메뉴 건너뛰기




Volumn 51, Issue 2, 2012, Pages 95-106

Amyloid beta peptide 1-42 disturbs intracellular calcium homeostasis through activation of GluN2B-containing N-methyl-d-aspartate receptors in cortical cultures

Author keywords

Alzheimer's disease; Amyloid beta peptide (A ); Calcium; GluN2A subunit; GluN2B subunit; N Methyl d aspartate receptor

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; CALCIUM ION; GLUN1 PROTEIN; GLUN2A PROTEIN; GLUN2B PROTEIN; N METHYL DEXTRO ASPARTIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; RECEPTOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84856958510     PISSN: 01434160     EISSN: 15321991     Source Type: Journal    
DOI: 10.1016/j.ceca.2011.11.008     Document Type: Article
Times cited : (155)

References (57)
  • 2
    • 0344845132 scopus 로고    scopus 로고
    • Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease
    • Oddo S., Caccamo A., Kitazawa M., Tseng B.P., LaFerla F.M. Amyloid deposition precedes tangle formation in a triple transgenic model of Alzheimer's disease. Neurobiol. Aging 2003, 24:1063-1070.
    • (2003) Neurobiol. Aging , vol.24 , pp. 1063-1070
    • Oddo, S.1    Caccamo, A.2    Kitazawa, M.3    Tseng, B.P.4    LaFerla, F.M.5
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 4
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin Notch, and the genesis and treatment of Alzheimer's disease
    • Selkoe D.J., Presenilin Notch, and the genesis and treatment of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:11039-11041.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 5
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren K.N., Manelli A.M., Stine W.B., Baker L.K., Krafft G.A., LaDu M.J. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J. Biol. Chem. 2002, 277:32046-32053.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 6
    • 0026570528 scopus 로고
    • Beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 1992, 12:376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 7
    • 33748792254 scopus 로고    scopus 로고
    • Beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-d-aspartate receptors in hippocampal neurons
    • Kelly B.L., Ferreira A. beta-Amyloid-induced dynamin 1 degradation is mediated by N-methyl-d-aspartate receptors in hippocampal neurons. J. Biol. Chem. 2006, 281:28079-28089.
    • (2006) J. Biol. Chem. , vol.281 , pp. 28079-28089
    • Kelly, B.L.1    Ferreira, A.2
  • 9
    • 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., et al. 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
  • 10
    • 50249135503 scopus 로고    scopus 로고
    • Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease
    • Bezprozvanny I., Mattson M.P. Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease. Trends Neurosci. 2008, 31:454-463.
    • (2008) Trends Neurosci. , vol.31 , pp. 454-463
    • Bezprozvanny, I.1    Mattson, M.P.2
  • 11
  • 12
    • 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., et al. 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
  • 13
    • 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
  • 14
    • 65249093004 scopus 로고    scopus 로고
    • A role for synaptic zinc in activity-dependent Abeta oligomer formation and accumulation at excitatory synapses
    • Deshpande A., Kawai H., Metherate R., Glabe C.G., Busciglio J. A role for synaptic zinc in activity-dependent Abeta oligomer formation and accumulation at excitatory synapses. J. Neurosci. 2009, 29:4004-4015.
    • (2009) J. Neurosci. , vol.29 , pp. 4004-4015
    • Deshpande, A.1    Kawai, H.2    Metherate, R.3    Glabe, C.G.4    Busciglio, J.5
  • 15
    • 33745268224 scopus 로고    scopus 로고
    • Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons
    • Deshpande A., Mina E., Glabe C., Busciglio J. Different conformations of amyloid beta induce neurotoxicity by distinct mechanisms in human cortical neurons. J. Neurosci. 2006, 26:6011-6018.
    • (2006) J. Neurosci. , vol.26 , pp. 6011-6018
    • Deshpande, A.1    Mina, E.2    Glabe, C.3    Busciglio, J.4
  • 16
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne S., Koh M.T., Kotilinek L., et al. A specific amyloid-beta protein assembly in the brain impairs memory. Nature 2006, 440:352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 17
    • 49249118742 scopus 로고    scopus 로고
    • Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death
    • Resende R., Ferreiro E., Pereira C., Resende de O.C. Neurotoxic effect of oligomeric and fibrillar species of amyloid-beta peptide 1-42: involvement of endoplasmic reticulum calcium release in oligomer-induced cell death. Neuroscience 2008, 155:725-737.
    • (2008) Neuroscience , vol.155 , pp. 725-737
    • Resende, R.1    Ferreiro, E.2    Pereira, C.3    Resende de, O.C.4
  • 18
    • 33751106208 scopus 로고    scopus 로고
    • Abeta42 is more rigid than Abeta40 at the C terminus: implications for Abeta aggregation and toxicity
    • Yan Y., Wang C. Abeta42 is more rigid than Abeta40 at the C terminus: implications for Abeta aggregation and toxicity. J. Mol. Biol. 2006, 364:853-862.
    • (2006) J. Mol. Biol. , vol.364 , pp. 853-862
    • Yan, Y.1    Wang, C.2
  • 19
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by amyloid-beta
    • Snyder E.M., Nong Y., Almeida C.G., et al. Regulation of NMDA receptor trafficking by amyloid-beta. Nat. Neurosci. 2005, 8:1051-1058.
    • (2005) Nat. Neurosci. , vol.8 , pp. 1051-1058
    • Snyder, E.M.1    Nong, Y.2    Almeida, C.G.3
  • 20
    • 28644442772 scopus 로고    scopus 로고
    • Modelling of amyloid beta-peptide induced lesions using roller-drum incubation of hippocampal slice cultures from neonatal rats
    • Johansson S., Radesater A.C., Cowburn R.F., Thyberg J., Luthman J. Modelling of amyloid beta-peptide induced lesions using roller-drum incubation of hippocampal slice cultures from neonatal rats. Exp. Brain Res. 2006, 168:11-24.
    • (2006) Exp. Brain Res. , vol.168 , pp. 11-24
    • Johansson, S.1    Radesater, A.C.2    Cowburn, R.F.3    Thyberg, J.4    Luthman, J.5
  • 21
    • 33750379305 scopus 로고    scopus 로고
    • Amyloid beta-peptide preconditioning reduces glutamate-induced neurotoxicity by promoting endocytosis of NMDA receptor
    • Goto Y., Niidome T., Akaike A., Kihara T., Sugimoto H. Amyloid beta-peptide preconditioning reduces glutamate-induced neurotoxicity by promoting endocytosis of NMDA receptor. Biochem. Biophys. Res. Commun. 2006, 351:259-265.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 259-265
    • Goto, Y.1    Niidome, T.2    Akaike, A.3    Kihara, T.4    Sugimoto, H.5
  • 22
    • 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
  • 23
    • 16544376850 scopus 로고    scopus 로고
    • Role of distinct NMDA receptor subtypes at central synapses
    • 2004, re16
    • Cull-Candy S.G., Leszkiewicz D.N. Role of distinct NMDA receptor subtypes at central synapses. Sci. STKE 2004, 2004, re16.
    • (2004) Sci. STKE
    • Cull-Candy, S.G.1    Leszkiewicz, D.N.2
  • 24
    • 33748921093 scopus 로고    scopus 로고
    • NMDA receptor function: subunit composition versus spatial distribution
    • Kohr G. NMDA receptor function: subunit composition versus spatial distribution. Cell Tissue Res. 2006, 326:439-446.
    • (2006) Cell Tissue Res. , vol.326 , pp. 439-446
    • Kohr, G.1
  • 25
    • 70450182118 scopus 로고    scopus 로고
    • Coupling of the NMDA receptor to neuroprotective and neurodestructive events
    • Hardingham G.E. Coupling of the NMDA receptor to neuroprotective and neurodestructive events. Biochem. Soc. Trans. 2009, 37:1147-1160.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1147-1160
    • Hardingham, G.E.1
  • 26
    • 0242573273 scopus 로고    scopus 로고
    • The NMDA receptor is coupled to the ERK pathway by a direct interaction between NR2B and RasGRF1
    • Krapivinsky G., Krapivinsky L., Manasian Y., et al. The NMDA receptor is coupled to the ERK pathway by a direct interaction between NR2B and RasGRF1. Neuron 2003, 40:775-784.
    • (2003) Neuron , vol.40 , pp. 775-784
    • Krapivinsky, G.1    Krapivinsky, L.2    Manasian, Y.3
  • 27
    • 33947331063 scopus 로고    scopus 로고
    • NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo
    • Liu Y., Wong T.P., Aarts M., et al. NMDA receptor subunits have differential roles in mediating excitotoxic neuronal death both in vitro and in vivo. J. Neurosci. 2007, 27:2846-2857.
    • (2007) J. Neurosci. , vol.27 , pp. 2846-2857
    • Liu, Y.1    Wong, T.P.2    Aarts, M.3
  • 28
    • 19544367458 scopus 로고    scopus 로고
    • Differential roles of NR2A- and NR2B-containing NMDA receptors in Ras-ERK signaling and AMPA receptor trafficking
    • Kim M.J., Dunah A.W., Wang Y.T., Sheng M. Differential roles of NR2A- and NR2B-containing NMDA receptors in Ras-ERK signaling and AMPA receptor trafficking. Neuron 2005, 46:745-760.
    • (2005) Neuron , vol.46 , pp. 745-760
    • Kim, M.J.1    Dunah, A.W.2    Wang, Y.T.3    Sheng, M.4
  • 29
    • 0042536471 scopus 로고    scopus 로고
    • Neuronal and glial calcium signaling in Alzheimer's disease
    • Mattson M.P., Chan S.L. Neuronal and glial calcium signaling in Alzheimer's disease. Cell Calcium 2003, 34:385-397.
    • (2003) Cell Calcium , vol.34 , pp. 385-397
    • Mattson, M.P.1    Chan, S.L.2
  • 30
    • 47749095383 scopus 로고    scopus 로고
    • Linking calcium to Abeta and Alzheimer's disease
    • Green K.N., LaFerla F.M. Linking calcium to Abeta and Alzheimer's disease. Neuron 2008, 59:190-194.
    • (2008) Neuron , vol.59 , pp. 190-194
    • Green, K.N.1    LaFerla, F.M.2
  • 31
    • 0037363599 scopus 로고    scopus 로고
    • Involvement of calcineurin in the neurotoxic effects induced by amyloid-beta and prion peptides
    • Agostinho P., Oliveira C.R. Involvement of calcineurin in the neurotoxic effects induced by amyloid-beta and prion peptides. Eur. J. Neurosci. 2003, 17:1189-1196.
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 1189-1196
    • Agostinho, P.1    Oliveira, C.R.2
  • 32
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • Ferreiro E., Resende R., Costa R., Oliveira C.R., Pereira C.M. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol. Dis. 2006, 23:669-678.
    • (2006) Neurobiol. Dis. , vol.23 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.M.5
  • 33
    • 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., et al. 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
  • 34
    • 0037041183 scopus 로고    scopus 로고
    • 5-Phosphonomethylquinoxalinediones as competitive NMDA receptor antagonists with a preference for the human 1A/2A, rather than 1A/2B receptor composition
    • Auberson Y.P., Allgeier H., Bischoff S., Lingenhoehl K., Moretti R., Schmutz M. 5-Phosphonomethylquinoxalinediones as competitive NMDA receptor antagonists with a preference for the human 1A/2A, rather than 1A/2B receptor composition. Bioorg. Med. Chem. Lett. 2002, 12:1099-1102.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1099-1102
    • Auberson, Y.P.1    Allgeier, H.2    Bischoff, S.3    Lingenhoehl, K.4    Moretti, R.5    Schmutz, M.6
  • 35
    • 33747598487 scopus 로고    scopus 로고
    • Equilibrium constants for (R)-[(S)-1-(4-bromo-phenyl)-ethylamino]-(2,3-dioxo-1,2,3,4-tetrahydroquino xalin-5-yl)-methyl-phosphonic acid (NVP-AAM077) acting at recombinant NR1/NR2A and NR1/NR2B N-methyl-d-aspartate receptors: implications for studies of synaptic transmission
    • Frizelle P.A., Chen P.E., Wyllie D.J. Equilibrium constants for (R)-[(S)-1-(4-bromo-phenyl)-ethylamino]-(2,3-dioxo-1,2,3,4-tetrahydroquino xalin-5-yl)-methyl-phosphonic acid (NVP-AAM077) acting at recombinant NR1/NR2A and NR1/NR2B N-methyl-d-aspartate receptors: implications for studies of synaptic transmission. Mol. Pharmacol. 2006, 70:1022-1032.
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1022-1032
    • Frizelle, P.A.1    Chen, P.E.2    Wyllie, D.J.3
  • 36
    • 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. 1993, 44:851-859.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 851-859
    • Williams, K.1
  • 37
    • 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
  • 38
    • 33645010267 scopus 로고    scopus 로고
    • Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors
    • Zhou M., Baudry M. Developmental changes in NMDA neurotoxicity reflect developmental changes in subunit composition of NMDA receptors. J. Neurosci. 2006, 26:2956-2963.
    • (2006) J. Neurosci. , vol.26 , pp. 2956-2963
    • Zhou, M.1    Baudry, M.2
  • 40
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla F.M. Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat. Rev. Neurosci. 2002, 3:862-872.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 41
    • 23044514738 scopus 로고    scopus 로고
    • 2+ flux through individual ion channels with high temporal and spatial resolution
    • 2+ flux through individual ion channels with high temporal and spatial resolution. J. Biomed. Opt. 2005, 10:11002.
    • (2005) J. Biomed. Opt. , vol.10 , pp. 11002
    • Demuro, A.1    Parker, I.2
  • 42
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A., Mina E., Kayed R., Milton S.C., Parker I., Glabe C.G. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 2005, 280:17294-17300.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 43
    • 79953133327 scopus 로고    scopus 로고
    • Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species
    • Jan A., Adolfsson O., Allaman I., et al. Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species. J. Biol. Chem. 2011, 286:8585-8596.
    • (2011) J. Biol. Chem. , vol.286 , pp. 8585-8596
    • Jan, A.1    Adolfsson, O.2    Allaman, I.3
  • 44
    • 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
  • 46
    • 34248172476 scopus 로고    scopus 로고
    • Toxicity of beta-amyloid in HEK293 cells expressing NR1/NR2A or NR1/NR2B N-methyl-d-aspartate receptor subunits
    • Domingues A., Almeida S., da Cruz e Silva E.F., Oliveira C.R., Rego A.C. Toxicity of beta-amyloid in HEK293 cells expressing NR1/NR2A or NR1/NR2B N-methyl-d-aspartate receptor subunits. Neurochem. Int. 2007, 50:872-880.
    • (2007) Neurochem. Int. , vol.50 , pp. 872-880
    • Domingues, A.1    Almeida, S.2    da Cruz e Silva, E.F.3    Oliveira, C.R.4    Rego, A.C.5
  • 48
    • 77949267093 scopus 로고    scopus 로고
    • 2+ dysregulation and neuronal death through activation of ionotropic glutamate receptors
    • 2+ dysregulation and neuronal death through activation of ionotropic glutamate receptors. Cell Calcium 2010, 47:264-272.
    • (2010) Cell Calcium , vol.47 , pp. 264-272
    • Alberdi, E.1    Sanchez-Gomez, M.V.2    Cavaliere, F.3
  • 49
    • 27744527103 scopus 로고    scopus 로고
    • Divergent effects of Abeta1-42 on ionotropic glutamate receptor-mediated responses in CA1 neurons in vivo
    • Szegedi V., Juhasz G., Budai D., Penke B. Divergent effects of Abeta1-42 on ionotropic glutamate receptor-mediated responses in CA1 neurons in vivo. Brain Res. 2005, 1062:120-126.
    • (2005) Brain Res. , vol.1062 , pp. 120-126
    • Szegedi, V.1    Juhasz, G.2    Budai, D.3    Penke, B.4
  • 50
    • 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
  • 51
    • 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
  • 52
    • 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
  • 53
    • 34547228856 scopus 로고    scopus 로고
    • Excitotoxicity in vitro by NR2A- and NR2B-containing NMDA receptors
    • von Engelhardt J., Coserea I., Pawlak V., et al. Excitotoxicity in vitro by NR2A- and NR2B-containing NMDA receptors. Neuropharmacology 2007, 53:10-17.
    • (2007) Neuropharmacology , vol.53 , pp. 10-17
    • von Engelhardt, J.1    Coserea, I.2    Pawlak, V.3
  • 54
    • 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
  • 55
    • 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
  • 56
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.