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Metabotropic Glutamate Receptor 5 Is a Coreceptor for Alzheimer Aβ Oligomer Bound to Cellular Prion Protein
Open accessAbstract
Soluble amyloid-β oligomers (Aβo) trigger Alzheimer's disease (AD) pathophysiology and bind with high affinity to cellular prion protein (PrP(C)). At the postsynaptic density (PSD), extracellular Aβo bound to lipid-anchored PrP(C) activates intracellular Fyn kinase to disrupt synapses. Here, we screened transmembrane PSD proteins heterologously for the ability to couple Aβo-PrP(C) with Fyn. Only coexpression of the metabotropic glutamate receptor, mGluR5, allowed PrP(C)-bound Aβo to activate Fyn. PrP(C) and mGluR5 interact physically, and cytoplasmic Fyn forms a complex with mGluR5. Aβo-PrP(C) generates mGluR5-mediated increases of intracellular calcium in Xenopus oocytes and in neurons, and the latter is also driven by human AD brain extracts. In addition, signaling by Aβo-PrP(C)-mGluR5 complexes mediates eEF2 phosphorylation and dendritic spine loss. For mice expressing familial AD transgenes, mGluR5 antagonism reverses deficits in learning, memory, and synapse density. Thus, Aβo-PrP(C) complexes at the neuronal surface activate mGluR5 to disrupt neuronal function.
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“Aβ oligomers can drive additional vicious cycles by stimulating metabotropic glutamate receptor 5 (mGluR5)146,147, which activates feedforward Ca2+–cAMP signaling and drive tau phosphorylation (Fig. 5, brown).”
From Stress weakens prefrontal networks: molecular insults to higher cognition (2015) · cites this paper as [147]
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“Amyloid-β oligomer binding results in aberrant neuronal signaling and the endocytosis of the dysfunctional synapse into the cell [126,127].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [126]
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“Among the Aβ binding candidates, cellular prion protein (PrPc) represents the most studied, either alone or through a complex with mGluR5 [37, 62, 72, 79].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [72]
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“The most studied binding partner is the PrPc, which through a cascade involving a complex with mGluR5 may lead to toxicity independently or via tau [37, 62, 72, 79].”
From Transmembrane protein 97 is a potential synaptic amyloid beta receptor in human Alzheimer’s disease (2024) · cites this paper as [72]
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“Amyloid-β oligomers bind to a protein complex comprised of cellular prion protein (PrPc) along with other proteins including leukocyte immunoglobulin-like receptor subfamily B2/paired immunoglobulin-like type 2 receptor B (LilrB2), and possibly also Nogo-66 receptor 1 (Nogo-1), low-affinity nerve growth factor (NGF) receptor [125] (Figure 3), and the metabotropic glutamate receptor 5 [126].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [126]
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1 retracted
Larson, M. E., Sherman, M. A., Amar, F., Nuvolone, M., Schneider, J. A., Bennett, D. A., Aguzzi, A., & Lesné, S. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.1858-12.2012 · Cited by 290
RetractedTriple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
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
A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738
Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
Self-citationAlzheimer’s Disease: The Challenge of the Second Century
Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424
Impaired Long-Term Potentiation, Spatial Learning, and Hippocampal Development in fyn Mutant Mice
Grant, S. G. N., O’Dell, T. J., Karl, K. A., Stein, P. L., Soriano, P. M., & Kandel, E. R. (1992) · Science · doi:10.1126/science.1361685 · Cited by 1,160
Proximal events in Wnt signal transduction
Angers, S., & Moon, R. T. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2717 · Cited by 1,135
Luján, R., Nusser, Z., Roberts, J. D. B., Shigemoto, R., & Somogyi, P. (1996) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1996.tb01611.x · Cited by 874
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 682
Self-citationRoberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4152-10.2011 · Cited by 654
Lu, Y.-M., Jia, Z., Janus, C., Henderson, J. T., Gerlai, R., Wojtowicz, J. M., & Roder, J. C. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-13-05196.1997 · Cited by 634
Lüscher, C., & Huber, K. M. (2010) · Neuron · doi:10.1016/j.neuron.2010.01.016 · Cited by 627
Park, S., Park, J. M., Kim, S., Kim, J.-A., Shepherd, J. D., Smith-Hicks, C. L., Chowdhury, S., Kaufmann, W., Kuhl, D., Ryazanov, A. G., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.05.023 · Cited by 516
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. (2002) · Science · doi:10.1126/science.1065983 · Cited by 497
Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5
Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., & Triller, A. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.029 · Cited by 468
Collins, M. O., Husi, H., Yu, L., Brandon, J. M., Anderson, C. N. G., Blackstock, W. P., Choudhary, J. S., & Grant, S. G. N. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03507.x · Cited by 448
Wang, Q., Walsh, D. M., Rowan, M. J., Selkoe, D. J., & Anwyl, R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1633-03.2004 · Cited by 437
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 435
The Hedgehog Signal Transduction Network
Robbins, D. J., Fei, D. L., & Galdo, N. A. R. (2012) · Science Signaling · doi:10.1126/scisignal.2002906 · Cited by 433
Reversing EphB2 depletion rescues cognitive functions in Alzheimer model
Cissé, M., Halabisky, B., Harris, J., Devidze, N., Dubal, D. B., Sun, B., Orr, A., Lotz, G., Kim, D. H., Hamto, P., et al. (2011) · Nature · doi:10.1038/nature09635 · Cited by 433
Memory Impairment in Transgenic Alzheimer Mice Requires Cellular Prion Protein
Gimbel, D. A., Nygaard, H. B., Coffey, E. E., Gunther, E. C., Laurén, J., Gimbel, Z. A., & Strittmatter, S. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.0395-10.2010 · Cited by 418
Self-citationPrybylowski, K., Chang, K., Sans, N., Kan, L., Vicini, S., & Wenthold, R. J. (2005) · Neuron · doi:10.1016/j.neuron.2005.08.016 · Cited by 405
Linhoff, M. W., Laurén, J., Cassidy, R. M., Dobie, F. A., Takahashi, H., Nygaard, H. B., Airaksinen, M. S., Strittmatter, S. M., & Craig, A. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.017 · Cited by 370
Self-citationLi, X., Alafuzoff, I., Soininen, H., Winblad, B., & Pei, J. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04833.x · Cited by 324
An, W.-L., Cowburn, R. F., Li, L., Braak, H., Alafuzoff, I., Iqbal, K., Iqbal, I.-G., Winblad, B., & Pei, J.-J. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63687-5 · Cited by 312
Interaction between Human Prion Protein and Amyloid-β (Aβ) Oligomers
Chen, S., Yadav, S. P., & Surewicz, W. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145516 · Cited by 301
Freir, D. B., Nicoll, A. J., Klyubin, I. V., Panico, S., Donald, J. M. M., Risse, E., Asante, E. A., Farrow, M. A., Sessions, R. B., Saibil, H. R., et al. (2011) · Nature Communications · doi:10.1038/ncomms1341 · Cited by 300
Homeostatic Scaling Requires Group I mGluR Activation Mediated by Homer1a
Hu, J.-H., Park, J. M., Park, S. J., Xiao, B., Dehoff, M. H., Kim, S., Hayashi, T., Schwarz, M. K., Huganir, R. L., Seeburg, P. H., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.008 · Cited by 263
Disrupted Homer scaffolds mediate abnormal mGluR5 function in a mouse model of fragile X syndrome
Ronesi, J. A., Collins, K. A., Hays, S. A., Tsai, N.-P., Guo, W., Birnbaum, S. G., Hu, J.-H., Worley, P. F., Gibson, J. R., & Huber, K. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3033 · Cited by 251
Hay, D. L., Poyner, D. R., & Sexton, P. M. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2005.06.015 · Cited by 239
Jankowsky, J. L., Xu, G. M., Fromholt, D., Gonzales, V., & Borchelt, D. (2003) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/62.12.1220 · Cited by 238
Barry, A. E., Klyubin, I., Mc Donald, J. M., Mably, A. J., Farrell, M. A., Scott, M., Walsh, D. M., & Rowan, M. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.6500-10.2011 · Cited by 237
mGluR5 Has a Critical Role in Inhibitory Learning
Xu, J., Zhu, Y., Contractor, A., & Heinemann, S. F. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5716-08.2009 · Cited by 228
Heidinger, V., Manzerra, P., Wang, X. Q., Strasser, U., Yu, S. P., Choi, D. W., & Behrens, M. M. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-13-05452.2002 · Cited by 223
Regulation of Embryonic Cell Adhesion by the Prion Protein
Trillo, E. M., Solis, G. P., Schrock, Y., Corinna, G., Luncz, L., Thomanetz, V., & Stuermer, C. A. O. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000055 · Cited by 223
Arc/Arg3.1 Regulates an Endosomal Pathway Essential for Activity-Dependent β-Amyloid Generation
Wu, J., Petralia, R. S., Kurushima, H., Patel, H., Jung, M., Volk, L. J., Chowdhury, S., Shepherd, J. D., Dehoff, M. H., Li, Y., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.036 · Cited by 221
Evolutionary expansion and anatomical specialization of synapse proteome complexity
Emes, R. D., Pocklington, A., Anderson, C. N. G., Bayés, À., Collins, M., Vickers, C., Croning, M., Malik, B., Choudhary, J., Armstrong, J., et al. (2008) · Nature Neuroscience · doi:10.1038/nn.2135 · Cited by 202
Vanderklish, P. W., & Edelman, G. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032681099 · Cited by 200
The in Vivo Brain Interactome of the Amyloid Precursor Protein
Bai, Y., Markham, K. A., Chen, F., Weerasekera, R., Watts, J. C., Horne, P., Wakutani, Y., Bagshaw, R., Mathews, P. M., Fraser, P. E., et al. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700077-mcp200 · Cited by 172
Moult, P. R., Gladding, C. M., Sanderson, T. M., Fitzjohn, S. M., Bashir, Z. I., Molnar, E., & Collingridge, G. L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4322-05.2006 · Cited by 172
Rammes, G., Hasenjäger, A., Sroka-Saidi, K., Deussing, J. M., & Parsons, C. G. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.01.051 · Cited by 163
Schmitt‐Ulms, G., Hansen, K. C., Liu, J., Cowdrey, C., Yang, J., DeArmond, S. J., Cohen, F. E., Prusiner, S. B., & Baldwin, M. A. (2004) · Nature Biotechnology · doi:10.1038/nbt969 · Cited by 162
Chung, E., Ji, Y., Sun, Y., Kascsak, R. J., Kascsak, R. B., Mehta, P. D., Strittmatter, S. M., & Wisniewski, T. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-130 · Cited by 152
Self-citationAutism, Alzheimer disease, and fragile X
Sokol, D. K., Maloney, B., Long, J. M., Ray, B., & Lahiri, D. K. (2011) · Neurology · doi:10.1212/wnl.0b013e3182166dc7 · Cited by 141 · cited 1×
“Shared pathways between AD and Fragile X have been reported (Sokol et al., 2011).”
NMDA receptor–independent long-term depression correlates with successful aging in rats
Lee, H., Min, S. S., Gallagher, M., & Kirkwood, A. (2005) · Nature Neuroscience · doi:10.1038/nn1586 · Cited by 126
Heraldo, F. H., Arantes, C., Santos, T. G., Machado, C. F., Roffé, M., Haji, G. N., Lee, K. S., Magalhães, A. C., Caetano, F. A., Mancini, G. L., et al. (2010) · The FASEB Journal · doi:10.1096/fj.10-161653 · Cited by 123
Saugstad, J. A., Segerson, T. P., & Westbrook, G. L. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-19-05979.1996 · Cited by 115
Amyloid-β induced signaling by cellular prion protein and Fyn kinase in Alzheimer disease
Um, J. W., & Strittmatter, S. M. (2013) · Prion · doi:10.4161/pri.22212 · Cited by 115
Self-citationAlbasanz, J. L., Dalfó, E., Ferrer, I., & Martı́n, M. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.05.001 · Cited by 111
Ménard, C., & Quirion, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028666 · Cited by 98
Majercak, J. M., Ray, W. J., Espeseth, A. S., Simon, A. J., Shi, X., Wolffe, C., Getty, K. L., Marine, S., Stec, E. M., Ferrer, M., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605461103 · Cited by 97
Nicolle, M. M., Colombo, P. J., Gallagher, M., & McKinney, M. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-21-09604.1999 · Cited by 87
Amyloid-β42 Interacts Mainly with Insoluble Prion Protein in the Alzheimer Brain
Zou, W., Xiao, X., Yuan, J., Puoti, G., Fujioka, H., Wang, X., Richardson, S. L., Zhou, X., Zou, R. S., Li, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199356 · Cited by 81
Breit, A., Büch, T., Boekhoff, I., Solinski, H. J., Damm, E., & Gudermann, T. W. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.07.007 · Cited by 80
GAP-43 augments G protein-coupled receptor transduction in Xenopus laevis oocytes.
Strittmatter, S. M., Cannon, S. C., Ross, E. M., Higashijima, T., & Fishman, M. C. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5327 · Cited by 75
Self-citationDravid, S. M., & Murray, T. F. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.059 · Cited by 70
Metabotropic glutamate receptor subtype 5 antagonism in learning and memory
Simonyi, Á., Schachtman, T. R., & Christoffersen, G. R. J. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.12.039 · Cited by 66
A δ-Catenin Signaling Pathway Leading to Dendritic Protrusions
Abu-Elneel, K., Ochiishi, T., Medina, M., Remedi, M. V., Gastaldi, L., Cáceres, A., & Kosik, K. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804688200 · Cited by 59
Choi, K. Y., Chung, S., & Roche, K. W. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6253-10.2011 · Cited by 51
Pyk2 uncouples metabotropic glutamate receptor G protein signaling but facilitates ERK1/2 activation
Nicodemo, A. A., Pampillo, M., Ferreira, L. T., Dale, L. B., Cregan, T., Ribeiro, F. M., & Ferguson, S. S. G. (2010) · Molecular Brain · doi:10.1186/1756-6606-3-4 · Cited by 48
Bizat, N., Peyrin, J., Haı̈k, S., Cochois, V., Beaudry, P., Laplanche, J., & Néri, C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5831-09.2010 · Cited by 46
Persistent Synapse Loss Induced by Repetitive LTD in Developing Rat Hippocampal Neurons
Shinoda, Y., Tanaka, T., Tominaga‐Yoshino, K., & Ogura, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010390 · Cited by 45
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Sevigny, J., Chiao, P., Bussière, T., Weinreb, P. H., Williams, L., Maier, M., Dunstan, R., Salloway, S., Chen, T., Ling, Y., et al. (2016) · Nature · doi:10.1038/nature19323 · Cited by 3,059
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Metadata
- Authors
- 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., Gunther, E. C., Nygaard, H. B., & Strittmatter, S. M.
- Affiliations
- Yale University (US)
- Corresponding author
- Strittmatter, Stephen M.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 79
- Issue
- 5
- Pages
- 887-902
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3768018
- OpenAlex
- W2061342941
- Cited by
- 572
- References
- 65
- Citations by year
- 2026: 28 · 2025: 31 · 2024: 29 · 2023: 35 · 2022: 38 · 2021: 32 · 2020: 59 · 2019: 45 · 2018: 46 · 2017: 63 · 2016: 59 · 2015: 58 · 2014: 45 · 2013: 4
- FWCI
- 34.36
- Type
- journal article
- Language
- en
- Update notices
- erratum (2013-10-16)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- YUHSpace (Yonsei University Medical Library) (submittedVersion, cc-by-nc-nd)
- Funders
- National Institute on Aging (P30AG008051, R01AG034924)
- National Institute of General Medical Sciences (T32GM007223, T32GM007205)
- National Institute of Neurological Disorders and Stroke (R01NS074319, R01NS073502, R01NS080388)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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
- metabotropic glutamate receptor 5, amyloid-beta oligomers, cellular prion protein, Alzheimer's disease, Fyn, postsynaptic density, intracellular calcium signaling, eEF2 phosphorylation, dendritic spine loss, learning and memory impairment, synaptic loss
- MeSH terms
- Alzheimer Disease, Animals, Calcium, Cells, Cultured, Humans, Neurons, Oocytes, Phosphorylation, Xenopus, Signal Transduction, Amyloid beta-Peptides, Receptors, Metabotropic Glutamate, PrPC Proteins, Proto-Oncogene Proteins c-fyn, Mice, Elongation Factor 2 Kinase, HEK293 Cells, Post-Synaptic Density, Receptor, Metabotropic Glutamate 5
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