Metabotropic Glutamate Receptor 5 Is a Coreceptor for Alzheimer Aβ Oligomer Bound to Cellular Prion Protein

Triple-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

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

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

Alzheimer’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

Perisynaptic Location of Metabotropic Glutamate Receptors mGluR1 and mGluR5 on Dendrites and Dendritic Spines in the Rat Hippocampus

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

Aberrant protein S-nitrosylation contributes to hyperexcitability-induced synaptic damage in Alzheimer’s disease: Mechanistic insights and potential therapies

Ghatak, S., Nakamura, T., & Lipton, S. A. (2023) · Frontiers in Neural Circuits · doi:10.3389/fncir.2023.1099467 · Cited by 26

NMDA receptors in neurodegenerative diseases: mechanisms and emerging therapeutic strategies

Zhang, K., Wen, M., Nan, X., Zhao, S., Li, H., Ai, Y., & Zhu, H. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1604378 · Cited by 29

Prelysosomal Compartments in the Unconventional Secretion of Amyloidogenic Seeds

Madsen, H. B., & Vilhardt, F. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010227 · Cited by 26

Biased agonism and allosteric modulation of metabotropic glutamate receptor 5

Trinh, P. N. H., May, L. T., Leach, K., & Gregory, K. J. (2018) · Clinical Science · doi:10.1042/cs20180374 · Cited by 28

MRZ-99030 – A novel modulator of Aβ aggregation: II – Reversal of Aβ oligomer-induced deficits in long-term potentiation (LTP) and cognitive performance in rats and mice

Rammes, G., Gravius, A., Ruitenberg, M., Wegener, N., Chambon, C., Sroka, K., Jeggo, R., Staniaszek, L. E., Spanswick, D. C., O‘Hare, E., et al. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.12.037 · Cited by 51

Copper binding and protein aggregation: a journey from the brain to the human lens

Posadas, Y., Sánchez‐López, C., & Quintanar, L. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00145h · Cited by 25

Inhibition of the Motor Protein Eg5/Kinesin-5 in Amyloid β-Mediated Impairment of Hippocampal Long-Term Potentiation and Dendritic Spine Loss

Freund, R. K., Gibson, E. S., Potter, H., & Dell’Acqua, M. L. (2016) · Molecular Pharmacology · doi:10.1124/mol.115.103085 · Cited by 24

Liver X receptor agonist treatment significantly affects phenotype and transcriptome of APOE3 and APOE4 Abca1 haplo-deficient mice

Carter, A. Y., Letronne, F., Fitz, N. F., Mounier, A., Wolfe, C. M., Nam, K. N., Reeves, V. L., Kamboh, H., Lefterov, I., & Koldamova, R. (2017) · PLOS ONE · doi:10.1371/journal.pone.0172161 · Cited by 28

Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance

Loh, D., & Reiter, R. J. (2022) · Molecules · doi:10.3390/molecules27030705 · Cited by 25

Updates on the Physiopathology of Group I Metabotropic Glutamate Receptors (mGluRI)-Dependent Long-Term Depression

Mango, D., & Ledonne, A. (2023) · Cells · doi:10.3390/cells12121588 · Cited by 25

Metabotropic glutamate receptor 5 as a potential therapeutic target in Huntington’s disease

Ribeiro, F. M., Hamilton, A., Doria, J. G., Guimaraes, I. M., Cregan, S. P., & Ferguson, S. S. G. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.948419 · Cited by 26

Single molecule experiments emphasize GM1 as a key player of the different cytotoxicity of structurally distinct Aβ1–42 oligomers

Calamai, M., Evangelisti, E., Cascella, R., Parenti, N., Cecchi, C., Stefani, M., & Pavone, F. S. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.12.009 · Cited by 27

Alzheimer's Toxic Amyloid Beta Oligomers: Unwelcome Visitors to the Na/K ATPase alpha3 Docking Station.

DiChiara, T., DiNunno, N., Clark, J. R., Bu, R. L., Cline, E. N., Rollins, M. G., Gong, Y., Brody, D. L., Sligar, S. G., Velasco, P. T., et al. (2017) · PubMed · Cited by 25

Prion gene paralogs are dispensable for early zebrafish development and have nonadditive roles in seizure susceptibility

Leighton, P. L. A., Kanyo, R., Neil, G. J., Pollock, N. M., & Allison, W. T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001171 · Cited by 25

Melatonin in Synaptic Impairments of Alzheimer’s Disease

Shi, Y., Fang, Y., Wei, Y., Jiang, Q., Zeng, P. H., Tang, N., Lu, Y., & Tian, Q. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171178 · Cited by 24

Analysis of RNA Expression Profiles Identifies Dysregulated Vesicle Trafficking Pathways in Creutzfeldt-Jakob Disease

Bartoletti‐Stella, A., Corrado, P., Mometto, N., Baiardi, S., Durrenberger, P. F., Arzberger, T., Reynolds, R., Kretzschmar, H. A., Capellari, S., & Parchi, P. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1421-1 · Cited by 24

Amyloid-β in Alzheimer’s disease – front and centre after all?

Weglinski, C., & Jeans, A. F. (2022) · Neuronal Signaling · doi:10.1042/ns20220086 · Cited by 24

APP Causes Hyperexcitability in Fragile X Mice

Westmark, C. J., Chuang, S.-C., Hays, S. A., Filon, M. J., Ray, B. C., Westmark, P. R., Gibson, J. R., Huber, K. M., & Wong, R. K. S. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00147 · Cited by 24

Senegenin Inhibits Aβ1-42-Induced PC12 Cells Apoptosis and Oxidative Stress via Activation of the PI3K/Akt Signaling Pathway

Ren, X., Zhang, J., Zhao, Y., & Sun, L. (2022) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s346238 · Cited by 22

Fragile X mental retardation protein expression in Alzheimer’s disease

Renoux, A. J., Carducci, N. M., Ahmady, A. A., & Todd, P. K. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00360 · Cited by 23

Fragile X mental retardation protein: from autism to neurodegenerative disease

Wang, H. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00043 · Cited by 26

Relationship Between β-Amyloid and Mitochondrial Dynamics

Kim, D. I., Lee, K. H., Oh, J. Y., Kim, J. S., & Han, H. J. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0434-4 · Cited by 23

The dual role of c‐src in cell‐to‐cell transmission of α‐synuclein

Choi, Y. R., Kim, J., Kang, S., Noh, H. R., Jou, I., Joe, E.-H., & Park, S. M. (2020) · EMBO Reports · doi:10.15252/embr.201948950 · Cited by 28

Store depletion-induced h-channel plasticity rescues a channelopathy linked to Alzheimer’s disease

Musial, T. F., Molina-Campos, E., Bean, L. A., Ybarra, N., Borenstein, R., Russo, M. L., Buss, E. W., Justus, D., Neuman, K. M., Ayala, G. D., et al. (2018) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2018.06.004 · Cited by 24

Sensing α‐Synuclein From the Outside via the Prion Protein: Implications for Neurodegeneration

Brás, I. C., Lopes, L. V., & Outeiro, T. F. (2018) · Movement Disorders · doi:10.1002/mds.27478 · Cited by 24

Prion protein and prion disease at a glance

Zhu, C., & Aguzzi, A. (2021) · Journal of Cell Science · doi:10.1242/jcs.245605 · Cited by 27

Role of mGlu5 in Persistent Forms of Hippocampal Synaptic Plasticity and the Encoding of Spatial Experience

Hagena, H., & Manahan‐Vaughan, D. (2022) · Cells · doi:10.3390/cells11213352 · Cited by 24

Anti-amyloid Antibody Therapies for Alzheimer’s Disease

Park, K. W. (2024) · Nuclear Medicine and Molecular Imaging · doi:10.1007/s13139-024-00848-3 · Cited by 25

Loss of tau and Fyn reduces compensatory effects of MAP2 for tau and reveals a Fyn‐independent effect of tau on calcium

Liu, G., Thangavel, R., Rysted, J., Kim, Y., Francis, M. B., Adams, E., Lin, Z., Taugher, R. J., Wemmie, J. A., Usachev, Y. M., et al. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24517 · Cited by 22

Membrane Binding Strongly Affecting the Dopamine Reactivity Induced by Copper Prion and Copper/Amyloid-β (Aβ) Peptides. A Ternary Copper/Aβ/Prion Peptide Complex Stabilized and Solubilized in Sodium Dodecyl Sulfate Micelles

Bacchella, C., Nicolis, S., Dell’Acqua, S., Rizzarelli, E., Monzani, E., & Casella, L. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b03153 · Cited by 23

The prion protein and its ligands: Insights into structure-function relationships

Shafiq, M., Vela, S. D., Amin, L., Younas, N., Harris, D. A., Zerr, I., Altmeppen, H. C., Svergun, D. I., & Glatzel, M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119240 · Cited by 21

Lipid Rafts Act as a Common Platform for Amyloid-β Oligomer-Induced Alzheimer’s Disease Pathology

Kawarabayashi, T., Nakamura, T., Sato, K., Seino, Y., Ichii, S., Nakahata, N., Takatama, M., Westaway, D. A., George‐Hyslop, P. S., & Shoji, M. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215662 · Cited by 22

Senegenin Inhibits Aβ1-42-Induced PC12 Cells Apoptosis and Oxidative Stress via Activation of the PI3K/Akt Signaling Pathway

Ren, X., Zhang, J., Zhao, Y., & Sun, L. (2022) · Dove Medical Press (Taylor and Francis Group) · Cited by 21

Regulation of beta‐amyloid for the treatment of Alzheimer's disease: Research progress of therapeutic strategies and bioactive compounds

Qiu, W., Liu, H., Liu, Y., Lü, X., Wang, L., Hu, Y., Feng, F., Li, Q., & Sun, H. (2023) · Medicinal Research Reviews · doi:10.1002/med.21947 · Cited by 20

Regulation of Neuronal Gene Expression by Local Axonal Translation

Korsak, L. I. T., Mitchell, M. E., Shepard, K. A., & Akins, M. R. (2016) · Current Genetic Medicine Reports · doi:10.1007/s40142-016-0085-2 · Cited by 21

Prion protein as a mediator of synaptic transmission

Steinert, J. R. (2015) · Communicative & Integrative Biology · doi:10.1080/19420889.2015.1063753 · Cited by 20

Functions of the cellular prion protein, the end of Moore's law, and Ockham's razor theory

del Rı́o, J. A., & Gavı́n, R. (2016) · Prion · doi:10.1080/19336896.2015.1126038 · Cited by 19

Hijacking PrPc-dependent signal transduction: when prions impair Aβ clearance

Hernandez-Rapp, J., Martin‐Lannerée, S., Hirsch, T. Z., Launay, J., & Mouillet‐Richard, S. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00025 · Cited by 24

The prion protein regulates glutamate-mediated Ca2+ entry and mitochondrial Ca2+ accumulation in neurons

Mario, A. D., Peggion, C., Massimino, M. L., Viviani, F., Castellani, A., Giacomello, M., Lim, D., Bertoli, A., & Sorgato, M. C. (2017) · Journal of Cell Science · doi:10.1242/jcs.196972 · Cited by 21

Copper- and Zinc-Promoted Interdomain Structure in the Prion Protein: A Mechanism for Autoinhibition of the Neurotoxic N-Terminus

Evans, E. G. B., & Millhauser, G. L. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.06.005 · Cited by 20

Transgenic Overexpression of the Disordered Prion Protein N1 Fragment in Mice Does Not Protect Against Neurodegenerative Diseases Due to Impaired ER Translocation

Mohammadi, B., Linsenmeier, L., Shafiq, M., Puig, B., Galliciotti, G., Giudici, C., Willem, M., Eden, T. W., Koch‐Nolte, F., Lin, Y.-H., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01917-2 · Cited by 20

Lipid rafts: linking prion protein to zinc transport and amyloid-β toxicity in Alzheimer's disease

Watt, N. T., Jarosz-Griffiths, H., & Hooper, N. M. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00041 · Cited by 22

Amelioration of amyloid β‐FcγRIIb neurotoxicity and tau pathologies by targeting LYN

Gwon, Y., Kim, S.-H., Kim, H. T., Kam, T.-I., Park, J., Lim, B., Cha, H., Chang, H.-J., Hong, Y. R., & Jung, Y.-K. (2019) · The FASEB Journal · doi:10.1096/fj.201800926r · Cited by 20

Inhibition of mGluR5/PI3K-AKT Pathway Alleviates Alzheimer’s Disease-Like Pathology Through the Activation of Autophagy in 5XFAD Mice

Chen, Y., Zhang, Y., Chen, Q., Liu, Y., Wei, X., Wu, M., Zhang, K., Liu, Y., & Wei, W. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-221058 · Cited by 19

Evidence that Alzheimer’s Disease Is a Disease of Competitive Synaptic Plasticity Gone Awry

Huang, Z. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240042 · Cited by 20

Alzheimer’s disease: Key developments support promising perspectives for therapy

Meldolesi, J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104316 · Cited by 19

Role of the TRPC1 Channel in Hippocampal Long-Term Depression and in Spatial Memory Extinction

Yerna, X., Schakman, O., Ratbi, I., Kreis, A., Lepannetier, S., de Clippele, M., Achouri, Y., Tajeddine, N., Tissir, F., Gualdani, R., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051712 · Cited by 19

Plexin-A4 mediates amyloid-β–induced tau pathology in Alzheimer’s disease animal model

Chung, S., Yang, J., Kim, H. J., Hwang, E. M., Lee, W., Suh, K. Y., Choi, H., & Mook‐Jung, I. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102075 · Cited by 17

Positron Emission Tomography in Animal Models of Alzheimer’s Disease Amyloidosis: Translational Implications

Ni, R. (2021) · Pharmaceuticals · doi:10.3390/ph14111179 · Cited by 18

Almost a century of prion protein(s): From pathology to physiology, and back to pathology

Peggion, C., Bertoli, A., & Sorgato, M. C. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.118 · Cited by 18

Mechanisms of neuroprotection against ischemic insult by stress‐inducible phosphoprotein‐1/prion protein complex

Beraldo, F. H., Ostapchenko, V. G., Xu, J. Z., Guglielmo, G. M. D., Fan, J., NICHOLLS, P. J., Caron, M. G., Prado, V. F., & Prado, M. A. M. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14281 · Cited by 18

Effects of Prion Protein on Aβ42 and Pyroglutamate-Modified AβpΕ3-42 Oligomerization and Toxicity

Pagano, K., Galante, D., D’Arrigo, C., Corsaro, A., Nizzari, M., Florio, T., Molinari, H., Tomaselli, S., & Ragona, L. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1202-x · Cited by 20

Amyloid-β1-42 dynamically regulates the migration of neural stem/progenitor cells via MAPK-ERK pathway

Wang, Z., Chen, Y., Li, X., Sultana, P., Yin, M., & Wang, Z. (2018) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2018.11.001 · Cited by 18

Vascular and non‐vascular contributors to memory reduction during traumatic brain injury

Charkviani, M., Muradashvili, N., & Lominadze, D. G. (2019) · European Journal of Neuroscience · doi:10.1111/ejn.14390 · Cited by 17

Binding between Prion Protein and Aβ Oligomers Contributes to the Pathogenesis of Alzheimer’s Disease

Kong, C., Xie, H., Gao, Z., Shao, M., Li, H., Shi, R., Cai, L., Gao, S., Sun, T., & Li, C. (2019) · Virologica Sinica · doi:10.1007/s12250-019-00124-1 · Cited by 18

Dissecting the copper bioinorganic chemistry of the functional and pathological roles of the prion protein: Relevance in Alzheimer's disease and cancer

Posadas, Y., López-Guerrero, V. E., Segovia, J., Perez‐Cruz, C., & Quintanar, L. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.102098 · Cited by 18

The MK2 cascade mediates transient alteration in mGluR‐LTD and spatial learning in a murine model of Alzheimer's disease

Privitera, L., Hogg, E. L., Lopes, M., Domingos, L. B., Gaestel, M., Müller, J., Wall, M. J., & Corrêa, S. A. L. (2022) · Aging Cell · doi:10.1111/acel.13717 · Cited by 17

Homer1a and mGluR1/5 Signaling in Homeostatic Sleep Drive and Output.

Martin, S. C., Monroe, S., & Diering, G. H. (2019) · Europe PMC (PubMed Central) · Cited by 18

Calmodulin and Amyloid Beta as Coregulators of Critical Events during the Onset and Progression of Alzheimer’s Disease

O’Day, D. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021393 · Cited by 17

Prions and Prion-Like Pathogens in Neurodegenerative Disorders

Peggion, C., Sorgato, M. C., & Bertoli, A. (2014) · Pathogens · doi:10.3390/pathogens3010149 · Cited by 17

Amyloid-β Causes NMDA Receptor Dysfunction and Dendritic Spine Loss through mGluR1 and AKAP150-Anchored Calcineurin Signaling

Prikhodko, O., Freund, R. K., Sullivan, E. M., Kennedy, M. J., & Dell’Acqua, M. L. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0675-24.2024 · Cited by 16

The Density of Group I mGlu5 Receptors Is Reduced along the Neuronal Surface of Hippocampal Cells in a Mouse Model of Alzheimer’s Disease

Martín‐Belmonte, A., Aguado, C., Alfaro‐Ruiz, R., Albasanz, J. L., Martı́n, M., Moreno‐Martínez, A. E., Fukazawa, Y., & Luján, R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115867 · Cited by 17

Prions induce an early Arc response and a subsequent reduction in mGluR5 in the hippocampus

Ojeda-Juárez, D., Lawrence, J. A., Soldau, K., Pizzo, D. P., Wheeler, E. C., Aguilar‐Calvo, P., Khuu, H., Chen, J., Malik, A., Funk, G., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105834 · Cited by 15

eEF2K regulates pain through translational control of BDNF

Smith, P. R., Garcia, G., Meyer, A. R., Ryazanov, A. G., Ma, T., Loerch, S., & Campbell, Z. T. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.023 · Cited by 17

Phosphoinositides: Two-Path Signaling in Neuronal Response to Oligomeric Amyloid β Peptide

Uranga, R. M., Alza, N. P., Conde, M. A., Antollini, S. S., & Salvador, G. A. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9885-3 · Cited by 16

PICALM rescues glutamatergic neurotransmission, behavioural function and survival in a Drosophila model of Aβ42 toxicity

Yu, Y., Niccoli, T., Ren, Z., Woodling, N. S., Aleyakpo, B., Szabadkai, G., & Partridge, L. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa125 · Cited by 19

News about Therapies of Alzheimer’s Disease: Extracellular Vesicles from Stem Cells Exhibit Advantages Compared to Other Treatments

Meldolesi, J. (2022) · Biomedicines · doi:10.3390/biomedicines10010105 · Cited by 16

Monitoring Ca2+ elevations in individual astrocytes upon local release of amyloid beta in acute brain slices

Tyurikova, O., Zheng, K., Rings, A., Drews, A., Klenerman, D., & Rusakov, D. A. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.12.007 · Cited by 18

Revisiting the Radiosynthesis of [18F]FPEB and Preliminary PET Imaging in a Mouse Model of Alzheimer’s Disease

Varlow, C., Murrell, E., Holland, J. P., Kassenbrock, A. R., Shannon, W. E. M. M., Liang, S. H., Vasdev, N., & Stephenson, N. A. (2020) · Molecules · doi:10.3390/molecules25040982 · Cited by 15

Structure of the photoreceptor synaptic assembly of the extracellular matrix protein pikachurin with the orphan receptor GPR179

Patil, D. N., Pantalone, S., Cao, Y., Laboute, T., Novick, S. J., Singh, S., Savino, S., Faravelli, S., Magnani, F., Griffin, P. R., et al. (2023) · Science Signaling · doi:10.1126/scisignal.add9539 · Cited by 15

Tau pathology is associated with postsynaptic metabotropic glutamate receptor 5 (mGluR5) in early Alzheimer's disease in a sex‐specific manner

Wang, Y., Wang, J., Chen, X., Lin, Z., You, Z., He, K., Guo, T., Zhao, J., Huang, Q., Ni, R., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70004 · Cited by 17

The Level of NMDA Receptor in the Membrane Modulates Amyloid-β Association and Perforation

Peters, C., Sepúlveda, F. J., Fernández-Pérez, E. J., Peoples, R. W., & Aguayo, L. G. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160170 · Cited by 15

Aβ41 Aggregates More Like Aβ40 than Like Aβ42: In Silico and in Vitro Study

Nguyen, H. L., Thu, T. T. M., Truong, P. M., Lan, P. D., Man, V. H., Nguyen, P. H., Tu, L. A., Chen, Y.-C., & Li, M. S. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b06368 · Cited by 15

Toward a unified therapeutics approach targeting putative amyloid-β oligomer receptors

Overk, C., & Masliah, E. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414554111 · Cited by 16

mGluR5 Positive and Negative Allosteric Modulators Differentially Affect Dendritic Spine Density and Morphology in the Prefrontal Cortex

LaCrosse, A., Taylor, S. B., Nemirovsky, N. E., Gass, J. T., & Olive, M. F. (2015) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527314666150429112849 · Cited by 15

mGluR5 as a Potential Orchestrator of Astrocyte Interactions in Neurological Disorders

Kim, J., Lee, J., Song, H., Koo, J. W., & Kang, S. (2025) · Neural Plasticity · doi:10.1155/np/7259018 · Cited by 14

Reduced Abundance and Subverted Functions of Proteins in Prion-Like Diseases: Gained Functions Fascinate but Lost Functions Affect Aetiology

Allison, W. T., DuVal, M. G., Nguyen-Phuoc, K., & Leighton, P. L. A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102223 · Cited by 17

Amyloid-β1-42 oligomers enhance mGlu5R-dependent synaptic weakening via NMDAR activation and complement C5aR1 signaling

Ng, A. N., Salter, E. W., Georgiou, J., Bortolotto, Z. A., & Collingridge, G. L. (2023) · iScience · doi:10.1016/j.isci.2023.108412 · Cited by 16

Dextran sulfate sodium inhibits amyloid‐β oligomer binding to cellular prion protein

Aimi, T., Suzuki, K., Hoshino, T., & Mizushima, T. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13166 · Cited by 14

Soluble Aβ aggregates can inhibit prion propagation

Sarell, C. J., Quarterman, E., Yip, D. C.-M., Terry, C., Nicoll, A. J., Wadsworth, J. D. F., Farrow, M. A., Walsh, D. M., & Collinge, J. (2017) · Open Biology · doi:10.1098/rsob.170158 · Cited by 14

Attenuation of Acute Intracerebral Hemorrhage-Induced Microglial Activation and Neuronal Death Mediated by the Blockade of Metabotropic Glutamate Receptor 5 In Vivo

Rahman, M. S., Yang, J., Luan, Y., Qiu, Z., Zhang, J., Lü, H., Chen, X., & Liu, Y. U. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03006-1 · Cited by 14

Resveratrol Differently Modulates Group I Metabotropic Glutamate Receptors Depending on Age in SAMP8 Mice

Sánchez-Melgar, A., Albasanz, J. L., Pallàs, M., & Martı́n, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00067 · Cited by 14

Anchorless risk or released benefit? An updated view on the ADAM10-mediated shedding of the prion protein

Mohammadi, B., Song, F., Matamoros‐Angles, A., Shafiq, M., Daμμe, M., Puig, B., Glatzel, M., & Altmeppen, H. C. (2022) · Cell and Tissue Research · doi:10.1007/s00441-022-03582-4 · Cited by 15

A 3D human iPSC-derived multi-cell type neurosphere system to model cellular responses to chronic amyloidosis

Wendt, S., Lin, A. J., Ebert, S. N., Brennan, D. J., Cai, W., Bai, Y., Kong, D. Y., Sorrentino, S., Groten, C. J., Lee, C., et al. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03433-3 · Cited by 13

Potential role of IP3/Ca2+ signaling and phosphodiesterases: Relevance to neurodegeneration in Alzheimer’s disease and possible therapeutic strategies

Dutta, B. J., Singh, S., Seksaria, S., Gupta, G. D., Bodakhe, S. H., & Singh, A. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115071 · Cited by 15

FGFR3 drives Aβ-induced tau uptake

Kim, D. K., Suh, K. Y., Park, J., Lee, S., Han, J., Chang, S., Kim, Y., & Mook‐Jung, I. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01274-3 · Cited by 14

Neuroprotective effect and potential of cellular prion protein and its cleavage products for treatment of neurodegenerative disorders part I. a literature review

Dexter, E., & Kong, Q. (2021) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2021.1965881 · Cited by 14

Is PSD-95 entangled in the side effects of antidepressants?

Stachowicz, K. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105391 · Cited by 12

Amyloid-β oligomers trigger sex-dependent inhibition of GIRK channel activity in hippocampal neurons in mice

Luo, H., de Velasco, E. M. F., Gansemer, B. M., Frederick, M. H., Aguado, C., Luján, R., Thayer, S. A., & Wickman, K. (2024) · Science Signaling · doi:10.1126/scisignal.ado4132 · Cited by 11

The role of the cellular prion protein in the uptake and toxic signaling of pathological neurodegenerative aggregates

Scialò, C., & Legname, G. (2020) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2020.08.008 · Cited by 12

Sigma ligands as potent inhibitors of Aβ and AβOs in neurons and promising therapeutic agents of Alzheimer's disease

Ma, W., Chen, A.-F., Xie, X., & Huang, Y. (2020) · Neuropharmacology · doi:10.1016/j.neuropharm.2020.108342 · Cited by 12

Early Effects of the Soluble Amyloid β25-35 Peptide in Rat Cortical Neurons: Modulation of Signal Transduction Mediated by Adenosine and Group I Metabotropic Glutamate Receptors

Castillo, C. A., Ballesteros‐Yáñez, I., León, D., Albasanz, J. L., & Martı́n, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126577 · Cited by 12

Stability in distribution for a stochastic Alzheimer’s disease model with reaction diffusion

Hu, J., Zhang, Q., Meyer‐Baese, A., & Ye, M. (2022) · Nonlinear Dynamics · doi:10.1007/s11071-022-07387-6 · Cited by 12

Development of small-molecule Tau-SH3 interaction inhibitors that prevent amyloid-β toxicity and network hyperexcitability

Roth, J. R., Rush, T., Thompson, S. J., Aldaher, A. R., Dunn, T. B., Mesina, J. S., Cochran, J. N., Boyle, N. R., Dean, H. B., Yang, Z. W., et al. (2023) · Neurotherapeutics · doi:10.1016/j.neurot.2023.10.001 · Cited by 12

AD molecular: Molecular imaging of Alzheimer's disease: PET imaging of neurotransmitter systems

Mecca, A. P. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.04.003 · Cited by 13

Sleep deprivation regulates availability of PrPC and Aβ peptides which can impair interaction between PrPC and laminin and neuronal plasticity

da Luz, M. H. M., Pino, J. M. V., Santos, T. G., Antunes, H. K. M., Martins, V. R., de Souza, A. A. L., Torquato, R. J. S., & Lee, K. S. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14960 · Cited by 11

Linkage of Non-receptor Tyrosine Kinase Fyn to mGlu5 Receptors in Striatal Neurons in a Depression Model

Mao, L., & Wang, J. Q. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.02.048 · Cited by 12

Adenosine and Metabotropic Glutamate Receptors Are Present in Blood Serum and Exosomes from SAMP8 Mice: Modulation by Aging and Resveratrol

Sánchez-Melgar, A., Albasanz, J. L., Griñán‐Ferré, C., Pallàs, M., & Martı́n, M. (2020) · Cells · doi:10.3390/cells9071628 · Cited by 12

Decoding the function of the N-terminal tail of the cellular prion protein to inspire novel therapeutic avenues for neurodegenerative diseases

Iraci, N., Stincardini, C., Barreca, M. L., & Biasini, E. (2014) · Virus Research · doi:10.1016/j.virusres.2014.10.015 · Cited by 12

Gene-environment interaction promotes Alzheimer's risk as revealed by synergy of repeated mild traumatic brain injury and mouse App knock-in

Chiasseu, M., Fesharaki‐Zadeh, A., Saito, T., Saido, T. C., & Strittmatter, S. M. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105059 · Cited by 11

Oligomers of Amyloid β Prevent Physiological Activation of the Cellular Prion Protein-Metabotropic Glutamate Receptor 5 Complex by Glutamate in Alzheimer Disease

Haas, L. T., & Strittmatter, S. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.720664 · Cited by 75

Metabotropic glutamate receptor 5 couples cellular prion protein to intracellular signalling in Alzheimer’s disease

Haas, L. T., Salazar, S. V., Kostylev, M. A., Um, J. W., Kaufman, A. C., & Strittmatter, S. M. (2015) · Brain · doi:10.1093/brain/awv356 · Cited by 145

Therapeutic Molecules and Endogenous Ligands Regulate the Interaction between Brain Cellular Prion Protein (PrPC) and Metabotropic Glutamate Receptor 5 (mGluR5)

Haas, L. T., Kostylev, M. A., & Strittmatter, S. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.584342 · Cited by 91

Prion Protein Complex with mGluR5 Mediates Amyloid-ß Synaptic Loss in Alzheimer’s Disease

Roseman, G. P., Fu, L., & Strittmatter, S. M. (2023) · Springer eBooks · doi:10.1007/978-3-031-20565-1_22

Cellular prion protein as a receptor for amyloid-β oligomers in Alzheimer's disease

Salazar, S. V., & Strittmatter, S. M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.062 · Cited by 94