The role of genetic risk factors of Alzheimer’s disease in synaptic dysfunction
Open accessAbstract
Alzheimer's disease (AD) is a neurodegenerative disease characterized by the progressive deterioration of cognitive functions. Due to the extended global life expectancy, the prevalence of AD is increasing among aging populations worldwide. While AD is a multifactorial disease, synaptic dysfunction is one of the major neuropathological changes that occur early in AD, before clinical symptoms appear, and is associated with the progression of cognitive deterioration. However, the underlying pathological mechanisms leading to this synaptic dysfunction remains unclear. Recent large-scale genomic analyses have identified more than 40 genetic risk factors that are associated with AD. In this review, we discuss the functional roles of these genes in synaptogenesis and synaptic functions under physiological conditions, and how their functions are dysregulated in AD. This will provide insights into the contributions of these encoded proteins to synaptic dysfunction during AD pathogenesis.
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A person with one copy of the APOE ε4 allele is more likely to be affected than a person with two copies.
“A person with one copy of this allele is more likely to be affected than a person with two copies [42,43,44].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [43]
The APOE ε4 allele greatly increases AD risk.
“The AD risk is greatly increased by the APOE ε4 allele.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [43]
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Meta-Analysis of 74,046 Individuals Identifies 11 New Susceptibility Loci for Alzheimer’s Disease
(EADI), E. A. D. I., Lambert, J.-C., (GERAD), G. A. E. R. I. A. D., Alzheimer's Disease Genetic Consortium (ADGC), (CHARGE), C. F. H. A. A. R. I. G. E., Ibrahim-Verbaas, C. A., Harold, D., Naj, A. C., Sims, R., Bellenguez, C., et al. (2013) · Nature Genetics · doi:10.1038/ng.2802 · Cited by 4,336 · see citing works
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · see citing works
<i>TREM2</i> Variants in Alzheimer's Disease
Guerreiro, R., Wojtas, A., Bras, J., Carrasquillo, M., Rogaeva, E., Majounie, E., Cruchaga, C., Sassi, C., Kauwe, J. S. K., Younkin, S., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1211851 · Cited by 3,020 · see citing works
Synapse loss in frontal cortex biopsies in Alzheimer's disease: Correlation with cognitive severity
DeKosky, S. T., & Scheff, S. W. (1990) · Annals of Neurology · doi:10.1002/ana.410270502 · Cited by 2,376 · see citing works
Disease-Associated Microglia: A Universal Immune Sensor of Neurodegeneration
Deczkowska, A., Keren-Shaul, H., Weiner, A., Colonna, M., Schwartz, M., & Amit, I. (2018) · Cell · doi:10.1016/j.cell.2018.05.003 · Cited by 1,474 · see citing works
Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies
Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425 · see citing works
Genome-wide association study identifies 74 loci associated with educational attainment
Okbay, A., Beauchamp, J. P., Fontana, M. A., Lee, J. J., Pers, T. H., Rietveld, C. A., Turley, P., Chen, G.-B., Emilsson, V., Meddens, S. F. W., et al. (2016) · Nature · doi:10.1038/nature17671 · Cited by 1,297 · see citing works
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201 · see citing works
Interleukin-33 in health and disease
Liew, F. Y., Girard, J., & Turnquist, H. R. (2016) · Nature reviews. Immunology · doi:10.1038/nri.2016.95 · Cited by 1,157 · see citing works
Lin, Y.-T., Seo, J., Gao, F., Feldman, H. M., Wen, H.-L., Penney, J., Cam, H. P., Gjoneska, E., Raja, W. K., Cheng, J., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.05.008 · Cited by 1,125 · see citing works
Trafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works
Wightman, D. P., Jansen, I. E., Savage, J. E., Shadrin, A. A., Bahrami, S., Holland, D., Rongve, A., Børte, S., Winsvold, B. S., Drange, O. K., et al. (2021) · Nature Genetics · doi:10.1038/s41588-021-00921-z · Cited by 1,011 · see citing works
TREM2 — a key player in microglial biology and Alzheimer disease
Ulland, T. K., & Colonna, M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0072-1 · Cited by 735 · see citing works
The genetics of Alzheimer disease
Tanzi, R. E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006296 · Cited by 727 · see citing works
Filipello, F., Morini, R., Corradini, I., Zerbi, V., Canzi, A., Michalski, B., Erreni, M., Markicevic, M., Starvaggi-Cucuzza, C., Otero, K., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.04.016 · Cited by 695 · see citing works
Vainchtein, I. D., Chin, G., Cho, F. S., Kelley, K. W., Miller, J. G., Chien, E. C., Liddelow, S. A., Nguyen, P. T., Nakao-Inoue, H., Dorman, L. C., et al. (2018) · Science · doi:10.1126/science.aal3589 · Cited by 657 · see citing works
Andersen, O. M., Reiche, J., Schmidt, V., Gotthardt, M., Spoelgen, R., Behlke, J., von Arnim, C. A. F., Breiderhoff, T., Jansen, P., Wu, X., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503689102 · Cited by 655 · see citing works
The Physiology, Pathology, and Potential Therapeutic Applications of the TREM2 Signaling Pathway
Deczkowska, A., Weiner, A., & Amit, I. (2020) · Cell · doi:10.1016/j.cell.2020.05.003 · Cited by 648 · see citing works
BDNF signaling in context: From synaptic regulation to psychiatric disorders
Wang, C. S., Kavalali, E. T., & Monteggia, L. M. (2021) · Cell · doi:10.1016/j.cell.2021.12.003 · Cited by 629 · see citing works
Microglial Remodeling of the Extracellular Matrix Promotes Synapse Plasticity
Nguyen, P. T., Dorman, L. C., Pan, S., Vainchtein, I. D., Han, R. T., Nakao-Inoue, H., Taloma, S. E., Barron, J. J., Molofsky, A. B., Kheirbek, M. A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.050 · Cited by 615 · see citing works
GWAS on family history of Alzheimer’s disease
Marioni, R. E., Harris, S. E., Zhang, Q., McRae, A. F., Hagenaars, S. P., Hill, W. D., Davies, G., Ritchie, C. W., Gale, C. R., Starr, J. M., et al. (2018) · Translational Psychiatry · doi:10.1038/s41398-018-0150-6 · Cited by 564 · see citing works
Schwartzentruber, J., Cooper, S., Liu, J. Z., Barrio-Hernandez, I., Bello, E., Kumasaka, N., Young, A. M. H., Franklin, R. J. M., Johnson, T., Estrada, K., et al. (2021) · Nature Genetics · doi:10.1038/s41588-020-00776-w · Cited by 532 · see citing works
Kim, T., Vidal, G. S., Djurisic, M., William, C. M., Birnbaum, M. E., Garcia, K. C., Hyman, B. T., & Shatz, C. J. (2013) · Science · doi:10.1126/science.1242077 · Cited by 410 · see citing works
Lee, C. Y. D., Daggett, A., Gu, X., Jiang, L.-L., Langfelder, P., Li, X., Wang, N., Zhao, Y., Park, C. S., Cooper, Y., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.02.002 · Cited by 396 · see citing works
Clusterin in Alzheimer’s Disease: Mechanisms, Genetics, and Lessons From Other Pathologies
Foster, E. M., Dangla-Valls, A., Lovestone, S., Ribe, E. M., & Buckley, N. J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00164 · Cited by 381 · see citing works
Zhao, J., Fu, Y., Yamazaki, Y., Ren, Y., Davis, M. D., Liu, C.-C., Lu, W., Wang, X., Chen, K., Cherukuri, Y., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19264-0 · Cited by 374 · see citing works
Differential loss of synaptic proteins in Alzheimer's disease: Implications for synaptic dysfunction
Reddy, P. H., Mani, G., Park, B. S., Jacques, J., MURDOCH, G. H., Whetsell, W. O., Kaye, J. A., & Mańczak, M. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-7203 · Cited by 372 · see citing works
IL-33 ameliorates Alzheimer's disease-like pathology and cognitive decline
Fu, A. K. Y., Hung, K.-W., Yuen, M. Y. F., Zhou, X., Mak, D. S. Y., Chan, I. C. W., Cheung, T. H., Zhang, B., Fu, W.-Y., Liew, F. Y., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604032113 · Cited by 369 · see citing works
Self-citationChen, Y., Durakoglugil, M. S., Xian, X., & Herz, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914984107 · Cited by 368 · see citing works
PirB restricts ocular-dominance plasticity in visual cortex
Syken, J., GrandPre, T., Kanold, P. O., & Shatz, C. J. (2006) · Science · doi:10.1126/science.1128232 · Cited by 340 · see citing works
Wang, C., Xiong, M., Gratuze, M., Bao, X., Shi, Y., Andhey, P. S., Manis, M., Schroeder, C., Yin, Z., Madore, C., et al. (2021) · Neuron · doi:10.1016/j.neuron.2021.03.024 · Cited by 334 · see citing works
Apolipoprotein E4 effects in Alzheimer’s disease are mediated by synaptotoxic oligomeric amyloid-β
Koffie, R. M., Hashimoto, T., Tai, H.-C., Kay, K. R., Serrano-Pozo, A., Joyner, D., Hou, S., Kopeikina, K. J., Frosch, M. P., Lee, V. M., et al. (2012) · Brain · doi:10.1093/brain/aws127 · Cited by 327 · see citing works
Cdk5 regulates EphA4-mediated dendritic spine retraction through an ephexin1-dependent mechanism
Fu, W., Chen, Y., Şahin, M., Zhao, X.-S., Shi, L., Bikoff, J. B., Lai, K., Yung, W., Fu, A. K. Y., Greenberg, M. E., et al. (2006) · Nature Neuroscience · doi:10.1038/nn1811 · Cited by 311 · see citing works
Self-citationSensory lesioning induces microglial synapse elimination via ADAM10 and fractalkine signaling
Gunner, G., Cheadle, L., Johnson, K. M., Ayata, P., Badimon, A., Mondo, E., Nagy, M. A., Liu, L., Bemiller, S. M., Kim, K.-W., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0419-y · Cited by 311 · see citing works
Loss of Bin1 Promotes the Propagation of Tau Pathology
Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works
Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258 · see citing works
Self-citationNovel allele-dependent role for APOE in controlling the rate of synapse pruning by astrocytes
Chung, W.-S., Verghese, P. B., Chakraborty, C., Joung, J., Hyman, B. T., Ulrich, J. D., Holtzman, D. M., & Barres, B. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609896113 · Cited by 242 · see citing works
Biology of GDNF and its receptors — Relevance for disorders of the central nervous system
Ibáñez, C. F., & Andressoo, J. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.01.021 · Cited by 234 · see citing works
Lynch, D. K., Winata, S. C., Lyons, R. J., Hughes, W. E., Lehrbach, G. M., Wasinger, V. C., Corthals, G. L., Cordwell, S. J., & Daly, R. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211407200 · Cited by 227 · see citing works
Production and functions of IL-33 in the central nervous system
Yasuoka, S., Kawanokuchi, J., Parajuli, B., Jin, S., Doi, Y., Noda, M., Sonobe, Y., Takeuchi, H., Mizuno, T., & Suzumura, A. (2011) · Brain Research · doi:10.1016/j.brainres.2011.02.045 · Cited by 222 · see citing works
Neurexins: molecular codes for shaping neuronal synapses
Gomez, A. M., Traunmüller, L., & Scheiffele, P. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-020-00415-7 · Cited by 221 · see citing works
Suh, J., Choi, S. H., Romano, D. M., Gannon, M. A., Lesinski, A. N., Kim, D. Y., & Tanzi, R. E. (2013) · Neuron · doi:10.1016/j.neuron.2013.08.035 · Cited by 217 · see citing works
REST and neural gene network dysregulation in iPSC models of Alzheimer’s disease
Meyer, K., Feldman, H. M., Lu, T., Drake, D., Lim, E. T., Ling, K.-H., Bishop, N. A., Pan, Y., Seo, J., Lin, Y.-T., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.023 · Cited by 216 · see citing works
Genetics of Alzheimer’s disease: where we are, and where we are going
Bellenguez, C., Grenier-Boley, B., & Lambert, J.-C. (2020) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.11.024 · Cited by 215 · see citing works
Microglia in Brain Development, Homeostasis, and Neurodegeneration
Bohlen, C. J., Friedman, B. A., Dejanovic, B., & Sheng, M. (2019) · Annual Review of Genetics · doi:10.1146/annurev-genet-112618-043515 · Cited by 212 · see citing works
Taoufik, E., Kouroupi, G., Zygogianni, O., & Matsas, R. (2018) · Open Biology · doi:10.1098/rsob.180138 · Cited by 206 · see citing works
Activity-Dependent Proteolytic Cleavage of Neuroligin-1
Suzuki, K., Hayashi, Y., Nakahara, S., Kumazaki, H., Prox, J., Horiuchi, K., Zeng, M., Tanimura, S., Nishiyama, Y., Osawa, S., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.10.003 · Cited by 204 · see citing works
Fu, A. K. Y., Hung, K.-W., Huang, H., Gu, S., Shen, Y., Cheng, E. Y. L., Ip, F. C. F., Huang, X., Fu, W.-Y., & Ip, N. Y. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405803111 · Cited by 201 · see citing works
Self-citationTranscriptomic and genetic studies identify IL-33 as a candidate gene for Alzheimer's disease
Chapuis, J., Hot, D., Hansmannel, F., Kerdraon, O., Ferreira, S., Hubans, C., Maurage, C. A., Huot, L., Bensemain, F., Laumet, G., et al. (2009) · Molecular Psychiatry · doi:10.1038/mp.2009.10 · Cited by 201 · see citing works
Coding mutations in <scp><i>SORL</i></scp><i>1</i> and <scp>A</scp>lzheimer disease
Vardarajan, B. N., Zhang, Y., Lee, J. H., Cheng, R., Bohm, C., Ghani, M., Reitz, C., Reyes‐Dumeyer, D., Shen, Y., Rogaeva, E., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24305 · Cited by 191 · see citing works
Versatile control of synaptic circuits by astrocytes: where, when and how?
Dallérac, G. M., Zapata, J., & Rouach, N. (2018) · Nature reviews. Neuroscience · doi:10.1038/s41583-018-0080-6 · Cited by 187 · see citing works
Synapse-Associated Protein-97 Mediates α-Secretase ADAM10 Trafficking and Promotes Its Activity
Marcello, E. E., Gardoni, F., Mauceri, D., Romorini, S., Jeromin, A., Epis, R., Borroni, B., Cattabeni, F., Sala, C., Padovani, A., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3439-06.2007 · Cited by 186 · see citing works
APCCdh1 mediates EphA4-dependent downregulation of AMPA receptors in homeostatic plasticity
Fu, A. K. Y., Hung, K.-W., Fu, W., Shen, C., Chen, Y., Xia, J., Lai, K., & Ip, N. Y. (2010) · Nature Neuroscience · doi:10.1038/nn.2715 · Cited by 181 · see citing works
Self-citationBjarnadóttir, M., Misner, D., Haverfield-Gross, S., Bruun, S., Helgason, V. G., Stefánsson, H., Sigmundsson, A., Firth, D. R., Nielsen, B., Stefansdottir, R., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4314-06.2007 · Cited by 176 · see citing works
Kuhn, P., Colombo, A. V., Schusser, B., Dreymüller, D., Wetzel, S., Schepers, U., Herber, J., Ludwig, A., Kremmer, E., Montag, D., et al. (2016) · eLife · doi:10.7554/elife.12748 · Cited by 173 · see citing works
BIN1 favors the spreading of Tau via extracellular vesicles
Crotti, A., Sait, H. R., McAvoy, K. M., Estrada, K., Ergun, A., Szak, S., Marsh, G., Jandreski, L., Peterson, M., Reynolds, T. L., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-45676-0 · Cited by 171 · see citing works
Çağlayan, Ş., Takagi‐Niidome, S., Liao, F., Carlo, A.-S., Schmidt, V., Burgert, T., Kitago, Y., Füchtbauer, E., Füchtbauer, A. C., Holtzman, D. M., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3007747 · Cited by 169 · see citing works
Bin1 and CD2AP polarise the endocytic generation of beta‐amyloid
Ubelmann, F., Burrinha, T., Salavessa, L., Gomes, R., Ferreira, C., Moreno, N., & Guimas Almeida, C. (2017) · The EMBO Reports · doi:10.15252/embr.201642738 · Cited by 165 · see citing works
Astrocytic ApoE reprograms neuronal cholesterol metabolism and histone-acetylation-mediated memory
Li, X., Zhang, J., Li, D., He, C., He, K., Xue, T., Wan, L., Zhang, C., & Liu, Q. (2021) · Neuron · doi:10.1016/j.neuron.2021.01.005 · Cited by 165 · see citing works
Huang, Y.-W. A., Zhou, B., Nabet, A. M., Wernig, M., & Südhof, T. C. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.2994-18.2019 · Cited by 152 · see citing works
Koo, S. J., Marković, S., Puchkov, D., Mahrenholz, C. C., Beceren‐Braun, F., Maritzen, T., Dernedde, J., Volkmer, R., Oschkinat, H., & Haucke, V. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107067108 · Cited by 142 · see citing works
Kim, J., Yoon, H., Basak, J., & Kim, J. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.0248 · Cited by 141 · see citing works
Astrocyte-secreted IL-33 mediates homeostatic synaptic plasticity in the adult hippocampus
Wang, Y., Fu, W., Cheung, K., Hung, K.-W., Chen, C., Geng, H.-Y., Yung, W., Qu, J. Y., Fu, A. K. Y., & Ip, N. Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2020810118 · Cited by 133 · see citing works
Self-citationProx, J., Bernreuther, C., Altmeppen, H. C., Grendel, J., Glatzel, M., D’Hooge, R., Stroobants, S., Ahmed, T., Balschun, D., Willem, M., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5910-12.2013 · Cited by 130 · see citing works
Subramanian, J., Savage, J. C., & Tremblay, M. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.592607 · Cited by 124 · see citing works
Bernard‐Trifilo, J. A., Kramár, E. A., Torp, R., Lin, C., Pineda, E. A., LYNCH, G. S., & Gall, C. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03062.x · Cited by 120 · see citing works
Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer’s disease
Marcello, E. E., Saraceno, C., Musardo, S., Vara, H., de la Fuente, A. G., Pelucchi, S., Marino, D. D., Borroni, B., Tramontano, A. L., Pérez‐Otaño, I., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci65401 · Cited by 117 · see citing works
Neuronal BIN1 Regulates Presynaptic Neurotransmitter Release and Memory Consolidation
Rossi, P. D., Nomura, T., Andrew, R. J., Masse, N. Y., Sampathkumar, V., Musial, T. F., Sudwarts, A., Recupero, A. J., Metayer, T. L., Hansen, M. T., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.026 · Cited by 117 · see citing works
Malinverno, M., Carta, M., Epis, R., Marcello, E. E., Verpelli, C., Cattabeni, F., Sala, C., Mulle, C., Luca, M. D., & Gardoni, F. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1984-10.2010 · Cited by 116 · see citing works
Synaptic neurexin-1 assembles into dynamically regulated active zone nanoclusters
Trotter, J. H., Hao, J., Maxeiner, S., Tsetsenis, T., Liu, Z., Zhuang, X., & Südhof, T. C. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201812076 · Cited by 112 · see citing works
Chen, F., Swartzlander, D. B., Ghosh, A., Fryer, J. D., Wang, B., & Zheng, H. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00426-7 · Cited by 99 · see citing works
Targeting Synaptic Dysfunction in Alzheimer’s Disease Therapy
Nisticò, R., Pignatelli, M., Piccinin, S., Mercuri, N. B., & Collingridge, G. L. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8324-3 · Cited by 97 · see citing works
EphA4 Activation of c-Abl Mediates Synaptic Loss and LTP Blockade Caused by Amyloid-β Oligomers
Vargas, L. M., Leal, N. R., Estrada, L. D., González, A., Serrano, F. G., Araya, K. A., Gysling, K., Inestrosa, N. C., Pasquale, E. B., & Alvarez, A. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092309 · Cited by 85 · see citing works
Seabold, G. K., Burette, A., Lim, I. A., Weinberg, R. J., & Hell, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212825200 · Cited by 83 · see citing works
Furin is an endogenous regulator of α-secretase associated APP processing
Hwang, E. M., Kim, S. K., Sohn, J.-H., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.077 · Cited by 82 · see citing works
Sheng, L., Chen, M., Cai, K., Song, Y., Yu, D., Zhang, H., & Xu, G. (2019) · The FASEB Journal · doi:10.1096/fj.201900527r · Cited by 81 · see citing works
PirB regulates a structural substrate for cortical plasticity.
Djurisic, M., Vidal, G. S., Mann, M., Aharon, A., Kim, T., Ferrao Santos, A., Zuo, Y., Hübener, M., & Shatz, C. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321092110 · Cited by 79 · see citing works
Alzheimer's Disease Risk Factor Pyk2 Mediates Amyloid-β-Induced Synaptic Dysfunction and Loss
Salazar, S. V., Cox, T. O., Lee, S., Brody, A. H., Chyung, A. S., Haas, L. T., & Strittmatter, S. M. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.1873-18.2018 · Cited by 77 · see citing works
Schürmann, B., Bermingham, D. P., Kopeikina, K. J., Myczek, K., Yoon, S., Horan, K. E., Kelly, C. J., Martin-de-Saavedra, M. D., Forrest, M. P., Fawcett-Patel, J. M., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0407-3 · Cited by 72 · see citing works
Lewandowski, C. T., Maldonado Weng, J., & LaDu, M. J. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104811 · Cited by 72 · see citing works
Pasciuto, E., Ahmed, T., Wahle, T., Gardoni, F., D’Andrea, L., Pacini, L., Jacquemont, S., Tassone, F., Balschun, D., Dotti, C. G., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.06.032 · Cited by 71 · see citing works
Ren, S., Yao, W., Tambini, M. D., Yin, T., Norris, K. A., & D'Adamio, L. (2020) · eLife · doi:10.7554/elife.57513 · Cited by 68 · see citing works
Johnson, R. I., Seppa, M. J., & Cagan, R. L. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200706108 · Cited by 67 · see citing works
SorLA Controls Neurotrophic Activity by Sorting of GDNF and Its Receptors GFRα1 and RET
Glerup, S., Lume, M., Olsen, D., Nyengaard, J. R., Vægter, C. B., Gustafsen, C., Christensen, E., Kjølby, M., Hay‐Schmidt, A., Bender, D., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2012.12.011 · Cited by 67 · see citing works
Alzheimer’s disease risk gene BIN1 induces Tau-dependent network hyperexcitability
Voskobiynyk, Y., Roth, J. R., Cochran, J. N., Rush, T., Carullo, N. V. N., Mesina, J. S., Waqas, M., Vollmer, R. M., Day, J. J., McMahon, L. L., et al. (2020) · eLife · doi:10.7554/elife.57354 · Cited by 66 · see citing works
Sorting receptor SORLA: cellular mechanisms and implications for disease
Schmidt, V., Subkhangulova, A., & Willnow, T. E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2410-z · Cited by 65 · see citing works
The role of CD2AP in the Pathogenesis of Alzheimer's Disease
Tao, Q.-Q., Chen, Y.-C., & Wu, Z.-Y. (2019) · Aging and disease · doi:10.14336/ad.2018.1025 · Cited by 61 · see citing works
The Non-receptor Tyrosine Kinase Pyk2 in Brain Function and Neurological and Psychiatric Diseases
de Pins, B., Mendes, T., Giralt, A., & Girault, J. (2021) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2021.749001 · Cited by 59 · see citing works
Proline-Rich Tyrosine Kinase 2 Regulates Hippocampal Long-Term Depression
Hsin, H., Kim, M. J., Wang, C.-F., & Sheng, M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1029-10.2010 · Cited by 55 · see citing works
<scp>APOE</scp> genotype affects the pre‐synaptic compartment of glutamatergic nerve terminals
Dumanis, S. B., DiBattista, A. M., Miessau, M., Moussa, C. E. H., & Rebeck, G. W. (2013) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07908.x · Cited by 55 · see citing works
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 · see citing works
Jiang, Y., Zhou, X., Wong, H. Y., Ouyang, L., Ip, F. C. F., Chau, V. M. N., Lau, S., Wu, W., Wong, D. Y. K., Seo, H., et al. (2022) · Nature Aging · doi:10.1038/s43587-022-00241-9 · Cited by 53 · see citing works
Self-citationVPS10P Domain Receptors: Sorting Out Brain Health and Disease
Malik, A. R., & Willnow, T. E. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.08.003 · Cited by 52 · see citing works
The Alzheimer's disease risk factor CD2AP maintains blood–brain barrier integrity
Cochran, J. N., Rush, T., Buckingham, S. C., & Roberson, E. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv371 · Cited by 50 · see citing works
SORLA attenuates EphA4 signaling and amyloid β–induced neurodegeneration
Huang, T. Y., Zhao, Y., Jiang, L.-L., Li, X., Liu, Y., Sun, Y., Piña-Crespo, J. C., Zhu, B., Masliah, E., Willnow, T. E., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20171413 · Cited by 50 · see citing works
The Role of APP in Structural Spine Plasticity
Montagna, E., Dorostkar, M. M., & Herms, J. W. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00136 · Cited by 49 · see citing works
Ren, S., Breuillaud, L., Yao, W., Yin, T., Norris, K. A., Zehntner, S. P., & D’Adamio, L. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.016395 · Cited by 47 · see citing works
The Role of Interleukin-33 in Patients with Mild Cognitive Impairment and Alzheimer's Disease
Liang, C., Su, K., Tsai, C., Lee, J., Chu, C., Yeh, T., Su, M., Lin, G., Lin, Y., Chu, H., et al. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00652-z · Cited by 46 · see citing works
Ojelade, S. A., Lee, T. V., Giagtzoglou, N., Yu, L., Ugur, B., Li, Y., Duraine, L., Zuo, Z., Petyuk, V., De Jager, P. L., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.041 · Cited by 42 · see citing works
TspanC8 tetraspanins differentially regulate ADAM10 endocytosis and half-life
Eschenbrenner, E., Jouannet, S., Clay, D., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900444 · Cited by 42 · see citing works
The Adaptor Protein CD2AP Is a Coordinator of Neurotrophin Signaling-Mediated Axon Arbor Plasticity
Harrison, B. J., Venkat, G., Lamb, J. L., Hutson, T. H., Drury, C., Rau, K. K., Bunge, M. B., Mendell, L. M., Gage, F. H., Johnson, R. D., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2423-15.2016 · Cited by 40 · see citing works
SORLA-Mediated Trafficking of TrkB Enhances the Response of Neurons to BDNF
Rohe, M., Hartl, D., Fjorback, A. N., Klose, J., & Willnow, T. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072164 · Cited by 39 · see citing works
Shi, L., Du, X., Zhou, H., Tao, C.-L., Liu, Y.-T., Meng, F., Wu, G., Xiong, Y., Xia, C., Wang, Y., et al. (2014) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145714000601 · Cited by 38 · see citing works
Reduction of AP180 and CALM Produces Defects in Synaptic Vesicle Size and Density
Petralia, R. S., Wang, Y., Indig, F. E., Bushlin, I., Wu, F., Mattson, M. P., & Yao, P. J. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8194-x · Cited by 37 · see citing works
The chaperone Clusterin in neurodegeneration−friend or foe?
Yuste‐Checa, P., Bracher, A., & Hartl, F. U. (2022) · BioEssays · doi:10.1002/bies.202100287 · Cited by 36 · see citing works
Sweet, R. A., MacDonald, M. L., Kirkwood, C. M., Ding, Y., Schempf, T. A., Jones-Laughner, J., Kofler, J., Ikonomović, M. D., López, O. L., Garver, M. E., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.056580 · Cited by 35 · see citing works
Activity-dependent modulation of hippocampal synaptic plasticity via PirB and endocannabinoids
Djurisic, M. R., Brott, B. K., Saw, N. L., Shamloo, M., & Shatz, C. J. (2018) · Molecular Psychiatry · doi:10.1038/s41380-018-0034-4 · Cited by 33 · see citing works
Ramakrishna, S., Jhaveri, V., Konings, S. C., Nawalpuri, B., Chakraborty, S., Holst, B., Schmid, B., Gouras, G. K., Freude, K., & Muddashetty, R. S. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0435-21.2021 · Cited by 33 · see citing works
ADAM10 Site-Dependent Biology: Keeping Control of a Pervasive Protease
Tosetti, F., Alessio, M., Poggi, A. D., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094969 · Cited by 32 · see citing works
Zhao, C., Du, C., Yan, P., Xu, Z., Sun, C., Liu, Y. U., & Hou, X. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8796-4 · Cited by 31 · see citing works
Cell-Autonomous Regulation of Dendritic Spine Density by PirB
Vidal, G. S., Djurisic, M. R., Brown, K., Sapp, R. W., & Shatz, C. J. (2016) · eNeuro · doi:10.1523/eneuro.0089-16.2016 · Cited by 31 · see citing works
Qiao, F., Gao, X., Li, Y., Cai, H.-Y., & Qi, J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140375 · Cited by 27 · see citing works
Characterization of a Novel DWD Protein that Participates in Heat Stress Response in Arabidopsis
Kim, S.-H., Lee, J.-H., Seo, K.-I., Ryu, B., Sung, Y., Chung, T., Deng, X. W., & Lee, J. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.0224 · Cited by 27 · see citing works
Yan, Y., Zhao, A., Qui, Y., Li, Y., Yan, R., Wang, Y., Xu, W. L., & Deng, Y. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00016 · Cited by 25 · see citing works
Zhou, X., Fu, A. K. Y., & Ip, N. Y. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.02.001 · Cited by 22 · see citing works
Self-citationPyk2 in dorsal hippocampus plays a selective role in spatial memory and synaptic plasticity
Mastrolia, V., Al–Massadi, O., de Pins, B., & Girault, J. (2021) · Scientific Reports · doi:10.1038/s41598-021-95813-x · Cited by 18 · see citing works
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 16 · see citing works
Zeng, F., Liu, J., He, H. J., Gao, X., Liao, M., Yu, X., Liu, Y., Zhu, S., & Jing, C. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190805165607 · Cited by 12 · see citing works
Nishizaki, T. (2017) · Neural Plasticity · doi:10.1155/2017/2531453 · Cited by 7 · see citing works
Effect of APOE Genotype on Synaptic Proteins in Earlier Adult Life
Sinclair, L. I., & Love, S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170316 · Cited by 4 · see citing works
Identification of two pathogenic mutations in SORL1 in early-onset Alzheimer’s disease
Qiu, G., Zhu, F., & Xu, C. (2021) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2021.05.020 · Cited by 3 · see citing works
The Alzheimer risk factor CD2AP causes dysfunction of the brain vascular networkPreprint
Vandal, M., Institóris, Á., Korin, B., Gunn, C., Lee, S., Lee, J. Y., Bourassa, P., Mishra, R. C., Peringod, G., Jiang, Y., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.10.419598 · Cited by 2 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- T. Kim, G.S. Vidal, M. Djurisic, C.M. William, M.E. Birnbaum, K.C. Garcia, B. T. Hyman, C.J. Shatz, Human LilrB2 is a β-amyloid receptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's model, Science 341 (80) (2013) 1399-1404, https://doi.org/10.1126/science.1242077. · DOI · Paper page
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Sorted by citations
Kong, F., Wu, T., Dai, J., Zhai, Z., Cai, J., Zhu, Z., Xu, Y., & Sun, T. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1205207 · Cited by 54 · see citing works
Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease
Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56 · see citing works
- Authors
- Fu, W.-Y., & Ip, N. Y.
- Affiliations
- Hong Kong University of Science and Technology (HK)
- Corresponding author
- Ip, Nancy Y.
- ORCID
- Ip, Nancy Y.
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2023-04
- Volume
- 139
- Pages
- 3-12
- ISSN
- 1084-9521 (ISSN-L)
- OpenAlex
- W4288906001
- Cited by
- 48
- References
- 122
- Citations by year
- 2026: 3 · 2025: 15 · 2024: 21 · 2023: 7 · 2022: 2
- FWCI
- 1.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Seminars in Cell and Developmental Biology (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- University Grants Committee (T13-605/18-W, AoE/M-604/16)
- Innovation and Technology Commission (ITC PD/17-9)
- Hong Kong University of Science and Technology (ITCPD/17-9)
- Shenzhen Knowledge Innovation Program (JCYJ20180507183642005, 2018YFE0203600, 2018B030336001, JCYJ20170413173717055)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- Alzheimer's disease, synaptic dysfunction, genetic risk factors, synaptogenesis, synapses, cognitive decline, neurodegeneration, early pathological changes, pathogenesis
- MeSH terms
- Alzheimer Disease, Cognition Disorders, Humans, Risk Factors, Synapses, Neurodegenerative Diseases
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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.
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