The Role of NMDA Receptors in Alzheimer’s Disease
Open accessAbstract
In Alzheimer's disease (AD), early synaptic dysfunction is associated with the increased oligomeric amyloid-beta peptide, which causes NMDAR-dependent synaptic depression and spine elimination. Memantine, low-affinity NMDAR channel blocker, has been used in the treatment of moderate to severe AD. However, clear evidence is still deficient in demonstrating the underlying mechanisms and a relationship between NMDARs dysfunction and AD. This review focuses on not only changes in expression of different NMDAR subunits, but also some unconventional modes of NMDAR action.
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N-methyl-d-aspartate receptor (NMDAR) activation and related excitotoxic events that lead to synaptic dysfunction are associated with AD pathology.
“N-methyl-d-aspartate receptor (NMDAR) activation and related excitotoxic events that lead to synaptic dysfunction has also been associated with AD pathology (Liu et al. 2019).”
From Alzheimer’s disease: Targeting the glutamatergic system (2020) · cites this paper as Liu et al. 2019
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The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Glutamate neurotoxicity and diseases of the nervous system
Choi, D. W. (1988) · Neuron · doi:10.1016/0896-6273(88)90162-6 · Cited by 8,152 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Magnesium gates glutamate-activated channels in mouse central neurones
Nowak, L. M., Bregestovski, P. D., Ascher, P., Herbet, A., & Prochiantz, A. (1984) · Nature · doi:10.1038/307462a0 · Cited by 4,033 · see citing works
Malenka, R. C., & Bear, M. F. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.012 · Cited by 3,968 · see citing works
Glutamate Receptor Ion Channels: Structure, Regulation, and Function
Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., Hansen, K. B., Yuan, H., Myers, S. J., & Dingledine, R. (2010) · Pharmacological Reviews · doi:10.1124/pr.109.002451 · Cited by 3,568 · see citing works
Monyer, H., Burnashev, N., Laurie, D., Sakmann, B. J., & Seeburg, P. H. (1994) · Neuron · doi:10.1016/0896-6273(94)90210-0 · Cited by 3,469 · see citing works
Voltage-dependent block by Mg2+ of NMDA responses in spinal cord neurones
Mayer, M. L., Westbrook, G. L., & Guthrie, P. B. (1984) · Nature · doi:10.1038/309261a0 · Cited by 2,906 · see citing works
Excitatory Amino Acids as a Final Common Pathway for Neurologic Disorders
Epstein, F. H., Lipton, S. A., & Rosenberg, P. A. (1994) · New England Journal of Medicine · doi:10.1056/nejm199403033300907 · Cited by 2,644 · see citing works
Cellular functions regulated by Src family kinases.
Thomas, S. M., & Brugge, J. (1997) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.13.1.513 · Cited by 2,610 · see citing works
Molecular dissection of reactive astrogliosis and glial scar formation
Sofroniew, M. V. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2009.08.002 · Cited by 2,594 · see citing works
NMDA receptor subunit diversity: impact on receptor properties, synaptic plasticity and disease
Paoletti, P., Bellone, C., & Zhou, Q. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3504 · Cited by 2,523 · see citing works
Glutamate and the pathophysiology of hypoxic–ischemic brain damage
Rothman, S. M., & Olney, J. W. (1986) · Annals of Neurology · doi:10.1002/ana.410190202 · Cited by 2,428 · see citing works
Choi, D. W. (1992) · Journal of Neurobiology · doi:10.1002/neu.480230915 · Cited by 2,304 · see citing works
Bloom (2014) · doi:10.1001/jamaneurol.2013.5847 · Cited by 2,194 · see citing works
Memantine in Moderate-to-Severe Alzheimer's Disease
Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043 · see citing works
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942 · see citing works
Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · see citing works
Ionic dependence of glutamate neurotoxicity
Choi, D. W. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-02-00369.1987 · Cited by 1,854 · see citing works
MacDermott, A. B., Mayer, M. L., Westbrook, G. L., Smith, S. J., & Barker, J. L. (1986) · Nature · doi:10.1038/321519a0 · Cited by 1,835 · see citing works
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works
NMDA receptor subunits: diversity, development and disease
Cull-Candy, S., Brickley, S., & Farrant, M. (2001) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00215-4 · Cited by 1,694 · see citing works
Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
Hardingham, G. E., Fukunaga, Y., & Bading, H. (2002) · Nature Neuroscience · doi:10.1038/nn835 · Cited by 1,686 · see citing works
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,677 · see citing works
Palop, J. J., Chin, J., Roberson, E. D., Wang, J., Thwin, M. T., Bien-Ly, N., Yoo, J., Ho, K. O., Yu, G.-Q., Kreitzer, A., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.07.025 · Cited by 1,653 · see citing works
Amyloid-β–induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks
Palop, J. J., & Mucke, L. (2010) · Nature Neuroscience · doi:10.1038/nn.2583 · Cited by 1,651 · see citing works
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644 · see citing works
Synaptic versus extrasynaptic NMDA receptor signalling: implications for neurodegenerative disorders
Hardingham, G. E., & Bading, H. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2911 · Cited by 1,644 · cited 1× · see citing works
“Furthermore, taking into account the fact that extrasynaptic GluN2B-containing NMDARs have been associated with excitotoxicity in AD (Hardingham and Bading, 2010), the use of a selective GluN2B subunit antagonists might be an interesting strategy to prevent synaptic dysfunction in AD.”
BackgroundShankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592 · see citing works
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588 · see citing works
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · see citing works
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426 · see citing works
Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo
Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265 · see citing works
Ciabarra, A., Sullivan, J., Gahn, L. G., Pecht, G., Heinemann, S., & Sevarino, K. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-10-06498.1995 · Cited by 1,254 · see citing works
Lacor, P. N., Buniel, M. C., Furlow, P. W., Sanz Clemente, A., Velasco, P. T., Wood, M., Viola, K. L., & Klein, W. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3501-06.2007 · Cited by 1,188 · see citing works
The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease
Rogaeva, E., Meng, Y., Lee, J. H., Gu, Y., Kawarai, T., Zou, F., Katayama, T., Baldwin, C. T., Cheng, R., Hasegawa, H., et al. (2007) · Nature Genetics · doi:10.1038/ng1943 · Cited by 1,167 · see citing works
Self-citationIntracellular injections of EGTA block induction of hippocampal long-term potentiation
Lynch, G., Larson, J., Kelso, S., Barrionuevo, G., & Schottler, F. (1983) · Nature · doi:10.1038/305719a0 · Cited by 1,116 · see citing works
NMDA receptor-dependent long-term potentiation and long-term depression (LTP/LTD).
Luscher, C., & Malenka, R. C. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005710 · Cited by 1,110 · cited 1× · see citing works
“On the contrary, a modest activation of NMDARs causes a modest increase in postsynaptic Ca 2 + and triggers phosphatases-mediated LTD (Luscher and Malenka, 2012).”
BackgroundRole of NMDA Receptor Subtypes in Governing the Direction of Hippocampal Synaptic Plasticity
Liu, L., Wong, T. P., Pozza, M. F., Lingenhoehl, K., Wang, Y., Sheng, M., Auberson, Y. P., & Wang, Y. T. (2004) · Science · doi:10.1126/science.1096615 · Cited by 1,106 · see citing works
Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · see citing works
Treatment of Ischemic Brain Damage by Perturbing NMDA Receptor- PSD-95 Protein Interactions
Aarts, M., Liu, Y., Liu, L.-D., Besshoh, S., Arundine, M., Gurd, J. W., Wang, Y.-T., Salter, M., & Tymianski, M. (2002) · Science · doi:10.1126/science.1072873 · Cited by 1,048 · see citing works
AMPAR Removal Underlies Aβ-Induced Synaptic Depression and Dendritic Spine Loss
Hsieh, H., Boehm, J., Sato, C., Iwatsubo, T., Tomita, T., Sisodia, S., & Malinow, R. (2006) · Neuron · doi:10.1016/j.neuron.2006.10.035 · Cited by 1,042 · see citing works
Role of Glutamate and NMDA Receptors in Alzheimer’s Disease
Wang, R., & Reddy, P. H. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160763 · Cited by 1,009 · see citing works
Pharmacology of glutamate neurotoxicity in cortical cell culture: attenuation by NMDA antagonists
Choi, D. W., Koh, J., & Peters, S. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-01-00185.1988 · Cited by 983 · see citing works
Li, S., Hong, S., Shepardson, N. E., Walsh, D. M., Shankar, G. M., & Selkoe, D. (2009) · Neuron · doi:10.1016/j.neuron.2009.05.012 · Cited by 972 · see citing works
Fellin, T., Pascual, O., Gobbo, S., Pozzan, T., Haydon, P. G., & Carmignoto, G. (2004) · Neuron · doi:10.1016/j.neuron.2004.08.011 · Cited by 970 · see citing works
Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond
Lipton, S. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1958 · Cited by 909 · see citing works
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882 · see citing works
Williams, K. L. (1993) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13275-6 · Cited by 860 · see citing works
β-Amyloid1–42 Binds to α7 Nicotinic Acetylcholine Receptor with High Affinity
Wang, H.-Y., Lee, D. H. S., D’Andrea, M. R., Peterson, P. A., Shank, R. P., & Reitz, A. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5626 · Cited by 818 · see citing works
Glutamate exocytosis from astrocytes controls synaptic strength
Jourdain, P., Bergersen, L. H., Bhaukaurally, K., Bezzi, P., Santello, M., Domercq, M., Matute, C., Tonello, F., Gundersen, V., & Volterra, A. (2007) · Nature Neuroscience · doi:10.1038/nn1849 · Cited by 806 · see citing works
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783 · see citing works
Src kinases: a hub for NMDA receptor regulation
Salter, M. W., & Kalia, L. V. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1368 · Cited by 777 · see citing works
Liu, Y., Wong, T. P., Aarts, M., Rooyakkers, A., Liu, L., Lai, T. W., Wu, D. C., Lu, J., Tymianski, M., Craig, A. M., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.0116-07.2007 · Cited by 773 · see citing works
NMDA receptors are expressed in oligodendrocytes and activated in ischaemia
Káradóttir, R. T., Cavelier, P., Bergersen, L. H., & Attwell, D. (2005) · Nature · doi:10.1038/nature04302 · Cited by 773 · see citing works
Ras and Rap control AMPA receptor trafficking during synaptic plasticity
Zhu, J. J., Qin, Y., Zhao, M., Van Aelst, L., & Malinow, R. (2002) · Cell · doi:10.1016/s0092-8674(02)00897-8 · Cited by 769 · see citing works
Picomolar Amyloid-β Positively Modulates Synaptic Plasticity and Memory in Hippocampus
Puzzo, D., Privitera, L., Leznik, E., Fà, M., Staniszewski, A., Palmeri, A., & Arancio, O. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2692-08.2008 · Cited by 740 · see citing works
Synaptic and extrasynaptic NMDA receptors are gated by different endogenous coagonists.
Papouin, T., Ladépêche, L., Ruel, J., Sacchi, S., Labasque, M., Hanini, M., Groc, L., Pollegioni, L., Mothet, J., & Oliet, S. (2012) · Cell · doi:10.1016/j.cell.2012.06.029 · Cited by 728 · see citing works
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. S., Gale, N. W., & Greenberg, M. E. (2000) · Cell · doi:10.1016/s0092-8674(00)00197-5 · Cited by 716 · see citing works
NMDA Receptor Subunit Composition Controls Synaptic Plasticity by Regulating Binding to CaMKII
Barria, A., & Malinow, R. (2005) · Neuron · doi:10.1016/j.neuron.2005.08.034 · Cited by 709 · see citing works
Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides
Hartmann, T., Bieger, S. C., Brühl, B., Tienari, P. J., Ida, N., Allsop, D., Roberts, G. W., Masters, C. L., Dotti, C. G., Unsicker, K., et al. (1997) · Nature Medicine · doi:10.1038/nm0997-1016 · Cited by 706 · see citing works
Parsons, C. G., Stöffler, A., & Danysz, W. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2007.07.013 · Cited by 701 · see citing works
Excitatory glycine receptors containing the NR3 family of NMDA receptor subunits
Chatterton, J. E., Awobuluyi, M., Premkumar, L. S., Takahashi, H., Talantova, M. V., Shin, Y., Cui, J., Tu, S., Sevarino, K. A., Nakanishi, N., et al. (2002) · Nature · doi:10.1038/nature715 · Cited by 695 · see citing works
Massey, P. V., Johnson, B. E., Moult, P. R., Auberson, Y. P., Brown, M. W., Molnár, E., Collingridge, G. L., & Bashir, Z. I. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1697-04.2004 · Cited by 693 · see citing works
Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V., Ito, A., Winblad, B., Glaser, E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806192105 · Cited by 693 · see citing works
Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686 · cited 1× · see citing works
“Some experiments indicated that tau is normally highly enriched in axons relative to dendrites (Binder et al., 1985), but in response to Aβ is extensively redistributed into the somato-dendritic compartment (Delacourte et al., 1990; Zempel et al., 2010).”
BackgroundFunctional and Pharmacological Differences Between Recombinant N -Methyl- d -Aspartate Receptors
Vicini, S., Wang, J. F., Li, J. H., Zhu, W. J., Wang, Y. H., Luo, J. H., Wolfe, B. B., & Grayson, D. R. (1998) · Journal of Neurophysiology · doi:10.1152/jn.1998.79.2.555 · Cited by 674 · see citing works
Synaptic plasticity in the hippocampus: LTP and LTD
Malenka, R. C. (1994) · Cell · doi:10.1016/0092-8674(94)90517-7 · Cited by 655 · see citing works
Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A. O., Wısnıewskı, T., Gunther, E. C., & Strittmatter, S. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3178 · Cited by 654 · see citing works
High-Affinity Zinc Inhibition of NMDA NR1–NR2A Receptors
Paoletti, P., Ascher, P., & Neyton, J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05711.1997 · Cited by 650 · see citing works
Regulation of NMDA receptor subunit expression and its implications for LTD, LTP, and metaplasticity
Yashiro, K., & Philpot, B. D. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.07.046 · Cited by 649 · see citing works
Control of local protein synthesis and initial events in myelination by action potentials
Wake, H., Lee, P. R., & Fields, R. D. (2011) · Science · doi:10.1126/science.1206998 · Cited by 636 · see citing works
SynGAP: a Synaptic RasGAP that Associates with the PSD-95/SAP90 Protein Family
Kim, J. H., Liao, D., Lau, L.-F., & Huganir, R. L. (1998) · Neuron · doi:10.1016/s0896-6273(00)81008-9 · Cited by 634 · see citing works
Imaging the evolution and pathophysiology of Alzheimer disease
Jagust, W. (2018) · Nature Reviews Neuroscience · doi:10.1038/s41583-018-0067-3 · Cited by 604 · see citing works
Crystal structure of a heterotetrameric NMDA receptor ion channel
Karakaş, E., & Furukawa, H. (2014) · Science · doi:10.1126/science.1251915 · Cited by 600 · see citing works
Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572 · see citing works
Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells.
Busciglio, J., Gabuzda, D. H., Matsudaira, P., & Yankner, B. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.2092 · Cited by 569 · see citing works
Source specificity of early calcium neurotoxicity in cultured embryonic spinal neurons
Tymianski, M., Charlton, M. P., Carlen, P. L., & Tator, C. (1993) · Journal of Neuroscience · doi:10.1523/jneurosci.13-05-02085.1993 · Cited by 567 · see citing works
NMDA receptors are expressed in developing oligodendrocyte processes and mediate injury
Salter, M. G., & Fern, R. F. (2005) · Nature · doi:10.1038/nature04301 · Cited by 556 · see citing works
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. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-03-01260.2000 · Cited by 537 · see citing works
Subunit-Specific NMDA Receptor Trafficking to Synapses
Barria, A., & Malinow, R. (2002) · Neuron · doi:10.1016/s0896-6273(02)00776-6 · Cited by 515 · see citing works
Sumi, M., Kiuchi, K., Ishikawa, T., Ishii, A., Hagiwara, M., Nagatsu, T., & Hidaka, H. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)92031-e · Cited by 511 · see citing works
NMDA receptor structures reveal subunit arrangement and pore architecture
Lee, C.-H., Lü, W., Michel, J. J. C., Goehring, A. S., Du, J., Song, X., & Gouaux, E. (2014) · Nature · doi:10.1038/nature13548 · Cited by 511 · see citing works
Update on Alzheimer’s Disease Therapy and Prevention Strategies
Graham, W. V., Bonito-Oliva, A., & Sakmar, T. P. (2017) · Annual Review of Medicine · doi:10.1146/annurev-med-042915-103753 · Cited by 506 · see citing works
NMDA receptors mediate calcium accumulation in myelin during chemical ischaemia
Micu, I., Jiang, Q., Coderre, E., Ridsdale, A., Zhang, L., Woulfe, J., Yin, X., Trapp, B. D., McRory, J. E., Rehak, R., et al. (2005) · Nature · doi:10.1038/nature04474 · Cited by 504 · see citing works
The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain
Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 502 · see citing works
Danysz, W., & Parsons, C. G. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02057.x · Cited by 500 · see citing works
The mechanisms and functions of spontaneous neurotransmitter release
Kavalali, E. T. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3875 · Cited by 486 · see citing works
Fischer, G., Mutel, V., Trube, G., Malherbe, P., Kew, J. N. C., MOHACSI, E., Heitz, M., & Kemp, J. A. (1997) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)37138-1 · Cited by 480 · see citing works
Nakazawa, T., Komai, S., Tezuka, T., Hisatsune, C., Umemori, H., Semba, K., Mishina, M., Manabe, T., & Yamamoto, T. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008085200 · Cited by 466 · see citing works
Nagele, R. G., D’Andrea, M. R., Anderson, W. J., & Wang, H.-Y. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00460-2 · Cited by 456 · see citing works
Molecular basis of NMDA receptor functional diversity
Paoletti, P. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07628.x · Cited by 446 · see citing works
Tau interacts with src-family non-receptor tyrosine kinases
Lee, G. S., Newman, S. T., Gard, D. L., Band, H., & Panchamoorthy, G. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.21.3167 · Cited by 445 · see citing works
In vivo staging of regional amyloid deposition
Grothe, M. J., Barthel, H., Sepulcre, J., Dyrba, M., Sabri, O., Teipel, S. J., Initiative, F. T. A. D. N., Initiative, A. D. N., Weiner, M., Aisen, P., et al. (2017) · Neurology · doi:10.1212/wnl.0000000000004643 · Cited by 440 · see citing works
Cook, D. G., Forman, M. S., Sung, J. C., Leight, S., Kolson, D. L., Iwatsubo, T., Lee, V. M.-Y., & Doms, R. W. (1997) · Nature Medicine · doi:10.1038/nm0997-1021 · Cited by 439 · see citing works
The NMDA Receptor Is Coupled to the ERK Pathway by a Direct Interaction between NR2B and RasGRF1
Krapivinsky, G. B., Krapivinsky, L., Manasian, Y., Ivanov, A., Tyzio, R., Pellegrino, C., Ben‐Ari, Y., Clapham, D. E., & Medina, I. (2003) · Neuron · doi:10.1016/s0896-6273(03)00645-7 · Cited by 431 · see citing works
Erreger, K., Dravid, S. M., Banke, T. G., Wyllie, D. J. A., & Traynelis, S. F. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2004.080028 · Cited by 427 · see citing works
Sucher, N. J., Akbarian, S., Chi, C.-L., Leclerc, C., Awobuluyi, M., Deitcher, D. L., Wu, M., Yuan, J., Jones, E. G., & Lipton, S. A. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-10-06509.1995 · Cited by 420 · see citing works
Phosphorylation of Tau by Fyn: Implications for Alzheimer's Disease
Lee, G. S., Thangavel, R., Sharma, V. M., Litersky, J. M., Bhaskar, K., Fang, S. M., Lana, H., Andreadis, A., Hoesen, G. W. V., & Ksiȩżak-Reding, H. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4162-03.2004 · Cited by 414 · see citing works
N-Methyl-d-aspartate (NMDA) receptor function and excitotoxicity in Huntington's disease
FAN, M., & Raymond, L. A. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.11.003 · Cited by 410 · see citing works
Danysz, W., & Parsons, C. G. (2003) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.938 · Cited by 404 · see citing works
Diversity in NMDA Receptor Composition
Sanz-Clemente, A., Nicoll, R. A., & Roche, K. W. (2012) · The Neuroscientist · doi:10.1177/1073858411435129 · Cited by 397 · see citing works
Tezuka, T., Umemori, H., Akiyama, T., Nakanishi, S., & Yamamoto, T. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.435 · Cited by 377 · see citing works
NMDA receptor surface mobility depends on NR2A-2B subunits
Groc, L., Heine, M., Cousins, S. L., Stephenson, F. A., Lounis, B., Cognet, L., & Choquet, D. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605238103 · Cited by 376 · see citing works
Wu, H.-Y., Hudry, E., Hashimoto, T., Kuchibhotla, K., Rozkalne, A., Fan, Z., Spires-Jones, T., Xie, H., Arbel-Ornath, M., Grosskreutz, C. L., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4456-09.2010 · Cited by 367 · see citing works
Glutamate receptor dynamics in dendritic microdomains.
Newpher, T. M., & Ehlers, M. D. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.030 · Cited by 356 · see citing works
NMDA Receptors Mediate Neuron-to-Glia Signaling in Mouse Cortical Astrocytes
Lalo, U., Pankratov, Y. V., Kirchhoff, F., North, R. A., & Verkhratsky, A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4689-05.2006 · Cited by 355 · see citing works
Long-term synaptic plasticity in hippocampal interneurons
Kullmann, D. M., & Lamsa, K. P. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2207 · Cited by 340 · see citing works
NMDA receptor function: subunit composition versus spatial distribution
Köhr, G. (2006) · Cell and Tissue Research · doi:10.1007/s00441-006-0273-6 · Cited by 334 · see citing works
Extracellular Glutamate Concentration in Hippocampal Slice
Herman, M. A., & Jahr, C. E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3009-07.2007 · Cited by 331 · see citing works
Salomone, S., Caraci, F., Leggio, G. M., Fedotova, J., & Drago, F. (2011) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2011.04134.x · Cited by 322 · see citing works
Jacob, C. P., Koutsilieri, E., Bartl, J., Neuen-Jacob, E., Arzberger, T., Zander, N., Ravid, R., Roggendorf, W., Riederer, P., & Grünblatt, E. (2007) · Journal of Alzheimer's Disease · doi:10.3233/jad-2007-11113 · Cited by 317 · see citing works
Almeida, C. G., Takahashi, R. H., & Gouras, G. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5078-05.2006 · Cited by 316 · see citing works
Vizi, E. S. (2000) · Pharmacological Reviews · doi:10.1016/s0031-6997(24)01436-4 · Cited by 311 · see citing works
Amyloid‐Beta Interaction with Mitochondria
Pagani, L., & Eckert, A. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/925050 · Cited by 309 · see citing works
Microtubule-associated protein tau is essential for long-term depression in the hippocampus
Kimura, T., Whitcomb, D. J., Jo, J., Regan, P., Piers, T., Heo, S., Brown, C., Hashikawa, T., Murayama, M., Seok, H., et al. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0144 · Cited by 307 · see citing works
Ellison, G. D. (1995) · Brain Research Reviews · doi:10.1016/0165-0173(94)00014-g · Cited by 304 · see citing works
Lazarov, O., Lee, M., Peterson, D. A., & Sisodia, S. S. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-22-09785.2002 · Cited by 302 · see citing works
Hansen, K. B., Ogden, K. K., Yuan, H., & Traynelis, S. F. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.035 · Cited by 300 · see citing works
GRIN2A mutation and early‐onset epileptic encephalopathy: personalized therapy with memantine
Pierson, T. M., Yuan, H., Marsh, E. D., Fajardo, K. V. F., Adams, D. R., Markello, T. C., Golas, G. A., Simeonov, D. R., Holloman, C., Tankovic, A., et al. (2014) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.39 · Cited by 294 · see citing works
In vivo staging of regional amyloid deposition
Grothe, M. J., Barthel, H., Sepulcre, J., Dyrba, M., Sabri, O., Teipel, S. J., Stern, Y., & Initiative, A. D. N. (2022) · DZNE Pub · doi:10.7916/0vj1-4c02 · Cited by 294 · see citing works
Assembly with the NR1 Subunit Is Required for Surface Expression of NR3A-Containing NMDA Receptors
Pérez‐Otaño, I., Schulteis, C. T., Contractor, A., Lipton, S. A., Trimmer, J. S., Sucher, N. J., & Heinemann, S. F. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-04-01228.2001 · Cited by 287 · see citing works
Synaptic and Extrasynaptic NMDA Receptor NR2 Subunits in Cultured Hippocampal Neurons
Thomas, C. G., Miller, A., & Westbrook, G. L. (2005) · Journal of Neurophysiology · doi:10.1152/jn.00771.2005 · Cited by 286 · see citing works
Kinoshita, A., Fukumoto, H., Shah, T., Whelan, C. M., Irizarry, M. C., & Hyman, B. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00643 · Cited by 284 · see citing works
Metabotropic NMDA receptor function is required for NMDA receptor-dependent long-term depression
Nabavi, S., Kessels, H. W. H. G., Alfonso, S., Aow, J., Fox, R., & Malinow, R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219454110 · Cited by 280 · see citing works
Roselli, F., Tirard, M., Lu, J., Hutzler, P., Lamberti, P., Livrea, P., Morabito, M. A., & Almeida, O. F. X. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3034-05.2005 · Cited by 276 · see citing works
The ER stress factor XBP1s prevents amyloid-β neurotoxicity
Casas-Tinto, S., Zhang, Y., Sanchez-Garcia, J., Gomez-Velazquez, M., Rincon-Limas, D. E., & Fernandez-Funez, P. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr100 · Cited by 275 · see citing works
Mechanism of NMDA receptor channel block by MK-801 and memantine
Song, X., Jensen, M. Ø., Jogini, V., Stein, R. A., Lee, C.-H., Mchaourab, H. S., Shaw, D. E., & Gouaux, E. (2018) · Nature · doi:10.1038/s41586-018-0039-9 · Cited by 266 · see citing works
Nishi, M., Hinds, H. L., Lu, H., Kawata, M., & Hayashi, Y. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-23-j0003.2001 · Cited by 262 · see citing works
Léveillé, F., Gaamouch, F. E., Gouix, E., Lecocq, M., Lobner, D., Nicole, O., & Buisson, A. (2008) · The FASEB Journal · doi:10.1096/fj.08-107268 · Cited by 258 · see citing works
Long-term potentiation and the role of N -methyl- d -aspartate receptors
Volianskis, A., France, G., Jensen, M. S., Bortolotto, Z. A., Jane, D. E., & Collingridge, G. L. (2015) · Brain Research · doi:10.1016/j.brainres.2015.01.016 · Cited by 252 · see citing works
Distinct Roles of Synaptic and Extrasynaptic NMDA Receptors in Excitotoxicity
Sattler, R., Xiong, Z., Lu, W.-Y., MacDonald, J. F., & Tymianski, M. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-01-00022.2000 · Cited by 247 · see citing works
NMDA Di-Heteromeric Receptor Populations and Associated Proteins in Rat Hippocampus
Al‐Hallaq, R. A., Conrads, T. P., Veenstra, T. D., & Wenthold, R. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2155-07.2007 · Cited by 247 · see citing works
Rönicke, R., Mikhaylova, M., Rönicke, S., Meinhardt, J., Schröder, U. H., Fändrich, M., Reiser, G., Kreutz, M. R., & Reymann, K. G. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.01.011 · Cited by 246 · see citing works
β-Amyloid Peptide Activates α7 Nicotinic Acetylcholine Receptors Expressed in Xenopus Oocytes
Dineley, K. T., Bell, K. A., Bui, D., & Sweatt, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200066200 · Cited by 241 · see citing works
Modulation of Triheteromeric NMDA Receptors by N-Terminal Domain Ligands
Hatton, C. J., & Paoletti, P. (2005) · Neuron · doi:10.1016/j.neuron.2005.03.005 · Cited by 237 · see citing works
Amyloid beta peptides and glutamatergic synaptic dysregulation
Parameshwaran, K., Dhanasekaran, M., & Suppiramaniam, V. D. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.10.008 · Cited by 232 · see citing works
Pharmacotherapies for Alzheimer's disease: Beyond cholinesterase inhibitors
Tayeb, H. O., Yang, H. D., Price, B. H., & Tarazi, F. I. (2011) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2011.12.002 · Cited by 231 · see citing works
Kaindl, A. M., Degos, V., Peineau, S., Gouadon, E., Chhor, V., Loron, G., Charpentier, T. L., Josserand, J., Ali, C., Vivien, D., et al. (2012) · Annals of Neurology · doi:10.1002/ana.23626 · Cited by 230 · see citing works
Reynolds, C. H., Garwood, C. J., Wray, S., Price, C., Kellie, S., Perera, T. P. S., Zvelebil, M., Yang, A., Sheppard, P. W., Varndell, I. M., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709715200 · Cited by 226 · see citing works
Groc, L., Choquet, D., Stephenson, F. A., Verrier, D., Manzoni, O. J., & Chavis, P. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.1772-07.2007 · Cited by 225 · see citing works
Amyloid β peptide oligomers directly activate NMDA receptors
Texidó, L., Martı́n-Satué, M., Alberdi, E. M., Solsona, C., & Matute, C. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.02.001 · Cited by 223 · see citing works
Kurup, P. K., Zhang, Y., Xu, J., Venkitaramani, D. V., Haroutunian, V. H., Greengard, P., Nairn, A. C., & Lombroso, P. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0157-10.2010 · Cited by 222 · see citing works
Differential Sensitivity of RecombinantN-Methyl-d-Aspartate Receptor Subtypes to Zinc Inhibition
Chen, N., Moshaver, A., & Raymond, L. A. (1997) · Molecular Pharmacology · doi:10.1124/mol.51.6.1015 · Cited by 215 · see citing works
Emerging roles of GluN3-containing NMDA receptors in the CNS
Pérez-Otaño, I., Larsen, R. S., & Wesseling, J. F. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.92 · Cited by 214 · see citing works
Morris, G. P., Clark, I. A., & Vissel, B. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1918-8 · Cited by 212 · see citing works
Sanderson, J. L., Gorski, J. A., & Dell’Acqua, M. L. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.043 · Cited by 210 · see citing works
Dysfunctional synapse in Alzheimer's disease – A focus on NMDA receptors
Mota, S. I., Ferreira, I. L., & Rego, A. C. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.013 · Cited by 206 · see citing works
Extrasynaptic and synaptic NMDA receptors form stable and uniform pools in rat hippocampal slices
Harris, A. Z., & Pettit, D. L. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.137679 · Cited by 202 · see citing works
Bolo, N. R. (2000) · Neuropsychopharmacology · doi:10.1016/s0893-133x(00)00116-0 · Cited by 202 · see citing works
Zhou, X., Hollern, D. P., Liao, J., Andrechek, E. R., & Wang, H. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.82 · Cited by 200 · see citing works
Expression and role of ionotropic glutamate receptors in pancreatic islet cells
Inagaki, N., Kuromi, H., Gonoi, T., Okamoto, Y., Ishida, H., Seino, Y., Kaneko, T., Iwanaga, T., & Seino, S. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.8.7768362 · Cited by 199 · see citing works
NMDA Receptor Activation Inhibits α-Secretase and Promotes Neuronal Amyloid-β Production
Lesné, S., Ali, C., Gabriel, C., Croci, N., MacKenzie, E. T., Glabe, C. G., Plotkine, M., Marchand‐Leroux, C., Vivien, D., & Buisson, A. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0849-05.2005 · Cited by 198 · see citing works
Mechanisms underlying NMDA receptor synaptic/extrasynaptic distribution and function
Gladding, C. M., & Raymond, L. A. (2011) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2011.05.001 · Cited by 197 · see citing works
Metabotropic NMDA receptor function is required for β-amyloid–induced synaptic depression
Kessels, H. W. H. G., Nabavi, S., & Malinow, R. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1219605110 · Cited by 196 · see citing works
Astrocyte NMDA receptors' activity sustains neuronal survival through a Cdk5–Nrf2 pathway
Jimenez-Blasco, D., Santofimia-Castaño, P., Gonzalez, A., Almeida, A., & Bolaños, J. P. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.49 · Cited by 196 · see citing works
Bordji, K., Becerril-Ortega, J., Nicole, O., & Buisson, A. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3021-10.2010 · Cited by 195 · see citing works
Ferreira, I. L., Bajouco, M., Mota, S. I., Auberson, Y. P., Oliveira, C. R., & Rego, A. C. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.11.008 · Cited by 185 · see citing works
Corlew, R., Wang, Y., Ghermazien, H., Erişir, A., & Philpot, B. D. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5494-06.2007 · Cited by 184 · see citing works
Kim, J., Anwyl, R., Suh, Y., Djamgoz, M. B. A., & Rowan, M. J. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-04-01327.2001 · Cited by 182 · see citing works
Characterisation of the Expression of NMDA Receptors in Human Astrocytes
Lee, M.-C., Ting, K.-K., Adams, S., Brew, B., Chung, R., & Guillemin, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014123 · Cited by 182 · see citing works
Combination Therapy in Alzheimer???s Disease: A Review of Current Evidence
Schmitt, B., Bernhardt, T., Moeller, H.-J., Heuser, I., & Fr??lich, L. (2004) · CNS Drugs · doi:10.2165/00023210-200418130-00001 · Cited by 182 · see citing works
Chenard, B. L., Bordner, J., Butler, T. W., Chambers, L. K., Collins, M. A., Costa, D. L. D., Ducat, M. F., Dumont, M. L., & Fox, C. B. (1995) · Journal of Medicinal Chemistry · doi:10.1021/jm00016a017 · Cited by 180 · see citing works
Hoey, S. E., Williams, R. J., & Perkinton, M. S. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.6017-08.2009 · Cited by 178 · see citing works
Multiple Defects in Energy Metabolism in Alzheimers Disease
Ferreira, I. L., Resende, R., Ferreiro, E. B., Rego, A. C., & Pereira, C. (2010) · Current Drug Targets · doi:10.2174/1389450111007011193 · Cited by 177 · see citing works
Wu, H.-M., Tzeng, N., Li, Q., Wei, S., Hu, X., Chen, S., Rawls, S. M., Flood, P. M., Hong, J., & Lu, R. (2009) · Neuropsychopharmacology · doi:10.1038/npp.2009.64 · Cited by 174 · see citing works
Hippocampal Long-Term Synaptic Plasticity and Signal Amplification of NMDA Receptors
MacDonald, J. F., Jackson, M., & Beazely, M. A. (2006) · Critical Reviews in Neurobiology · doi:10.1615/critrevneurobiol.v18.i1-2.80 · Cited by 174 · see citing works
Fox, C., Crugel, M., Maidment, I., Auestad, B. H., Coulton, S., Treloar, A., Ballard, C., Boustani, M., Katona, C., & Livingston, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035185 · Cited by 173 · see citing works
Physiological Roles of Non-Neuronal NMDA Receptors
Hogan-Cann, A. D., & Anderson, C. M. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.05.012 · Cited by 171 · see citing works
Influence of the NR3A subunit on NMDA receptor functions
Henson, M. A., Roberts, A. C., Pérez‐Otaño, I., & Philpot, B. D. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.01.004 · Cited by 170 · see citing works
Allosteric modulators of NMDA receptors: multiple sites and mechanisms
Zhu, S., & Paoletti, P. (2014) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2014.10.009 · Cited by 167 · see citing works
Andras, I. E., Deli, M. A., Veszelka, S., Hayashi, K., Hennig, B., & Toborek, M. J. (2007) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600445 · Cited by 167 · see citing works
Ting, K. K., Brew, B. J., & Guillemin, G. J. (2009) · Journal of Neuroinflammation · doi:10.1186/1742-2094-6-36 · Cited by 166 · see citing works
NR3A-containing NMDARs promote neurotransmitter release and spike timing–dependent plasticity
Larsen, R. S., Corlew, R., Henson, M. A., Roberts, A. C., Mishina, M., Watanabe, M., Lipton, S. A., Nakanishi, N., Pérez‐Otaño, I., Weinberg, R. J., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2750 · Cited by 165 · see citing works
Downregulation of NR3A-Containing NMDARs Is Required for Synapse Maturation and Memory Consolidation
Roberts, A. C., Díez‐García, J., Rodriguiz, R. M., López, I. P., Luján, R., Martínez-Turrillas, R., Picó, E., Henson, M. A., Bernardo, D., Jarrett, T. M., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.06.016 · Cited by 163 · see citing works
Synapse-Specific Expression of Functional Presynaptic NMDA Receptors in Rat Somatosensory Cortex
Brasier, D. J., & Feldman, D. E. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3915-07.2008 · Cited by 162 · see citing works
Wang, C., Pralong, W. F., Schulz, M. F., Rougon, G. N., Aubry, J., Pagliusi, S. R., Robert, A., & Kiss, J. Z. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.6.1565 · Cited by 162 · see citing works
Liu, S., Zhang, N., Guo, Y., Zhao, R., Shi, T., Feng, S., Wang, S.-Q., Yang, Q., Li, X., Wu, Y., et al. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.5828-11.2012 · Cited by 161 · see citing works
Self-citationCharacterization of pancreatic NMDA receptors as possible drug targets for diabetes treatment
Marquard, J., Otter, S., Welters, A., Stirban, A., Fischer, A., Eglinger, J., Herebian, D., Kletke, O., Klemen, M. S., Stožer, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3822 · Cited by 161 · see citing works
Momiyama, A., Feldmeyer, D., & Cull-Candy, S. G. (1996) · The Journal of Physiology · doi:10.1113/jphysiol.1996.sp021507 · Cited by 160 · see citing works
Proton-gated Ca2+-permeable TRP channels damage myelin in conditions mimicking ischaemia
Hamilton, N. B., Kołodziejczyk, K., Kougioumtzidou, E., & Attwell, D. (2016) · Nature · doi:10.1038/nature16519 · Cited by 159 · see citing works
Relationship between Availability of NMDA Receptor Subunits and Their Expression at the Synapse
Prybylowski, K., Fu, Z., Losi, G., Hawkins, L. M., Luo, J.-H., Chang, K., Wenthold, R., & Vicini, S. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-20-08902.2002 · Cited by 156 · see citing works
Mishizen-Eberz, A. J., Rissman, R. A., Carter, T. L., Ikonomovic, M. D., Wolfe, B. B., & Armstrong, D. M. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.09.016 · Cited by 156 · see citing works
The diagnostic value of FDG and amyloid PET in Alzheimer’s disease—A systematic review
Rice, L., & Bisdas, S. (2017) · European Journal of Radiology · doi:10.1016/j.ejrad.2017.07.014 · Cited by 150 · see citing works
Martel, M., Wyllie, D. J. A., & Hardingham, G. E. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.080 · Cited by 149 · see citing works
Zhou, X., Ding, Q., Chen, Z., Yun, H., & Wang, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.482000 · Cited by 148 · see citing works
Sze, C., Bi, H., Kleinschmidt-DeMasters, B. K., Filley, C. M., & Martin, L. J. (2001) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(00)00467-6 · Cited by 146 · see citing works
Paradoxical Upregulation of Glutamatergic Presynaptic Boutons during Mild Cognitive Impairment
Bell, K. F. S., Bennett, D. A., & Cuello, A. C. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3269-07.2007 · Cited by 145 · see citing works
Unconventional NMDA Receptor Signaling
Doré, K., Stein, I. S., Brock, J. A., Castillo, P. E., Zito, K., & Sjöström, P. J. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1825-17.2017 · Cited by 145 · see citing works
Non-Ionotropic NMDA Receptor Signaling Drives Activity-Induced Dendritic Spine Shrinkage
Stein, I. S., Gray, J. A., & Zito, K. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.4289-14.2015 · Cited by 143 · see citing works
Invulnerability of retinal ganglion cells to NMDA excitotoxicity
Ullian, E. M., Barkis, W. B., Chen, S., Diamond, J. S., & Barres, B. A. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.05.002 · Cited by 143 · see citing works
Park, H., Popescu, A., & Poo, M.-M. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.045 · Cited by 142 · see citing works
GluN3 subunit-containing NMDA receptors: not just one-trick ponies
Pachernegg, S., Strutz‐Seebohm, N., & Hollmann, M. (2012) · Trends in Neurosciences · doi:10.1016/j.tins.2011.11.010 · Cited by 141 · see citing works
Li, C., Xiao, L., Liu, X., Yang, W., Shen, W., Hu, C., Yang, G., & He, C. (2013) · Glia · doi:10.1002/glia.22469 · Cited by 139 · see citing works
Matsuda, K., Fletcher, M., Kamiya, Y., & Yuzaki, M. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-31-10064.2003 · Cited by 138 · see citing works
Regulation of NMDA receptor Ca2+ signalling and synaptic plasticity
Lau, C. G., Takeuchi, K., Rodenas-Ruano, A., Takayasu, Y., Murphy, J., Bennett, M. V. L., & Zukin, R. S. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371369 · Cited by 138 · see citing works
Neuropathologic changes in Alzheimer's disease: potential targets for treatment.
Wenk, G. L. (2006) · PubMed · Cited by 134 · see citing works
Amyloid-β Induces Caspase-Dependent Loss of PSD-95 and Synaptophysin Through NMDA Receptors
Liu, J., Chang, L., Roselli, F., Almeida, O. F. X., Gao, X., Wang, X., Yew, D. T. W., & Wu, Y. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100948 · Cited by 133 · see citing works
Self-citationLRP in Amyloid‐β Production and Metabolism
Bu, G., Cam, J. A., & Zerbinatti, C. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.005 · Cited by 133 · see citing works
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Sorted by citations
Comprehensive Review on Alzheimer’s Disease: Causes and Treatment
Breijyeh, Z., & Karaman, R. (2020) · Molecules · doi:10.3390/molecules25245789 · Cited by 2,789 · see citing works
Alzheimer’s disease: Targeting the glutamatergic system
Conway, M. E. (2020) · Biogerontology · doi:10.1007/s10522-020-09860-4 · Cited by 180 · see citing works
New therapeutics beyond amyloid-β and tau for the treatment of Alzheimer’s disease
Zhang, F., Zhong, R.-J., Cheng, C., Li, S., & Le, W.-D. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-00565-5 · Cited by 105 · see citing works
Alzheimer’s disease as type 3 diabetes: understanding the link and implications
Kciuk, M., Kruczkowska, W., Gałęziewska, J., Wanke, K., Kałuzińska-Kołat, Ż., Aleksandrowicz, M., & Kontek, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252211955 · Cited by 98 · see citing works
Drug Delivery Systems as a Strategy to Improve the Efficacy of FDA-Approved Alzheimer’s Drugs
Nunes, D., Loureiro, J. A., & Pereira, M. C. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14112296 · Cited by 68 · see citing works
Mitochondria and Cellular Redox State on the Route from Ageing to Alzheimer's Disease
Abate, G., Vezzoli, M., Sandri, M., Rungratanawanich, W., Memo, M., & Uberti, D. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111385 · Cited by 41 · see citing works
Dulewicz, M., Kulczyńska-Przybik, A., Słowik, A., Borawska, R., & Mroczko, B. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10194575 · Cited by 22 · see citing works
Role of Ion Channels in Alzheimer’s Disease Pathophysiology
Bhoi, R., Mitra, T., Tejaswi, K., Manoj, V., & Ghatak, S. (2025) · The Journal of Membrane Biology · doi:10.1007/s00232-025-00341-8 · Cited by 19 · see citing works
Synaptic Organizers in Alzheimer’s Disease: A Classification Based on Amyloid-β Sensitivity
Lee, A. K., Khaled, H., Chofflet, N., & Takahashi, H. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00281 · Cited by 14 · see citing works
Auvelity as a Potential Treatment for Alzheimer’s Disease
Lepkowsky, C. M. (2022) · Medical Research Archives · doi:10.18103/mra.v10i10.3206 · Cited by 2 · see citing works
- Authors
- Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y.
- Affiliations
- Tsinghua University (CN)
- Capital Medical University (CN)
- Corresponding author
- Wu, Yan
- Venue
- Frontiers in Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2019-02-08
- Volume
- 13
- Pages
- 43-43
- ISSN
- 1662-453X (ISSN-L)
- PMC
- PMC6375899
- OpenAlex
- W2911747652
- Cited by
- 535
- References
- 339
- Citations by year
- 2026: 51 · 2025: 80 · 2024: 82 · 2023: 103 · 2022: 92 · 2021: 71 · 2020: 47 · 2019: 9
- FWCI
- 6.45
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- NMDA receptor, Alzheimer's disease, amyloid-beta oligomers, synaptic dysfunction, synaptic depression, memantine, NMDA receptor subunits
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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