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Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Open accessAbstract
A pathological hallmark of Alzheimer's disease is an accumulation of insoluble plaque containing the amyloid-beta peptide of 40-42 amino acid residues. Prefibrillar, soluble oligomers of amyloid-beta have been recognized to be early and key intermediates in Alzheimer's-disease-related synaptic dysfunction. At nanomolar concentrations, soluble amyloid-beta oligomers block hippocampal long-term potentiation, cause dendritic spine retraction from pyramidal cells and impair rodent spatial memory. Soluble amyloid-beta oligomers have been prepared from chemical syntheses, transfected cell culture supernatants, transgenic mouse brain and human Alzheimer's disease brain. Together, these data imply a high-affinity cell-surface receptor for soluble amyloid-beta oligomers on neurons-one that is central to the pathophysiological process in Alzheimer's disease. Here we identify the cellular prion protein (PrP(C)) as an amyloid-beta-oligomer receptor by expression cloning. Amyloid-beta oligomers bind with nanomolar affinity to PrP(C), but the interaction does not require the infectious PrP(Sc) conformation. Synaptic responsiveness in hippocampal slices from young adult PrP null mice is normal, but the amyloid-beta oligomer blockade of long-term potentiation is absent. Anti-PrP antibodies prevent amyloid-beta-oligomer binding to PrP(C) and rescue synaptic plasticity in hippocampal slices from oligomeric amyloid-beta. Thus, PrP(C) is a mediator of amyloid-beta-oligomer-induced synaptic dysfunction, and PrP(C)-specific pharmaceuticals may have therapeutic potential for Alzheimer's disease.
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In the citing paper
“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 [37]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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 [37]
Experimental — accuracy not yet measuredIn the citing paper
“Aβ binds to α7 nicotinic acetylcholine receptors (α7 nAChRs) and to metabotropic glutamate receptors, in particular mGluR5 [31–33].”
From ApoE, ApoE Receptors, and the Synapse in Alzheimer's Disease (2017) · cites this paper as [33]
In the citing paper
“A genome-wide association study (GWAS) identified PrPC as a potential high-affinity receptor for oAβ [87].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [87]
In the citing paper
“Subsequent studies showed that oAβ, especially high-molecular weight oligomers [88], preferentially bind to PrPC within an N-terminal 95-111aa segment [87].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [87]
In the citing paper
“oligomer binding is significantly reduced in PrPC knock-out cells (Lauren et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lauren et al., 2009
In the citing paper
“Aβ oligomers bind with nanomolar affinity to cellular prion protein (PrPC) and that anti-PrP antibodies reduce oligomer binding to neurons and rescue synaptic plasticity (Lauren et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lauren et al., 2009
In the citing paper
“explaining the finding that knocking-down these proteins or adding antibodies against their extracellular domains blocks the accumulation of ADDL clusters (“hotspots”) at synapses (De Felice et al., 2007; Decker et al., 2010a; Lauren et al., 2009).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Lauren et al., 2009
In the citing paper
“PrPC binds synthetic Aβ oligomers with high affinity and plays a role in the oligomer-mediated inhibition of LTP (17).”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [17]
In the citing paper
“In an elegant study Lauren et al. (17) reported that PrPC mediates the Aβ oligomer-induced hippocampal synaptic plasticity impairment.”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [17]
In the citing paper
“The 22 °C-Aβ oligomers impaired recognition memory in both Prnp +/+ and Prnp 0/0 mice (Fig. 4C).”
From Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein (2010) · cites this paper as [17]
In the citing paper
“When amyloid-β oligomers bind to PrPc, long-term potentiation and the formation of new memories are disrupted [129,130,131].”
From Sigma-2 Receptors—From Basic Biology to Therapeutic Target: A Focus on Age-Related Degenerative Diseases (2023) · cites this paper as [130]
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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedThe 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
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
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
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
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012
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 1,722
Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
Büeler, H., Fischer, M., Lang, Y., Bluethmann, H., Lipp, H., DeArmond, S. J., Prusiner, S. B., Aguet, M., & Weissmann, C. (1992) · Nature · doi:10.1038/356577a0 · Cited by 1,678
Shankar, 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
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Muradashvili, N., Benton, R. L., Saatman, K. E., Tyagi, S. C., & Lominadze, D. G. (2014) · Metabolic Brain Disease · doi:10.1007/s11011-014-9550-3 · Cited by 66
Mallucci, G. R. (2009) · Prion · doi:10.4161/pri.3.4.9981 · Cited by 66
Yamamoto, K., Ueta, Y., Wang, L., Yamamoto, R., Inoue, N., Inokuchi, K., Aiba, A., Yonekura, H., & Kato, N. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6752-10.2011 · Cited by 69
Review: Contribution of transgenic models to understanding human prion disease
Wadsworth, J. D. F., Asante, E. A., & Collinge, J. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01129.x · Cited by 67
Béland, M., & Roucou, X. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07613.x · Cited by 65
Eisbach, S. E., & Outeiro, T. F. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1038-9 · Cited by 65
Walsh, K. P., Minamide, L. S., Kane, S. J., Shaw, A. E., Brown, D. R., Pulford, B. E., Zabel, M. D., Lambeth, J. D., Kuhn, T. B., & Bamburg, J. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095995 · Cited by 69
Scarano, S., Lisi, S., Ravelet, C., Peyrin, É., & Minunni, M. (2016) · Analytica Chimica Acta · doi:10.1016/j.aca.2016.08.008 · Cited by 65
Beraldo, F. H., Ostapchenko, V. G., Caetano, F. A., Guimarães, A. L. S., Ferretti, G. D. S., Daude, N., Bertram, L. N., Nogueira, K. D. O. P. C., Silva, J. L., Westaway, D. A., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.738286 · Cited by 67
Prion-like propagation of β-amyloid aggregates in the absence of APP overexpression
Ruiz‐Riquelme, A., Lau, H. H. C., Stuart, E., Goczi, A. N., Wang, Z., Schmitt‐Ulms, G., & Watts, J. C. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0529-x · Cited by 69
The neuronal insulin receptor in its environment
Gralle, M. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13909 · Cited by 64
PTK2B/Pyk2 overexpression improves a mouse model of Alzheimer's disease
Giralt, A., de Pins, B., Cifuentes-Díaz, C., López-Molina, L., Farah, A. T., Tible, M., Deramecourt, V., Arold, S. T., Ginés, S., Hugon, J., et al. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.05.020 · Cited by 64
Amyloid and Alzheimer's Disease: Inside and Out
Tam, J. H. K., & Pasternak, S. (2012) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100013408 · Cited by 64
CRISPR-Cas9-Based Knockout of the Prion Protein and Its Effect on the Proteome
Mehrabian, M., Dylan, B., MacIsaac, S., Kim, J. K., Gunawardana, C. G., Wang, H., & Schmitt‐Ulms, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0114594 · Cited by 64
A role for the neurexin–neuroligin complex in Alzheimer's disease
Sindi, I. A., Tannenberg, R. K., & Dodd, P. R. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.032 · Cited by 65
Biscaro, B., Lindvall, O., Höck, C., Ekdahl, C. T., & Nitsch, R. M. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2055-09.2009 · Cited by 64
The functional neurophysiology of the amyloid precursor protein (APP) processing pathway
Randall, A. D., Witton, J., Booth, C., Hynes-Allen, A. M., & Brown, J. T. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.02.011 · Cited by 66
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Guglielmotto, M., Monteleone, D., Giliberto, L., Fornaro, M., Borghi, R., Tamagno, E., & Tabaton, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110884 · Cited by 64
Tamagnini, F., Scullion, S., Brown, J. T., & Randall, A. D. (2014) · Hippocampus · doi:10.1002/hipo.22403 · Cited by 66
Kaiser, D., Acharya, M., Leighton, P. L. A., Wang, H., Daude, N., Wohlgemuth, S. L., Shi, B., & Allison, W. T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051305 · Cited by 63
Alzheimer brain-derived amyloid β-protein impairs synaptic remodeling and memory consolidation
Borlikova, G. G., Trejo, M., Mably, A. J., Donald, J. M. M., Frigerio, C. S., Regan, C. M., Murphy, K. J., Masliah, E., & Walsh, D. M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.10.028 · Cited by 65
Role of Tau Protein in Neuronal Damage in Alzheimer's Disease and Down Syndrome
Cárdenas, A. M., Ardiles, Á. O., Barraza, N., Báez‐Matus, X., & Caviedes, P. A. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.012 · Cited by 68
Puig, B., Altmeppen, H. C., & Glatzel, M. (2014) · Prion · doi:10.4161/pri.27892 · Cited by 63
Zhang, H., Wu, S., & Xing, D. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.09.004 · Cited by 64
Matheou, C. J., Younan, N. D., & Viles, J. H. (2014) · Biochemical Journal · doi:10.1042/bj20141168 · Cited by 64
Prion Neurotoxicity: Insights from Prion Protein Mutants
Solomon, I. H., Schepker, J. A., & Harris, D. A. (2010) · Caister Academic Press eBooks · doi:10.21775/9781912530076.01 · Cited by 63
Mallucci, G. R., Klenerman, D., & Rubinsztein, D. C. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-040320-120625 · Cited by 62
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Wongchitrat, P., Chanmee, T., & Govitrapong, P. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03761-6 · Cited by 65
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Oliveira, L. M. A., Gomes, R. A., Yang, D. T., Dennison, S. R., Família, C., Lages, A., Coelho, A. V., Murphy, R. M., Phoenix, D. A., & Quintas, A. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2012.12.001 · Cited by 62
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Zou, W., Langeveld, J., Xiao, X., Chen, S., McGeer, P. L., Yuan, J., Payne, M. C., Kang, H., McGeehan, J. E., Sy, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.088831 · Cited by 62
Rubenstein, R., Chang, B., Grinkina, N., Drummond, E., Davies, P., Ruditzky, M., Sharma, D. R., Wang, K., & Wısnıewskı, T. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0435-7 · Cited by 63
Cheng, L., Zhao, W., & Hill, A. F. (2017) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2017.11.011 · Cited by 65
Matos, C. O., Passos, Y. M., do Amaral, M. J., Macedo, B., Tempone, M. H., Bezerra, O. C. D. L., Moraes, M. O., Almeida, M. S., Weber, G., Missailidis, S., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201901897r · Cited by 62
Mukhopadhyay, S. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c07598 · Cited by 61
Endocytic pathways mediating oligomeric Aβ42 neurotoxicity
Yu, C., Nwabuisi‐Heath, E., Laxton, K., & LaDu, M. J. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-19 · Cited by 63
Aptamer and its applications in neurodegenerative diseases
Qu, J. T., Yu, S., Yuan, Z., Zheng, Y., Yang, H., & Zhang, J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2345-4 · Cited by 62
Alzheimer’s disease: analysis of a mathematical model incorporating the role of prions
Helal, M., Hingant, E., Pujo-Menjouet, L., & Webb, G. F. (2013) · Journal of Mathematical Biology · doi:10.1007/s00285-013-0732-0 · Cited by 62
The levels of water-soluble and triton-soluble Aβ are increased in Alzheimer's disease brain
McDonald, J. M., Cairns, N. J., Taylor‐Reinwald, L., Holtzman, D. M., & Walsh, D. M. (2012) · Brain Research · doi:10.1016/j.brainres.2012.02.041 · Cited by 61
Kellock, J., Hopping, G., Caughey, B. W., & Daggett, V. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.013 · Cited by 60
Thomas, M. H., Pelleïeux, S., Vitale, N., & Olivier, J. L. (2016) · Biochimie · doi:10.1016/j.biochi.2016.07.013 · Cited by 60
Shi, X., Sun, K., Hu, R., Liu, X.-Y., Hu, Q., Sun, X., Yao, B., Sun, N., Hao, J., Wei, P., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1327-16.2016 · Cited by 63
Zhang, Y., Zhao, Y., Zhang, L., Yu, W., Wang, Y., & Chang, W. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00339 · Cited by 58
Homeostatic Disinhibition in the Aging Brain and Alzheimer's Disease
Gleichmann, M., Chow, V. W., & Mattson, M. P. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101674 · Cited by 59
Stravalaci, M., Bastone, A., Beeg, M., Cagnotto, A., Colombo, L., Fede, G. D., Tagliavini, F., Cantú, L., Favero, E. D., Mazzanti, M., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.334979 · Cited by 60
Fleisch, V. C., Leighton, P. L. A., Wang, H., Pillay, L. M., Ritzel, R. G., Bhinder, G., Roy, B., Tierney, K. B., Ali, D. W., Waskiewicz, A. J., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.03.007 · Cited by 62
Sink Hypothesis and Therapeutic Strategies for Attenuating Aβ Levels
Zhang, Y., & Lee, D. H. S. (2011) · The Neuroscientist · doi:10.1177/1073858410381532 · Cited by 61
Antibody-based therapy in Alzheimer's disease
Pul, R., Dodel, R. C., & Stangel, M. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.552884 · Cited by 59
G Protein–Coupled Receptors, Cholinergic Dysfunction, and Aβ Toxicity in Alzheimer’s Disease
Thathiah, A., & Strooper, B. D. (2009) · Science Signaling · doi:10.1126/scisignal.293re8 · Cited by 59
Marcello, E. E., Borroni, B., Pelucchi, S., Gardoni, F., & Luca, M. D. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1386176 · Cited by 58
Amin, L., & Harris, D. A. (2021) · Nature Communications · doi:10.1038/s41467-021-23507-z · Cited by 59
Gomes, P., Tzouanou, F., Skolariki, K., Vamvaka-Iakovou, A., Nogueras‐Ortiz, C. J., Tsirtsaki, K., Waites, C. L., Vlamos, P., Sousa, N., Costa‐Silva, B., et al. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114183 · Cited by 60
Alzheimer's disease therapeutic research: the path forward
Aisen, P. S. S. (2009) · Alzheimer s Research & Therapy · doi:10.1186/alzrt2 · Cited by 59
ADSC Therapy in Neurodegenerative Disorders
Chan, T.-M., Chen, J. Y.-R., Ho, L.-I., Lin, H.-P., Hsueh, K.-W., Liu, D. D., Chen, Y.-H., Hsieh, A.-C., Tsai, N., Hueng, D., et al. (2014) · Cell Transplantation · doi:10.3727/096368914x678445 · Cited by 57
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Li, J., Zhang, C., Li, J., Li, F., Jiang, X., Chen, J., Pang, Z., & Zhang, Q. (2013) · Pharmaceutical Research · doi:10.1007/s11095-013-1025-4 · Cited by 57
Young, L. M., Mahood, R. A., Saunders, J. C., Tu, L., Raleigh, D. P., Radford, S. E., & Ashcroft, A. E. (2015) · The Analyst · doi:10.1039/c5an00865d · Cited by 57
Sinnen, B. L., Bowen, A. B., Gibson, E. S., & Kennedy, M. J. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1603-16.2016 · Cited by 59
Lau, H. H. C., Ingelsson, M., & Watts, J. C. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02201-2 · Cited by 57
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Ebenezer, P. J., Weidner, A. M., LeVine, H., Markesbery, W. R., Murphy, M. P., Zhang, L., Dasuri, K., Fernandez-Kim, S. O., Bruce-Keller, A. J., Gavilán, E., et al. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-101161 · Cited by 58
Peters, C., Espinoza, M. P., Gallegos, S., Opazo, C., & Aguayo, L. G. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.11.019 · Cited by 56
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Zhang, J., Wu, J., Wang, G., He, L., Zheng, Z., Wu, M., & Zhang, Y. (2023) · ACS Nano · doi:10.1021/acsnano.3c03172 · Cited by 56
Xie, G., Tian, W., Wei, T., & Liu, F. (2014) · Free Radical Research · doi:10.3109/10715762.2014.987274 · Cited by 57
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Sarkar, B., Das, A. K., & Maiti, S. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00084 · Cited by 56
Yin, C., Deng, Y., Gao, J., Li, X., Liu, Y., & Gong, Q. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.04.022 · Cited by 56
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Vitola, P. L., Beeg, M., Balducci, C., Santamaria, G., Restelli, E., Colombo, L., Caldinelli, L., Pollegioni, L., Gobbi, M., Chiesa, R., et al. (2018) · Brain · doi:10.1093/brain/awy318 · Cited by 56
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Arena, G., Mendola, D. L., Pappalardo, G., Sóvágó, I., & Rizzarelli, E. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.038 · Cited by 55
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Xu, S., Su, Z., Zhang, Z., Nie, Y., Wang, J., Ge, G., & Luo, X. (2017) · Journal of Materials Chemistry B · doi:10.1039/c7tb02129a · Cited by 55
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Lee, S., Salazar, S. V., Cox, T. O., & Strittmatter, S. M. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.2983-18.2018 · Cited by 55
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Rudajev, V., & Novotný, J. (2020) · Membranes · doi:10.3390/membranes10090226 · Cited by 55
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Siddiqui, A., Shah, Z., Jahan, R. N., Othman, I., & Kumari, Y. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112250 · Cited by 54
Bigi, A., Cascella, R., Chiti, F., & Cecchi, C. (2022) · BioEssays · doi:10.1002/bies.202200086 · Cited by 56
Ding, M., Ding, S., Du, D., Wang, X., Hu, X., Guan, P., Lyu, Z., & Lin, Y. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117087 · Cited by 54
Amyloid beta receptors responsible for neurotoxicity and cellular defects in Alzheimer’s disease
Kam, T., Gwon, Y., & Jung, Y. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1706-0 · Cited by 59
Deleterious effects of soluble amyloid-β oligomers on multiple steps of synaptic vesicle trafficking
Park, J., Jang, M., & Chang, S. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.03.004 · Cited by 57
Gourdain, P., Ballerini, C., Nicot, A. B., & Carnaud, C. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-25 · Cited by 54
New insights into cellular prion protein (PrPc) functions: The “ying and yang” of a relevant protein
Nicolás, O., Gavı́n, R., & del Rı́o, J. A. (2009) · Brain Research Reviews · doi:10.1016/j.brainresrev.2009.06.002 · Cited by 54
Jen, A., Parkyn, C. J., Mootoosamy, R. C., Ford, M. J., Warley, A., Liu, Q., Bu, G., Baskakov, I. V., Moestrup, S. K., McGuinness, L., et al. (2010) · Journal of Cell Science · doi:10.1242/jcs.058099 · Cited by 57
Lizama, B. N., Kahle, J., Catalano, S. M., Caggiano, A. O., Grundman, M., & Hamby, M. E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076251 · Cited by 54
Tau acts as a mediator forAlzheimer's disease‐related synaptic deficits
Liao, D., Miller, E. C., & Teravskis, P. J. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12504 · Cited by 53
The Binding Receptors of Aβ: an Alternative Therapeutic Target for Alzheimer’s Disease
Xia, M., Cheng, X., Yi, R., Gao, D., & Xiong, J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8994-0 · Cited by 53
Amyloid Oligomer Neurotoxicity, Calcium Dysregulation, and Lipid Rafts
Malchiodi‐Albedi, F., Paradisi, S., Matteucci, A., Frank, C., & Diociaiuti, M. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/906964 · Cited by 55
Dinamarca, M. C., Weinstein, D. B., Monasterio, O., & Inestrosa, N. C. (2011) · Biochemistry · doi:10.1021/bi201246t · Cited by 53
Abu‐Rumeileh, S., Lattanzio, F., Maserati, M. S., Rizzi, R., Capellari, S., & Parchi, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160740 · Cited by 53
Cellular Prion Protein (PrPc): Putative Interacting Partners and Consequences of the Interaction
Miranzadeh Mahabadi, H., & Taghibiglou, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197058 · Cited by 52
Alzheimer’s Disease: A Molecular View of β-Amyloid Induced Morbific Events
Asik, R. M., Suganthy, N., Aarifa, M. A., Kumar, A., Szigeti, K., Máthé, D., Gulyás, B. Z., Archunan, G., & Padmanabhan, P. (2021) · Biomedicines · doi:10.3390/biomedicines9091126 · Cited by 54
Zinc Transporter mRNA Levels in Alzheimer's Disease Postmortem Brain
Beyer, N., Coulson, D. T. R., Heggarty, S., Ravid, R., Hellemans, J., Irvine, G. B., & Johnston, J. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112105 · Cited by 55
Murakami, K. (2014) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2014.940275 · Cited by 53
Roles of endoproteolytic α‐cleavage and shedding of the prion protein in neurodegeneration
Altmeppen, H. C., Prox, J., Puig, B., Dohler, F., Falker‐Gieske, C., Krasemann, S., & Glatzel, M. (2013) · FEBS Journal · doi:10.1111/febs.12196 · Cited by 56
Cissé, M., & Mucke, L. (2009) · Nature · doi:10.1038/4571090a · Cited by 52
Association of the RAGE G82S polymorphism with Alzheimer’s disease
Daborg, J., von Otter, M., Sjölander, A., Nilsson, S., Minthon, L., Gustafson, D., Skoog, I. G., Blennow, K., & Zetterberg, H. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0437-0 · Cited by 52
Wang, J., Ye, F., Cheng, X., Zhang, X., Liu, F., Liu, G., Ni, M., Qiao, S., Zhou, W., & Zhang, Y. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160138 · Cited by 52
Salazar, S. V., Gallardo, C., Kaufman, A. C., Herber, C. S., Haas, L. T., Robinson, S., Manson, J. C., Lee, M. K., & Strittmatter, S. M. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0722-17.2017 · Cited by 55
Self-citationRegulation of microglia by glutamate and its signal pathway in neurodegenerative diseases
Zhang, X., Wang, D., Zhang, B., Zhu, J., Zhou, Z., & Cui, L. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.04.001 · Cited by 53
Prion Protein: The Molecule of Many Forms and Faces
Kovač, V., & Šerbec, V. Č. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031232 · Cited by 55
Metadata
- Authors
- Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M.
- Affiliations
- Yale University (US)
- Corresponding author
- Strittmatter, Stephen M.
- Venue
- Nature
- Published
- 2009-02
- Volume
- 457
- Issue
- 7233
- Pages
- 1128-1132
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2748841
- OpenAlex
- W2171526610
- Cited by
- 1,560
- References
- 37
- Citations by year
- 2026: 46 · 2025: 45 · 2024: 50 · 2023: 52 · 2022: 87 · 2021: 82 · 2020: 85 · 2019: 71 · 2018: 108 · 2017: 117 · 2016: 103 · 2015: 98 · 2014: 104 · 2013: 116 · 2012: 119
- FWCI
- 87.03
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- U.S. Public Health Service (5T32GN07205)
- National Institute on Drug Abuse (P30DA018343)
- National Institute of Neurological Disorders and Stroke (R01NS042304, R01NS039962, R37NS033020)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- cellular prion protein, amyloid-beta oligomers, Alzheimer's disease, synaptic plasticity, long-term potentiation, cell surface receptors, lipid rafts, hippocampus, anti-PrP antibodies, prion disease, expression cloning, neurotoxicity, spatial memory, neuroprotection, neurodegeneration
- MeSH terms
- Alzheimer Disease, Amyloidosis, Animals, Chlorocebus aethiops, Hippocampus, Humans, Mice, Inbred C57BL, Neuronal Plasticity, Neurons, Peptide Fragments, Prions, Protein Binding, Receptors, Cell Surface, Synapses, Amyloid beta-Peptides, Long-Term Potentiation, COS Cells, Mice, Amyloid Precursor Protein Secretases, Protein Multimerization
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