus 로고
    • PDZ domains: structural modules for protein complex assembly
    • Hung A.Y., Sheng M. PDZ domains: structural modules for protein complex assembly. J. Biol. Chem. 2002, 277:5699-5702.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5699-5702
    • Hung, A.Y.1    Sheng, M.2
  • 99
    • 33645837486 scopus 로고    scopus 로고
    • Opposing role of synaptic and extrasynaptic NMDA receptors in regulation of the extracellular signal-regulated kinases (ERK) activity in cultured rat hippocampal neurons
    • Ivanov A., Pellegrino C., Rama S., Dumalska I., Salyha Y., Ben-Ari Y., Medina I. Opposing role of synaptic and extrasynaptic NMDA receptors in regulation of the extracellular signal-regulated kinases (ERK) activity in cultured rat hippocampal neurons. J. Physiol. 2006, 572:789-798.
    • (2006) J. Physiol. , vol.572 , pp. 789-798
    • Ivanov, A.1    Pellegrino, C.2    Rama, S.3    Dumalska, I.4    Salyha, Y.5    Ben-Ari, Y.6    Medina, I.7
  • 100
    • 1542346231 scopus 로고    scopus 로고
    • Regulation of proteins affecting NMDA receptor-induced excitotoxicity in a Huntington's mouse model
    • Jarabek B.R., Yasuda R.P., Wolfe B.B. Regulation of proteins affecting NMDA receptor-induced excitotoxicity in a Huntington's mouse model. Brain 2004, 127:505-516.
    • (2004) Brain , vol.127 , pp. 505-516
    • Jarabek, B.R.1    Yasuda, R.P.2    Wolfe, B.B.3
  • 102
    • 38049107891 scopus 로고    scopus 로고
    • Mind bomb-2 is an E3 ligase that ubiquitinates the N-methyl-d-aspartate receptor NR2B subunit in a phosphorylation-dependent manner
    • Jurd R., Thornton C., Wang J., Luong K., Phamluong K., Kharazia V., Gibb S.L., Ron D. Mind bomb-2 is an E3 ligase that ubiquitinates the N-methyl-d-aspartate receptor NR2B subunit in a phosphorylation-dependent manner. J. Biol. Chem. 2008, 283:301-310.
    • (2008) J. Biol. Chem. , vol.283 , pp. 301-310
    • Jurd, R.1    Thornton, C.2    Wang, J.3    Luong, K.4    Phamluong, K.5    Kharazia, V.6    Gibb, S.L.7    Ron, D.8
  • 104
    • 33750211862 scopus 로고    scopus 로고
    • PSD-95 is a negative regulator of the tyrosine kinase Src in the NMDA receptor complex
    • Kalia L.V., Pitcher G.M., Pelkey K.A., Salter M.W. PSD-95 is a negative regulator of the tyrosine kinase Src in the NMDA receptor complex. EMBO J. 2006, 25:4971-4982.
    • (2006) EMBO J. , vol.25 , pp. 4971-4982
    • Kalia, L.V.1    Pitcher, G.M.2    Pelkey, K.A.3    Salter, M.W.4
  • 107
    • 17244381176 scopus 로고    scopus 로고
    • Activity-dependent NMDA receptor degradation mediated by retrotranslocation and ubiquitination
    • Kato A., Rouach N., Nicoll R.A., Bredt D.S. Activity-dependent NMDA receptor degradation mediated by retrotranslocation and ubiquitination. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:5600-5605.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 5600-5605
    • Kato, A.1    Rouach, N.2    Nicoll, R.A.3    Bredt, D.S.4
  • 108
    • 0032521090 scopus 로고    scopus 로고
    • Developmental changes in NMDA receptor glycine affinity and ifenprodil sensitivity reveal three distinct populations of NMDA receptors in individual rat cortical neurons
    • Kew J.N., Richards J.G., Mutel V., Kemp J.A. Developmental changes in NMDA receptor glycine affinity and ifenprodil sensitivity reveal three distinct populations of NMDA receptors in individual rat cortical neurons. J. Neurosci. 1998, 18:1935-1943.
    • (1998) J. Neurosci. , vol.18 , pp. 1935-1943
    • Kew, J.N.1    Richards, J.G.2    Mutel, V.3    Kemp, J.A.4
  • 109
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim E., Sheng M. PDZ domain proteins of synapses. Nat. Rev. Neurosci. 2004, 5:771-781.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 110
    • 0029887701 scopus 로고    scopus 로고
    • Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein
    • Klauck T.M., Faux M.C., Labudda K., Langeberg L.K., Jaken S., Scott J.D. Coordination of three signaling enzymes by AKAP79, a mammalian scaffold protein. Science 1996, 271:1589-1592.
    • (1996) Science , vol.271 , pp. 1589-1592
    • Klauck, T.M.1    Faux, M.C.2    Labudda, K.3    Langeberg, L.K.4    Jaken, S.5    Scott, J.D.6
  • 112
    • 33747059623 scopus 로고    scopus 로고
    • Differential control of postsynaptic density scaffolds via actin-dependent and -independent mechanisms
    • Kuriu T., Inoue A., Bito H., Sobue K., Okabe S. Differential control of postsynaptic density scaffolds via actin-dependent and -independent mechanisms. J. Neurosci. 2006, 26:7693-7706.
    • (2006) J. Neurosci. , vol.26 , pp. 7693-7706
    • Kuriu, T.1    Inoue, A.2    Bito, H.3    Sobue, K.4    Okabe, S.5
  • 113
    • 77951653236 scopus 로고    scopus 로고
    • Abeta-mediated NMDA receptor endocytosis in Alzheimer's disease involves ubiquitination of the tyrosine phosphatase STEP61
    • Kurup P., Zhang Y., Xu J., Venkitaramani D.V., Haroutunian V., Greengard P., Nairn A.C., Lombroso P.J. Abeta-mediated NMDA receptor endocytosis in Alzheimer's disease involves ubiquitination of the tyrosine phosphatase STEP61. J. Neurosci. 2010, 30:5948-5957.
    • (2010) J. Neurosci. , vol.30 , pp. 5948-5957
    • Kurup, P.1    Zhang, Y.2    Xu, J.3    Venkitaramani, D.V.4    Haroutunian, V.5    Greengard, P.6    Nairn, A.C.7    Lombroso, P.J.8
  • 114
    • 33846633336 scopus 로고    scopus 로고
    • Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease
    • Lacor P.N., Buniel M.C., Furlow P.W., Clemente A.S., Velasco P.T., Wood M., Viola K.L., Klein W.L. Abeta oligomer-induced aberrations in synapse composition, shape, and density provide a molecular basis for loss of connectivity in Alzheimer's disease. J. Neurosci. 2007, 27:796-807.
    • (2007) J. Neurosci. , vol.27 , pp. 796-807
    • Lacor, P.N.1    Buniel, M.C.2    Furlow, P.W.3    Clemente, A.S.4    Velasco, P.T.5    Wood, M.6    Viola, K.L.7    Klein, W.L.8
  • 116
    • 34249099711 scopus 로고    scopus 로고
    • NMDA receptor trafficking in synaptic plasticity and neuropsychiatric disorders
    • Lau C.G., Zukin R.S. NMDA receptor trafficking in synaptic plasticity and neuropsychiatric disorders. Nat. Rev. Neurosci. 2007, 8:413-426.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 413-426
    • Lau, C.G.1    Zukin, R.S.2
  • 117
    • 0347506604 scopus 로고    scopus 로고
    • Differential binding of the AP-2 adaptor complex and PSD-95 to the C-terminus of the NMDA receptor subunit NR2B regulates surface expression
    • Lavezzari G., McCallum J., Lee R., Roche K.W. Differential binding of the AP-2 adaptor complex and PSD-95 to the C-terminus of the NMDA receptor subunit NR2B regulates surface expression. Neuropharmacology 2003, 45:729-737.
    • (2003) Neuropharmacology , vol.45 , pp. 729-737
    • Lavezzari, G.1    McCallum, J.2    Lee, R.3    Roche, K.W.4
  • 118
    • 34147117789 scopus 로고    scopus 로고
    • Tonic activation of NMDA receptors by ambient glutamate of non-synaptic origin in the rat hippocampus
    • Le Meur K., Galante M., Angulo M.C., Audinat E. Tonic activation of NMDA receptors by ambient glutamate of non-synaptic origin in the rat hippocampus. J. Physiol. 2007, 580:373-383.
    • (2007) J. Physiol. , vol.580 , pp. 373-383
    • Le Meur, K.1    Galante, M.2    Angulo, M.C.3    Audinat, E.4
  • 119
    • 57349135887 scopus 로고    scopus 로고
    • Neuronal viability is controlled by a functional relation between synaptic and extrasynaptic NMDA receptors
    • Leveille F., El Gaamouch F., Gouix E., Lecocq M., Lobner D., Nicole O., Buisson A. Neuronal viability is controlled by a functional relation between synaptic and extrasynaptic NMDA receptors. FASEB J. 2008, 22:4258-4271.
    • (2008) FASEB J. , vol.22 , pp. 4258-4271
    • Leveille, F.1    El Gaamouch, F.2    Gouix, E.3    Lecocq, M.4    Lobner, D.5    Nicole, O.6    Buisson, A.7
  • 120
    • 74549155949 scopus 로고    scopus 로고
    • Location, location, location: contrasting roles of synaptic and extrasynaptic NMDA receptors in Huntington's disease
    • Levine M.S., Cepeda C., Andre V.M. Location, location, location: contrasting roles of synaptic and extrasynaptic NMDA receptors in Huntington's disease. Neuron 2010, 65:145-147.
    • (2010) Neuron , vol.65 , pp. 145-147
    • Levine, M.S.1    Cepeda, C.2    Andre, V.M.3
  • 121
    • 0036728049 scopus 로고    scopus 로고
    • Differential regulation of synaptic and extra-synaptic NMDA receptors
    • Li B., Chen N., Luo T., Otsu Y., Murphy T.H., Raymond L.A. Differential regulation of synaptic and extra-synaptic NMDA receptors. Nat. Neurosci. 2002, 5:833-834.
    • (2002) Nat. Neurosci. , vol.5 , pp. 833-834
    • Li, B.1    Chen, N.2    Luo, T.3    Otsu, Y.4    Murphy, T.H.5    Raymond, L.A.6
  • 122
    • 14844314896 scopus 로고    scopus 로고
    • Enhanced striatal NR2B-containing N-methyl-d-aspartate receptor-mediated synaptic currents in a mouse model of Huntington disease
    • Li L., Murphy T.H., Hayden M.R., Raymond L.A. Enhanced striatal NR2B-containing N-methyl-d-aspartate receptor-mediated synaptic currents in a mouse model of Huntington disease. J. Neurophysiol. 2004, 92:2738-2746.
    • (2004) J. Neurophysiol. , vol.92 , pp. 2738-2746
    • Li, L.1    Murphy, T.H.2    Hayden, M.R.3    Raymond, L.A.4
  • 124
    • 0038216785 scopus 로고    scopus 로고
    • Integrins regulate NMDA receptor-mediated synaptic currents
    • Lin B., Arai A.C., Lynch G., Gall C.M. Integrins regulate NMDA receptor-mediated synaptic currents. J. Neurophysiol. 2003, 89:2874-2878.
    • (2003) J. Neurophysiol. , vol.89 , pp. 2874-2878
    • Lin, B.1    Arai, A.C.2    Lynch, G.3    Gall, C.M.4
  • 125
    • 8544244897 scopus 로고    scopus 로고
    • Postsynaptic density protein-95 regulates NMDA channel gating and surface expression
    • Lin Y., Skeberdis V.A., Francesconi A., Bennett M.V., Zukin R.S. Postsynaptic density protein-95 regulates NMDA channel gating and surface expression. J. Neurosci. 2004, 24:10138-10148.
    • (2004) J. Neurosci. , vol.24 , pp. 10138-10148
    • Lin, Y.1    Skeberdis, V.A.2    Francesconi, A.3    Bennett, M.V.4    Zukin, R.S.5
  • 126
    • 0028762647 scopus 로고
    • Excitatory amino acids as a final common pathway for neurologic disorders
    • Lipton S.A., Rosenberg P.A. Excitatory amino acids as a final common pathway for neurologic disorders. N. Engl. J. Med. 1994, 330:613-622.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 613-622
    • Lipton, S.A.1    Rosenberg, P.A.2
  • 128
    • 1842664189 scopus 로고    scopus 로고
    • Antiparkinsonian activity of Ro 25-6981, a NR2B subunit specific NMDA receptor antagonist, in animal models of Parkinson's disease
    • Loschmann P.A., De Groote C., Smith L., Wullner U., Fischer G., Kemp J.A., Jenner P., Klockgether T. Antiparkinsonian activity of Ro 25-6981, a NR2B subunit specific NMDA receptor antagonist, in animal models of Parkinson's disease. Exp. Neurol. 2004, 187:86-93.
    • (2004) Exp. Neurol. , vol.187 , pp. 86-93
    • Loschmann, P.A.1    De Groote, C.2    Smith, L.3    Wullner, U.4    Fischer, G.5    Kemp, J.A.6    Jenner, P.7    Klockgether, T.8
  • 129
    • 0031032658 scopus 로고    scopus 로고
    • The majority of N-methyl-d-aspartate receptor complexes in adult rat cerebral cortex contain at least three different subunits (NR1/NR2A/NR2B)
    • Luo J., Wang Y., Yasuda R.P., Dunah A.W., Wolfe B.B. The majority of N-methyl-d-aspartate receptor complexes in adult rat cerebral cortex contain at least three different subunits (NR1/NR2A/NR2B). Mol. Pharmacol. 1997, 51:79-86.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 79-86
    • Luo, J.1    Wang, Y.2    Yasuda, R.P.3    Dunah, A.W.4    Wolfe, B.B.5
  • 130
    • 78049395303 scopus 로고    scopus 로고
    • Ubiquitination in postsynaptic function and plasticity
    • Mabb A.M., Ehlers M.D. Ubiquitination in postsynaptic function and plasticity. Annu. Rev. Cell Dev. Biol. 2010, 26:179-210.
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 179-210
    • Mabb, A.M.1    Ehlers, M.D.2
  • 134
    • 58149476292 scopus 로고    scopus 로고
    • In developing hippocampal neurons, NR2B-containing N-methyl-d-aspartate receptors (NMDARs) can mediate signaling to neuronal survival and synaptic potentiation, as well as neuronal death
    • Martel M.A., Wyllie D.J., Hardingham G.E. In developing hippocampal neurons, NR2B-containing N-methyl-d-aspartate receptors (NMDARs) can mediate signaling to neuronal survival and synaptic potentiation, as well as neuronal death. Neuroscience 2009, 158:334-343.
    • (2009) Neuroscience , vol.158 , pp. 334-343
    • Martel, M.A.1    Wyllie, D.J.2    Hardingham, G.E.3
  • 135
    • 0037320688 scopus 로고    scopus 로고
    • Assembly and plasticity of the glutamatergic postsynaptic specialization
    • McGee A.W., Bredt D.S. Assembly and plasticity of the glutamatergic postsynaptic specialization. Curr. Opin. Neurobiol. 2003, 13:111-118.
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 111-118
    • McGee, A.W.1    Bredt, D.S.2
  • 138
    • 37449011119 scopus 로고    scopus 로고
    • Corticostriatal synaptic function in mouse models of Huntington's disease: early effects of huntingtin repeat length and protein load
    • Milnerwood A.J., Raymond L.A. Corticostriatal synaptic function in mouse models of Huntington's disease: early effects of huntingtin repeat length and protein load. J. Physiol. 2007, 585:817-831.
    • (2007) J. Physiol. , vol.585 , pp. 817-831
    • Milnerwood, A.J.1    Raymond, L.A.2
  • 139
    • 77958192164 scopus 로고    scopus 로고
    • Early synaptic pathophysiology in neurodegeneration: insights from Huntington's disease
    • Milnerwood A.J., Raymond L.A. Early synaptic pathophysiology in neurodegeneration: insights from Huntington's disease. Trends Neurosci. 2010, 33:513-523.
    • (2010) Trends Neurosci. , vol.33 , pp. 513-523
    • Milnerwood, A.J.1    Raymond, L.A.2
  • 140
    • 0028343648 scopus 로고
    • Developmental and regional expression in the rat brain and functional properties of four NMDA receptors
    • Monyer H., Burnashev N., Laurie D.J., Sakmann B., Seeburg P.H. Developmental and regional expression in the rat brain and functional properties of four NMDA receptors. Neuron 1994, 12:529-540.
    • (1994) Neuron , vol.12 , pp. 529-540
    • Monyer, H.1    Burnashev, N.2    Laurie, D.J.3    Sakmann, B.4    Seeburg, P.H.5
  • 141
    • 0742270492 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 phosphorylates the N-terminal domain of the postsynaptic density protein PSD-95 in neurons
    • Morabito M.A., Sheng M., Tsai L.H. Cyclin-dependent kinase 5 phosphorylates the N-terminal domain of the postsynaptic density protein PSD-95 in neurons. J. Neurosci. 2004, 24:865-876.
    • (2004) J. Neurosci. , vol.24 , pp. 865-876
    • Morabito, M.A.1    Sheng, M.2    Tsai, L.H.3
  • 143
    • 23044455322 scopus 로고    scopus 로고
    • Distinct triggering and expression mechanisms underlie LTD of AMPA and NMDA synaptic responses
    • Morishita W., Marie H., Malenka R.C. Distinct triggering and expression mechanisms underlie LTD of AMPA and NMDA synaptic responses. Nat. Neurosci. 2005, 8:1043-1050.
    • (2005) Nat. Neurosci. , vol.8 , pp. 1043-1050
    • Morishita, W.1    Marie, H.2    Malenka, R.C.3
  • 144
    • 0034234519 scopus 로고    scopus 로고
    • Abnormal synaptic plasticity and impaired spatial cognition in mice transgenic for exon 1 of the human Huntington's disease mutation
    • Murphy K.P., Carter R.J., Lione L.A., Mangiarini L., Mahal A., Bates G.P., Dunnett S.B., Morton A.J. Abnormal synaptic plasticity and impaired spatial cognition in mice transgenic for exon 1 of the human Huntington's disease mutation. J. Neurosci. 2000, 20:5115-5123.
    • (2000) J. Neurosci. , vol.20 , pp. 5115-5123
    • Murphy, K.P.1    Carter, R.J.2    Lione, L.A.3    Mangiarini, L.4    Mahal, A.5    Bates, G.P.6    Dunnett, S.B.7    Morton, A.J.8
  • 147
    • 33746009937 scopus 로고    scopus 로고
    • A novel route for F-box protein-mediated ubiquitination links CHIP to glycoprotein quality control
    • Nelson R.F., Glenn K.A., Miller V.M., Wen H., Paulson H.L. A novel route for F-box protein-mediated ubiquitination links CHIP to glycoprotein quality control. J. Biol. Chem. 2006, 281:20242-20251.
    • (2006) J. Biol. Chem. , vol.281 , pp. 20242-20251
    • Nelson, R.F.1    Glenn, K.A.2    Miller, V.M.3    Wen, H.4    Paulson, H.L.5
  • 148
    • 43449102784 scopus 로고    scopus 로고
    • Glutamate receptor dynamics in dendritic microdomains
    • Newpher T.M., Ehlers M.D. Glutamate receptor dynamics in dendritic microdomains. Neuron 2008, 58:472-497.
    • (2008) Neuron , vol.58 , pp. 472-497
    • Newpher, T.M.1    Ehlers, M.D.2
  • 149
    • 65149090058 scopus 로고    scopus 로고
    • Spine microdomains for postsynaptic signaling and plasticity
    • Newpher T.M., Ehlers M.D. Spine microdomains for postsynaptic signaling and plasticity. Trends Cell Biol. 2009, 19:218-227.
    • (2009) Trends Cell Biol. , vol.19 , pp. 218-227
    • Newpher, T.M.1    Ehlers, M.D.2
  • 150
    • 0037025303 scopus 로고    scopus 로고
    • Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420
    • Nguyen T.H., Liu J., Lombroso P.J. Striatal enriched phosphatase 61 dephosphorylates Fyn at phosphotyrosine 420. J. Biol. Chem. 2002, 277:24274-24279.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24274-24279
    • Nguyen, T.H.1    Liu, J.2    Lombroso, P.J.3
  • 151
    • 0032692172 scopus 로고    scopus 로고
    • Calcium-dependent cleavage of striatal enriched tyrosine phosphatase (STEP)
    • Nguyen T.H., Paul S., Xu Y., Gurd J.W., Lombroso P.J. Calcium-dependent cleavage of striatal enriched tyrosine phosphatase (STEP). J. Neurochem. 1999, 73:1995-2001.
    • (1999) J. Neurochem. , vol.73 , pp. 1995-2001
    • Nguyen, T.H.1    Paul, S.2    Xu, Y.3    Gurd, J.W.4    Lombroso, P.J.5
  • 152
    • 0029946167 scopus 로고    scopus 로고
    • Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
    • Niethammer M., Kim E., Sheng M. Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. J. Neurosci. 1996, 16:2157-2163.
    • (1996) J. Neurosci. , vol.16 , pp. 2157-2163
    • Niethammer, M.1    Kim, E.2    Sheng, M.3
  • 153
    • 39249084983 scopus 로고    scopus 로고
    • Gene-environment interactions modulating cognitive function and molecular correlates of synaptic plasticity in Huntington's disease transgenic mice
    • Nithianantharajah J., Barkus C., Murphy M., Hannan A.J. Gene-environment interactions modulating cognitive function and molecular correlates of synaptic plasticity in Huntington's disease transgenic mice. Neurobiol. Dis. 2008, 29:490-504.
    • (2008) Neurobiol. Dis. , vol.29 , pp. 490-504
    • Nithianantharajah, J.1    Barkus, C.2    Murphy, M.3    Hannan, A.J.4
  • 154
    • 0033568842 scopus 로고    scopus 로고
    • Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit
    • Okabe S., Miwa A., Okado H. Alternative splicing of the C-terminal domain regulates cell surface expression of the NMDA receptor NR1 subunit. J. Neurosci. 1999, 19:7781-7792.
    • (1999) J. Neurosci. , vol.19 , pp. 7781-7792
    • Okabe, S.1    Miwa, A.2    Okado, H.3
  • 156
    • 34548814154 scopus 로고    scopus 로고
    • A pilot study of the clinical efficacy and safety of memantine for Huntington's disease
    • Ondo W.G., Mejia N.I., Hunter C.B. A pilot study of the clinical efficacy and safety of memantine for Huntington's disease. Parkinsonism Relat. Disord. 2007, 13:453-454.
    • (2007) Parkinsonism Relat. Disord. , vol.13 , pp. 453-454
    • Ondo, W.G.1    Mejia, N.I.2    Hunter, C.B.3
  • 158
    • 33846920665 scopus 로고    scopus 로고
    • NMDA receptor subunits: function and pharmacology
    • Paoletti P., Neyton J. NMDA receptor subunits: function and pharmacology. Curr. Opin. Pharmacol. 2007, 7:39-47.
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 39-47
    • Paoletti, P.1    Neyton, J.2
  • 159
    • 35948937549 scopus 로고    scopus 로고
    • The dichotomy of NMDA receptor signaling
    • Papadia S., Hardingham G.E. The dichotomy of NMDA receptor signaling. Neuroscientist 2007, 13:572-579.
    • (2007) Neuroscientist , vol.13 , pp. 572-579
    • Papadia, S.1    Hardingham, G.E.2
  • 161
    • 34948842904 scopus 로고    scopus 로고
    • Memantine: a NMDA receptor antagonist that improves memory by restoration of homeostasis in the glutamatergic system-too little activation is bad, too much is even worse
    • Parsons C.G., Stoffler A., Danysz W. Memantine: a NMDA receptor antagonist that improves memory by restoration of homeostasis in the glutamatergic system-too little activation is bad, too much is even worse. Neuropharmacology 2007, 53:699-723.
    • (2007) Neuropharmacology , vol.53 , pp. 699-723
    • Parsons, C.G.1    Stoffler, A.2    Danysz, W.3
  • 166
    • 20444397745 scopus 로고    scopus 로고
    • Ontogeny of postsynaptic density proteins at glutamatergic synapses
    • Petralia R.S., Sans N., Wang Y.X., Wenthold R.J. Ontogeny of postsynaptic density proteins at glutamatergic synapses. Mol. Cell. Neurosci. 2005, 29:436-452.
    • (2005) Mol. Cell. Neurosci. , vol.29 , pp. 436-452
    • Petralia, R.S.1    Sans, N.2    Wang, Y.X.3    Wenthold, R.J.4
  • 168
    • 0346158326 scopus 로고    scopus 로고
    • Internalization at glutamatergic synapses during development
    • Petralia R.S., Wang Y.X., Wenthold R.J. Internalization at glutamatergic synapses during development. Eur. J. Neurosci. 2003, 18:3207-3217.
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 3207-3217
    • Petralia, R.S.1    Wang, Y.X.2    Wenthold, R.J.3
  • 169
    • 78649994240 scopus 로고    scopus 로고
    • NR2B-NMDA receptor mediated modulation of the tyrosine phosphatase STEP regulates glutamate induced neuronal cell death
    • Poddar R., Deb I., Mukherjee S., Paul S. NR2B-NMDA receptor mediated modulation of the tyrosine phosphatase STEP regulates glutamate induced neuronal cell death. J. Neurochem. 2010, 115:1350-1362.
    • (2010) J. Neurochem. , vol.115 , pp. 1350-1362
    • Poddar, R.1    Deb, I.2    Mukherjee, S.3    Paul, S.4
  • 170
    • 24644491679 scopus 로고    scopus 로고
    • The synaptic localization of NR2B-containing NMDA receptors is controlled by interactions with PDZ proteins and AP-2
    • Prybylowski K., Chang K., Sans N., Kan L., Vicini S., Wenthold R.J. The synaptic localization of NR2B-containing NMDA receptors is controlled by interactions with PDZ proteins and AP-2. Neuron 2005, 47:845-857.
    • (2005) Neuron , vol.47 , pp. 845-857
    • Prybylowski, K.1    Chang, K.2    Sans, N.3    Kan, L.4    Vicini, S.5    Wenthold, R.J.6
  • 171
    • 4344717226 scopus 로고    scopus 로고
    • Lateral organization of endocytic machinery in dendritic spines
    • Racz B., Blanpied T.A., Ehlers M.D., Weinberg R.J. Lateral organization of endocytic machinery in dendritic spines. Nat. Neurosci. 2004, 7:917-918.
    • (2004) Nat. Neurosci. , vol.7 , pp. 917-918
    • Racz, B.1    Blanpied, T.A.2    Ehlers, M.D.3    Weinberg, R.J.4
  • 173
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1999, 1451:1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 175
    • 0034770032 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of ionotropic glutamate receptors by Fyn or Src differentially modulates their susceptibility to calpain and enhances their binding to spectrin and PSD-95
    • Rong Y., Lu X., Bernard A., Khrestchatisky M., Baudry M. Tyrosine phosphorylation of ionotropic glutamate receptors by Fyn or Src differentially modulates their susceptibility to calpain and enhances their binding to spectrin and PSD-95. J. Neurochem. 2001, 79:382-390.
    • (2001) J. Neurochem. , vol.79 , pp. 382-390
    • Rong, Y.1    Lu, X.2    Bernard, A.3    Khrestchatisky, M.4    Baudry, M.5
  • 176
    • 0028965220 scopus 로고
    • Synaptic NMDA receptor channels have a low open probability
    • Rosenmund C., Feltz A., Westbrook G.L. Synaptic NMDA receptor channels have a low open probability. J. Neurosci. 1995, 15:2788-2795.
    • (1995) J. Neurosci. , vol.15 , pp. 2788-2795
    • Rosenmund, C.1    Feltz, A.2    Westbrook, G.L.3
  • 178
    • 0034143323 scopus 로고    scopus 로고
    • A developmental change in NMDA receptor-associated proteins at hippocampal synapses
    • Sans N., Petralia R.S., Wang Y.X., Blahos J., Hell J.W., Wenthold R.J. A developmental change in NMDA receptor-associated proteins at hippocampal synapses. J. Neurosci. 2000, 20:1260-1271.
    • (2000) J. Neurosci. , vol.20 , pp. 1260-1271
    • Sans, N.1    Petralia, R.S.2    Wang, Y.X.3    Blahos, J.4    Hell, J.W.5    Wenthold, R.J.6
  • 179
    • 77956998216 scopus 로고    scopus 로고
    • Casein kinase 2 regulates the NR2 subunit composition of synaptic NMDA receptors
    • Sanz-Clemente A., Matta J.A., Isaac J.T., Roche K.W. Casein kinase 2 regulates the NR2 subunit composition of synaptic NMDA receptors. Neuron 2010, 67:984-996.
    • (2010) Neuron , vol.67 , pp. 984-996
    • Sanz-Clemente, A.1    Matta, J.A.2    Isaac, J.T.3    Roche, K.W.4
  • 180
    • 1542614144 scopus 로고    scopus 로고
    • Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors
    • Scott D.B., Blanpied T.A., Ehlers M.D. Coordinated PKA and PKC phosphorylation suppresses RXR-mediated ER retention and regulates the surface delivery of NMDA receptors. Neuropharmacology 2003, 45:755-767.
    • (2003) Neuropharmacology , vol.45 , pp. 755-767
    • Scott, D.B.1    Blanpied, T.A.2    Ehlers, M.D.3
  • 181
    • 4143131141 scopus 로고    scopus 로고
    • Endocytosis and degradative sorting of NMDA receptors by conserved membrane-proximal signals
    • Scott D.B., Michailidis I., Mu Y., Logothetis D., Ehlers M.D. Endocytosis and degradative sorting of NMDA receptors by conserved membrane-proximal signals. J. Neurosci. 2004, 24:7096-7109.
    • (2004) J. Neurosci. , vol.24 , pp. 7096-7109
    • Scott, D.B.1    Michailidis, I.2    Mu, Y.3    Logothetis, D.4    Ehlers, M.D.5
  • 182
    • 0034625631 scopus 로고    scopus 로고
    • Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport
    • Setou M., Nakagawa T., Seog D.H., Hirokawa N. Kinesin superfamily motor protein KIF17 and mLin-10 in NMDA receptor-containing vesicle transport. Science 2000, 288:1796-1802.
    • (2000) Science , vol.288 , pp. 1796-1802
    • Setou, M.1    Nakagawa, T.2    Seog, D.H.3    Hirokawa, N.4
  • 183
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar G.M., Bloodgood B.L., Townsend M., Walsh D.M., Selkoe D.J., Sabatini B.L. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 2007, 27:2866-2875.
    • (2007) J. Neurosci. , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.L.6
  • 184
    • 30744437894 scopus 로고    scopus 로고
    • Striatal neuronal apoptosis is preferentially enhanced by NMDA receptor activation in YAC transgenic mouse model of Huntington disease
    • Shehadeh J., Fernandes H.B., Zeron Mullins M.M., Graham R.K., Leavitt B.R., Hayden M.R., Raymond L.A. Striatal neuronal apoptosis is preferentially enhanced by NMDA receptor activation in YAC transgenic mouse model of Huntington disease. Neurobiol. Dis. 2006, 21:392-403.
    • (2006) Neurobiol. Dis. , vol.21 , pp. 392-403
    • Shehadeh, J.1    Fernandes, H.B.2    Zeron Mullins, M.M.3    Graham, R.K.4    Leavitt, B.R.5    Hayden, M.R.6    Raymond, L.A.7
  • 185
    • 0028219211 scopus 로고
    • Changing subunit composition of heteromeric NMDA receptors during development of rat cortex
    • Sheng M., Cummings J., Roldan L.A., Jan Y.N., Jan L.Y. Changing subunit composition of heteromeric NMDA receptors during development of rat cortex. Nature 1994, 368:144-147.
    • (1994) Nature , vol.368 , pp. 144-147
    • Sheng, M.1    Cummings, J.2    Roldan, L.A.3    Jan, Y.N.4    Jan, L.Y.5
  • 186
    • 0343192494 scopus 로고    scopus 로고
    • Growth of the NMDA receptor industrial complex
    • Sheng M., Lee S.H. Growth of the NMDA receptor industrial complex. Nat. Neurosci. 2000, 3:633-635.
    • (2000) Nat. Neurosci. , vol.3 , pp. 633-635
    • Sheng, M.1    Lee, S.H.2
  • 187
    • 0033860051 scopus 로고    scopus 로고
    • Ligand-gated ion channel interactions with cytoskeletal and signaling proteins
    • Sheng M., Pak D.T. Ligand-gated ion channel interactions with cytoskeletal and signaling proteins. Annu. Rev. Physiol. 2000, 62:755-778.
    • (2000) Annu. Rev. Physiol. , vol.62 , pp. 755-778
    • Sheng, M.1    Pak, D.T.2
  • 191
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: regulation and function
    • Smotrys J.E., Linder M.E. Palmitoylation of intracellular signaling proteins: regulation and function. Annu. Rev. Biochem. 2004, 73:559-587.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 193
    • 0033514448 scopus 로고    scopus 로고
    • Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
    • Song J.Y., Ichtchenko K., Sudhof T.C., Brose N. Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses. Proc Natl Acad Sci USA 1999, 96:1100-1105.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1100-1105
    • Song, J.Y.1    Ichtchenko, K.2    Sudhof, T.C.3    Brose, N.4
  • 196
    • 0034659803 scopus 로고    scopus 로고
    • C-Terminal truncation of NR2A subunits impairs synaptic but not extrasynaptic localization of NMDA receptors
    • Steigerwald F., Schulz T.W., Schenker L.T., Kennedy M.B., Seeburg P.H., Kohr G. C-Terminal truncation of NR2A subunits impairs synaptic but not extrasynaptic localization of NMDA receptors. J. Neurosci. 2000, 20:4573-4581.
    • (2000) J. Neurosci. , vol.20 , pp. 4573-4581
    • Steigerwald, F.1    Schulz, T.W.2    Schenker, L.T.3    Kennedy, M.B.4    Seeburg, P.H.5    Kohr, G.6
  • 197
    • 42949104029 scopus 로고    scopus 로고
    • Assembly and forward trafficking of NMDA receptors (review)
    • Stephenson F.A., Cousins S.L., Kenny A.V. Assembly and forward trafficking of NMDA receptors (review). Mol. Membr. Biol. 2008, 25:311-320.
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 311-320
    • Stephenson, F.A.1    Cousins, S.L.2    Kenny, A.V.3
  • 198
    • 66749167799 scopus 로고    scopus 로고
    • Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity
    • Subramaniam S., Sixt K.M., Barrow R., Snyder S.H. Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity. Science 2009, 324:1327-1330.
    • (2009) Science , vol.324 , pp. 1327-1330
    • Subramaniam, S.1    Sixt, K.M.2    Barrow, R.3    Snyder, S.H.4
  • 199
    • 0035816627 scopus 로고    scopus 로고
    • Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-d-aspartate receptors via post-synaptic density 95
    • Sun Y., Savanenin A., Reddy P.H., Liu Y.F. Polyglutamine-expanded huntingtin promotes sensitization of N-methyl-d-aspartate receptors via post-synaptic density 95. J. Biol. Chem. 2001, 276:24713-24718.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24713-24718
    • Sun, Y.1    Savanenin, A.2    Reddy, P.H.3    Liu, Y.F.4
  • 200
    • 0037127073 scopus 로고    scopus 로고
    • Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors
    • Takasu M.A., Dalva M.B., Zigmond R.E., Greenberg M.E. Modulation of NMDA receptor-dependent calcium influx and gene expression through EphB receptors. Science 2002, 295:491-495.
    • (2002) Science , vol.295 , pp. 491-495
    • Takasu, M.A.1    Dalva, M.B.2    Zigmond, R.E.3    Greenberg, M.E.4
  • 201
    • 0033582266 scopus 로고    scopus 로고
    • PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-d-aspartate receptor subunit NR2A
    • Tezuka T., Umemori H., Akiyama T., Nakanishi S., Yamamoto T. PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-d-aspartate receptor subunit NR2A. Proc Natl Acad Sci USA 1999, 96:435-440.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 435-440
    • Tezuka, T.1    Umemori, H.2    Akiyama, T.3    Nakanishi, S.4    Yamamoto, T.5
  • 202
    • 33645822456 scopus 로고    scopus 로고
    • Synaptic and extrasynaptic NMDA receptor NR2 subunits in cultured hippocampal neurons
    • Thomas C.G., Miller A.J., Westbrook G.L. Synaptic and extrasynaptic NMDA receptor NR2 subunits in cultured hippocampal neurons. J. Neurophysiol. 2006, 95:1727-1734.
    • (2006) J. Neurophysiol. , vol.95 , pp. 1727-1734
    • Thomas, C.G.1    Miller, A.J.2    Westbrook, G.L.3
  • 203
    • 0031040615 scopus 로고    scopus 로고
    • Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-d-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies
    • Tingley W.G., Ehlers M.D., Kameyama K., Doherty C., Ptak J.B., Riley C.T., Huganir R.L. Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-d-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies. J. Biol. Chem. 1997, 272:5157-5166.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5157-5166
    • Tingley, W.G.1    Ehlers, M.D.2    Kameyama, K.3    Doherty, C.4    Ptak, J.B.5    Riley, C.T.6    Huganir, R.L.7
  • 204
    • 0033562610 scopus 로고    scopus 로고
    • The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro
    • Tovar K.R., Westbrook G.L. The incorporation of NMDA receptors with a distinct subunit composition at nascent hippocampal synapses in vitro. J. Neurosci. 1999, 19:4180-4188.
    • (1999) J. Neurosci. , vol.19 , pp. 4180-4188
    • Tovar, K.R.1    Westbrook, G.L.2
  • 205
    • 0037061686 scopus 로고    scopus 로고
    • Mobile NMDA receptors at hippocampal synapses
    • Tovar K.R., Westbrook G.L. Mobile NMDA receptors at hippocampal synapses. Neuron 2002, 34:255-264.
    • (2002) Neuron , vol.34 , pp. 255-264
    • Tovar, K.R.1    Westbrook, G.L.2
  • 206
    • 0037417988 scopus 로고    scopus 로고
    • Developmental loss of miniature N-methyl-d-aspartate receptor currents in NR2A knockout mice
    • Townsend M., Yoshii A., Mishina M., Constantine-Paton M. Developmental loss of miniature N-methyl-d-aspartate receptor currents in NR2A knockout mice. Proc Natl Acad Sci USA 2003, 100:1340-1345.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1340-1345
    • Townsend, M.1    Yoshii, A.2    Mishina, M.3    Constantine-Paton, M.4
  • 207
    • 48749085218 scopus 로고    scopus 로고
    • New concepts in synaptic biology derived from single-molecule imaging
    • Triller A., Choquet D. New concepts in synaptic biology derived from single-molecule imaging. Neuron 2008, 59:359-374.
    • (2008) Neuron , vol.59 , pp. 359-374
    • Triller, A.1    Choquet, D.2
  • 209
    • 36348975209 scopus 로고    scopus 로고
    • Glutamate transporters: confining runaway excitation by shaping synaptic transmission
    • Tzingounis A.V., Wadiche J.I. Glutamate transporters: confining runaway excitation by shaping synaptic transmission. Nat. Rev. Neurosci. 2007, 8:935-947.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 935-947
    • Tzingounis, A.V.1    Wadiche, J.I.2
  • 211
    • 17644368893 scopus 로고    scopus 로고
    • Cognitive dysfunction precedes neuropathology and motor abnormalities in the YAC128 mouse model of Huntington's disease
    • Van Raamsdonk J.M., Pearson J., Slow E.J., Hossain S.M., Leavitt B.R., Hayden M.R. Cognitive dysfunction precedes neuropathology and motor abnormalities in the YAC128 mouse model of Huntington's disease. J. Neurosci. 2005, 25:4169-4180.
    • (2005) J. Neurosci. , vol.25 , pp. 4169-4180
    • Van Raamsdonk, J.M.1    Pearson, J.2    Slow, E.J.3    Hossain, S.M.4    Leavitt, B.R.5    Hayden, M.R.6
  • 214
    • 0141542665 scopus 로고    scopus 로고
    • Cdk5 activation induces hippocampal CA1 cell death by directly phosphorylating NMDA receptors
    • Wang J., Liu S., Fu Y., Wang J.H., Lu Y. Cdk5 activation induces hippocampal CA1 cell death by directly phosphorylating NMDA receptors. Nat. Neurosci. 2003, 6:1039-1047.
    • (2003) Nat. Neurosci. , vol.6 , pp. 1039-1047
    • Wang, J.1    Liu, S.2    Fu, Y.3    Wang, J.H.4    Lu, Y.5
  • 215
    • 0036323370 scopus 로고    scopus 로고
    • Rapid recruitment of NMDA receptor transport packets to nascent synapses
    • Washbourne P., Bennett J.E., McAllister A.K. Rapid recruitment of NMDA receptor transport packets to nascent synapses. Nat. Neurosci. 2002, 5:751-759.
    • (2002) Nat. Neurosci. , vol.5 , pp. 751-759
    • Washbourne, P.1    Bennett, J.E.2    McAllister, A.K.3
  • 216
    • 4644310691 scopus 로고    scopus 로고
    • Cycling of NMDA receptors during trafficking in neurons before synapse formation
    • Washbourne P., Liu X.B., Jones E.G., McAllister A.K. Cycling of NMDA receptors during trafficking in neurons before synapse formation. J. Neurosci. 2004, 24:8253-8264.
    • (2004) J. Neurosci. , vol.24 , pp. 8253-8264
    • Washbourne, P.1    Liu, X.B.2    Jones, E.G.3    McAllister, A.K.4
  • 218
    • 0032527719 scopus 로고    scopus 로고
    • Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin
    • Wechsler A., Teichberg V.I. Brain spectrin binding to the NMDA receptor is regulated by phosphorylation, calcium and calmodulin. EMBO J. 1998, 17:3931-3939.
    • (1998) EMBO J. , vol.17 , pp. 3931-3939
    • Wechsler, A.1    Teichberg, V.I.2
  • 220
    • 3042662151 scopus 로고    scopus 로고
    • NR2B selective NMDA receptor antagonist CP-101,606 prevents levodopa-induced motor response alterations in hemi-parkinsonian rats
    • Wessell R.H., Ahmed S.M., Menniti F.S., Dunbar G.L., Chase T.N., Oh J.D. NR2B selective NMDA receptor antagonist CP-101,606 prevents levodopa-induced motor response alterations in hemi-parkinsonian rats. Neuropharmacology 2004, 47:184-194.
    • (2004) Neuropharmacology , vol.47 , pp. 184-194
    • Wessell, R.H.1    Ahmed, S.M.2    Menniti, F.S.3    Dunbar, G.L.4    Chase, T.N.5    Oh, J.D.6
  • 222
    • 34547105826 scopus 로고    scopus 로고
    • Fyn-mediated phosphorylation of NR2B Tyr-1336 controls calpain-mediated NR2B cleavage in neurons and heterologous systems
    • Wu H.Y., Hsu F.C., Gleichman A.J., Baconguis I., Coulter D.A., Lynch D.R. Fyn-mediated phosphorylation of NR2B Tyr-1336 controls calpain-mediated NR2B cleavage in neurons and heterologous systems. J. Biol. Chem. 2007, 282:20075-20087.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20075-20087
    • Wu, H.Y.1    Hsu, F.C.2    Gleichman, A.J.3    Baconguis, I.4    Coulter, D.A.5    Lynch, D.R.6
  • 223
    • 0031013896 scopus 로고    scopus 로고
    • Competitive binding of alpha-actinin and calmodulin to the NMDA receptor
    • Wyszynski M., Lin J., Rao A., Nigh E., Beggs A.H., Craig A.M., Sheng M. Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. Nature 1997, 385:439-442.
    • (1997) Nature , vol.385 , pp. 439-442
    • Wyszynski, M.1    Lin, J.2    Rao, A.3    Nigh, E.4    Beggs, A.H.5    Craig, A.M.6    Sheng, M.7
  • 226
    • 0037418013 scopus 로고    scopus 로고
    • Eye opening induces a rapid dendritic localization of PSD-95 in central visual neurons
    • Yoshii A., Sheng M.H., Constantine-Paton M. Eye opening induces a rapid dendritic localization of PSD-95 in central visual neurons. Proc Natl Acad Sci USA 2003, 100:1334-1339.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1334-1339
    • Yoshii, A.1    Sheng, M.H.2    Constantine-Paton, M.3
  • 227
    • 47949102102 scopus 로고    scopus 로고
    • Postsynaptic density-95 (PSD-95) and calcineurin control the sensitivity of N-methyl-d-aspartate receptors to calpain cleavage in cortical neurons
    • Yuen E.Y., Ren Y., Yan Z. Postsynaptic density-95 (PSD-95) and calcineurin control the sensitivity of N-methyl-d-aspartate receptors to calpain cleavage in cortical neurons. Mol. Pharmacol. 2008, 74:360-370.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 360-370
    • Yuen, E.Y.1    Ren, Y.2    Yan, Z.3
  • 228
    • 0037075624 scopus 로고    scopus 로고
    • Increased sensitivity to N-methyl-d-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease
    • Zeron M.M., Hansson O., Chen N., Wellington C.L., Leavitt B.R., Brundin P., Hayden M.R., Raymond L.A. Increased sensitivity to N-methyl-d-aspartate receptor-mediated excitotoxicity in a mouse model of Huntington's disease. Neuron 2002, 33:849-860.
    • (2002) Neuron , vol.33 , pp. 849-860
    • Zeron, M.M.1    Hansson, O.2    Chen, N.3    Wellington, C.L.4    Leavitt, B.R.5    Brundin, P.6    Hayden, M.R.7    Raymond, L.A.8
  • 229
    • 45049085513 scopus 로고    scopus 로고
    • Full length mutant huntingtin is required for altered Ca2+ signaling and apoptosis of striatal neurons in the YAC mouse model of Huntington's disease
    • Zhang H., Li Q., Graham R.K., Slow E., Hayden M.R., Bezprozvanny I. Full length mutant huntingtin is required for altered Ca2+ signaling and apoptosis of striatal neurons in the YAC mouse model of Huntington's disease. Neurobiol. Dis. 2008, 31:80-88.
    • (2008) Neurobiol. Dis. , vol.31 , pp. 80-88
    • Zhang, H.1    Li, Q.2    Graham, R.K.3    Slow, E.4    Hayden, M.R.5    Bezprozvanny, I.6
  • 230
    • 33748314491 scopus 로고    scopus 로고
    • Distinct perisynaptic and synaptic localization of NMDA and AMPA receptors on ganglion cells in rat retina
    • Zhang J., Diamond J.S. Distinct perisynaptic and synaptic localization of NMDA and AMPA receptors on ganglion cells in rat retina. J. Comp. Neurol. 2006, 498:810-820.
    • (2006) J. Comp. Neurol. , vol.498 , pp. 810-820
    • Zhang, J.1    Diamond, J.S.2
  • 231
    • 38349009068 scopus 로고    scopus 로고
    • Cdk5 regulates the phosphorylation of tyrosine 1472 NR2B and the surface expression of NMDA receptors
    • Zhang S., Edelmann L., Liu J., Crandall J.E., Morabito M.A. Cdk5 regulates the phosphorylation of tyrosine 1472 NR2B and the surface expression of NMDA receptors. J. Neurosci. 2008, 28:415-424.
    • (2008) J. Neurosci. , vol.28 , pp. 415-424
    • Zhang, S.1    Edelmann, L.2    Liu, J.3    Crandall, J.E.4    Morabito, M.A.5
  • 232
    • 33846847943 scopus 로고    scopus 로고
    • Decoding NMDA receptor signaling: identification of genomic programs specifying neuronal survival and death
    • Zhang S.J., Steijaert M.N., Lau D., Schutz G., Delucinge-Vivier C., Descombes P., Bading H. Decoding NMDA receptor signaling: identification of genomic programs specifying neuronal survival and death. Neuron 2007, 53:549-562.
    • (2007) Neuron , vol.53 , pp. 549-562
    • Zhang, S.J.1    Steijaert, M.N.2    Lau, D.3    Schutz, G.4    Delucinge-Vivier, C.5    Descombes, P.6    Bading, H.7
  • 234
    • 41149121009 scopus 로고    scopus 로고
    • Synaptic metaplasticity through NMDA receptor lateral diffusion
    • Zhao J., Peng Y., Xu Z., Chen R.Q., Gu Q.H., Chen Z., Lu W. Synaptic metaplasticity through NMDA receptor lateral diffusion. J. Neurosci. 2008, 28:3060-3070.
    • (2008) J. Neurosci. , vol.28 , pp. 3060-3070
    • Zhao, J.1    Peng, Y.2    Xu, Z.3    Chen, R.Q.4    Gu, Q.H.5    Chen, Z.6    Lu, W.7
  • 235
    • 77955643169 scopus 로고    scopus 로고
    • Molecular mechanisms and potential therapeutical targets in Huntington's disease
    • Zuccato C., Valenza M., Cattaneo E. Molecular mechanisms and potential therapeutical targets in Huntington's disease. Physiol. Rev. 2010, 90:905-981.
    • (2010) Physiol. Rev. , vol.90 , pp. 905-981
    • Zuccato, C.1    Valenza, M.2    Cattaneo, E.3


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