Analyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities
Open accessAbstract
Synaptic failure is an immediate cause of cognitive decline and memory dysfunction in Alzheimer's disease. Dendritic spines are specialized structures on neuronal processes, on which excitatory synaptic contacts take place and the loss of dendritic spines directly correlates with the loss of synaptic function. Dendritic spines are readily accessible for both in vitro and in vivo experiments and have, therefore, been studied in great detail in Alzheimer's disease mouse models. To date, a large number of different mechanisms have been proposed to cause dendritic spine dysfunction and loss in Alzheimer's disease. For instance, amyloid beta fibrils, diffusible oligomers or the intracellular accumulation of amyloid beta have been found to alter the function and structure of dendritic spines by distinct mechanisms. Furthermore, tau hyperphosphorylation and microglia activation, which are thought to be consequences of amyloidosis in Alzheimer's disease, may also contribute to spine loss. Lastly, genetic and therapeutic interventions employed to model the disease and elucidate its pathogenetic mechanisms in experimental animals may cause alterations of dendritic spines on their own. However, to date none of these mechanisms have been translated into successful therapeutic approaches for the human disease. Here, we critically review the most intensely studied mechanisms of spine loss in Alzheimer's disease as well as the possible pitfalls inherent in the animal models of such a complex neurodegenerative disorder.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Healthy turnover of dendritic spines depends on cytoskeletal proteins.
“Dendritic spines serve as docking points for presynaptic axons, and healthy turnover of dendritic spines depends on cytoskeletal proteins [113].”
From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [113]
Loss of dendritic spines is a characteristic of the brains of AD patients, indicative of synaptic failure and a loss of robust neural networking.
“The loss of dendritic spines is a characteristic of the brains of AD patients, indicative of synaptic failure and a loss of robust neural networking [113].”
From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [113]
Dendritic spines serve as docking points for presynaptic axons.
“Dendritic spines serve as docking points for presynaptic axons, and healthy turnover of dendritic spines depends on cytoskeletal proteins [113].”
From Rlip76: An Unexplored Player in Neurodegeneration and Alzheimer’s Disease? (2022) · cites this paper as [113]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · see citing works
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397 · see citing works
Synaptic Pruning by Microglia Is Necessary for Normal Brain Development
Paolicelli, R. C., Bolasco, G., Pagani, F., Maggi, L., Scianni, M., Panzanelli, P., Giustetto, M., Ferreira, T. A., Guiducci, E., Dumas, L., et al. (2011) · Science · doi:10.1126/science.1202529 · Cited by 4,244 · see citing works
Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530 · see citing works
Phases of Aβ-deposition in the human brain and its relevance for the development of AD
Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490 · see citing works
Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172 · see citing works
Microglia promote learning-dependent synapse formation through brain-derived neurotrophic factor
Parkhurst, C. N., Yang, G., Ninan, I., Savas, J. N., Yates, J. R., Lafaille, J. J., Hempstead, B. L., Littman, D. R., & Gan, W.-B. (2013) · Cell · doi:10.1016/j.cell.2013.11.030 · Cited by 2,599 · see citing works
AMPA Receptor Trafficking and Synaptic Plasticity
Malinow, R., & Malenka, R. C. (2002) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.25.112701.142758 · Cited by 2,588 · 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
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works
Stages of the Pathologic Process in Alzheimer Disease: Age Categories From 1 to 100 Years
Braak, H., Thal, D. R., Ghebremedhin, E., & Del Tredici, K. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e318232a379 · Cited by 2,194 · see citing works
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962 · see citing works
Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892 · see citing works
Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644 · see citing works
Microglial interactions with synapses are modulated by visual experience
Tremblay, M.-È., Lowery, R. L., & Majewska, A. K. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000527 · Cited by 1,542 · see citing works
Dendritic spine pathology in neuropsychiatric disorders
Penzes, P., Cahill, M. E., Jones, K. A., VanLeeuwen, J.-E., & Woolfrey, K. M. (2011) · Nature Neuroscience · doi:10.1038/nn.2741 · Cited by 1,523 · see citing works
Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology
Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507 · see citing works
Uber eine eigenartige Erkrankung der Hirnrinde
Alzheimer, A. (1907) · Medical Entomology and Zoology · Cited by 1,503 · see citing works
Single App knock-in mouse models of Alzheimer’s disease
Saito, T., Matsuba, Y., Mihira, N., Takano, J., Nilsson, P., Itohara, S., Iwata, N., & Saido, T. C. (2014) · Nature Neuroscience · doi:10.1038/nn.3697 · Cited by 1,447 · see citing works
Propagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works
Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type
Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,380 · see citing works
Synaptic Activity Regulates Interstitial Fluid Amyloid-β Levels In Vivo
Cirrito, J. R., Yamada, K. A., Finn, M. B., Sloviter, R. S., Bales, K. R., May, P. C., Schoepp, D. D., Paul, S. M., Mennerick, S., & Holtzman, D. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.10.028 · Cited by 1,265 · see citing works
Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance
Castellano, J. M., Kim, J., Stewart, F. R., Jiang, H., DeMattos, R. B., Patterson, B. W., Fagan, A. M., Morris, J. C., Mawuenyega, K. G., Cruchaga, C., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002156 · Cited by 1,227 · see citing works
A Phase 3 Trial of Semagacestat for Treatment of Alzheimer's Disease
Doody, R. S., Raman, R., Farlow, M., Iwatsubo, T., Vellas, B., Joffe, S., Kieburtz, K., He, F., Sun, X., Thomas, R. G., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1210951 · Cited by 1,224 · see citing works
Structure and function of dendritic spines
Nimchinsky, E. A., Sabatini, B. L., & Svoboda, K. (2002) · Annual Review of Physiology · doi:10.1146/annurev.physiol.64.081501.160008 · Cited by 1,208 · see citing works
Rapid formation and selective stabilization of synapses for enduring motor memories
Xu, T., Yu, X., Perlik, A. J., Tobin, W. F., Zweig, J. A., Tennant, K., Jones, T., & Zuo, Y. (2009) · Nature · doi:10.1038/nature08389 · Cited by 1,193 · see citing works
Stably maintained dendritic spines are associated with lifelong memories
Yang, G., Pan, F., & Gan, W.-B. (2009) · Nature · doi:10.1038/nature08577 · Cited by 1,182 · see citing works
Clusters of Hyperactive Neurons Near Amyloid Plaques in a Mouse Model of Alzheimer’s Disease
Busche, M. A., Eichhoff, G., Adelsberger, H., Abramowski, D., Wiederhold, K.-H., Haass, C., Staufenbiel, M., Konnerth, A., & Garaschuk, O. (2008) · Science · doi:10.1126/science.1162844 · Cited by 1,125 · see citing works
Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works
Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer’s disease
Giannakopoulos, P., Herrmann, F. R., Bussière, T., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Gold, G., & Hof, P. R. (2003) · Neurology · doi:10.1212/01.wnl.0000063311.58879.01 · Cited by 1,118 · see citing works
Sperling, R. A., LaViolette, P. S., O'Keefe, K., O'Brien, J., Rentz, D. M., Pihlajamaki, M., Marshall, G., Hyman, B. T., Selkoe, D. J., Hedden, T., et al. (2009) · Neuron · doi:10.1016/j.neuron.2009.07.003 · Cited by 1,027 · see citing works
Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment
Scheff, S. W., Price, D. A., Schmitt, F. A., & Mufson, E. J. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.012 · Cited by 1,017 · see citing works
Trans-Synaptic Spread of Tau Pathology In Vivo
Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994 · see citing works
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991 · see citing works
Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works
Aβ42‐driven cerebral amyloidosis in transgenic mice reveals early and robust pathology
Radde, R., Bolmont, T., Kaeser, S. A., Coomaraswamy, J., Lindau, D., Stoltze, L., Calhoun, M. E., Jäggi, F., Wolburg, H., Gengler, S., et al. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400784 · Cited by 986 · see citing works
Chishti, M. A., Yang, D.-S., Janus, C., Phinney, A. L., Horne, P., Pearson, J., Strome, R., Zuker, N., Loukides, J., French, J., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100710200 · Cited by 955 · see citing works
Koffie, R. M., Meyer-Luehmann, M., Hashimoto, T., Adams, K. W., Mielke, M. L., Garcia-Alloza, M., Micheva, K. D., Smith, S. J., Kim, M. L., Lee, V. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811698106 · Cited by 850 · see citing works
The Genetics of Alzheimer Disease: Back to the Future
Bertram, L., Lill, C. M., & Tanzi, R. E. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.013 · Cited by 834 · see citing works
Synaptic alterations in CA1 in mild Alzheimer disease and mild cognitive impairment
Scheff, S. W., Price, D. A., Schmitt, F. A., DeKosky, S. T., & Mufson, E. J. (2007) · Neurology · doi:10.1212/01.wnl.0000260698.46517.8f · Cited by 824 · see citing works
Dendritic Spine Pathology: Cause or Consequence of Neurological Disorders?
Fiala, J. C., Spacek, J., & Harris, K. M. (2002) · Brain Research Reviews · doi:10.1016/s0165-0173(02)00158-3 · Cited by 811 · see citing works
Experience-dependent plasticity of dendritic spines in the developing rat barrel cortex in vivo
Lendvai, B., Stern, E. A., Chen, B., & Svoboda, K. (2000) · Nature · doi:10.1038/35009107 · Cited by 802 · see citing works
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783 · see citing works
Src kinases: a hub for NMDA receptor regulation
Salter, M. W., & Kalia, L. V. (2004) · Nature reviews. Neuroscience · doi:10.1038/nrn1368 · Cited by 777 · see citing works
Brain homogenates from human tauopathies induce tau inclusions in mouse brain
Clavaguera, F., Akatsu, H., Fraser, G. M., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 750 · see citing works
Postsynaptic signaling and plasticity mechanisms
Sheng, M., & Kim, M. J. (2002) · Science · doi:10.1126/science.1075333 · Cited by 731 · see citing works
Busche, M. A., Chen, X., Henning, H. A., Reichwald, J., Staufenbiel, M., Sakmann, B., & Konnerth, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206171109 · Cited by 715 · see citing works
Takahashi, R. H., Milner, T. A., Li, F., Nam, E. E., Edgar, M. A., Yamaguchi, H., Beal, M. F., Xu, H., Greengard, P., & Gouras, G. K. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64463-x · Cited by 706 · see citing works
Tu, H., Nelson, O. L., Bezprozvanny, A., Wang, Z., Lee, S.-F., Hao, Y.-H., Serneels, L., Strooper, B. D., Yu, G., & Борисович, Б. И. (2006) · Cell · doi:10.1016/j.cell.2006.06.059 · Cited by 691 · see citing works
LTP Inhibits LTD in the Hippocampus via Regulation of GSK3β
Peineau, S., Taghibiglou, C., Bradley, C. A., Wong, T. P., Liu, L., Lu, J., Lo, E., Wu, D., Saule, E., Bouschet, T., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.029 · Cited by 690 · see citing works
Berg, L., McKeel, D. W., Miller, J. P., Storandt, M., Rubin, E. H., Morris, J. C., Baty, J., Coats, M., Norton, J., Goate, A. M., et al. (1998) · Archives of Neurology · doi:10.1001/archneur.55.3.326 · Cited by 657 · see citing works
Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons
Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A. O., Wısnıewskı, T., Gunther, E. C., & Strittmatter, S. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3178 · Cited by 654 · see citing works
Roberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4152-10.2011 · Cited by 654 · see citing works
Regulation of Tau Pathology by the Microglial Fractalkine Receptor
Bhaskar, K., Konerth, M., Kokiko-Cochran, O. N., Cardona, A., Ransohoff, R. M., & Lamb, B. T. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.023 · Cited by 639 · see citing works
Sanchez, P. E., Zhu, L., Verret, L., Vossel, K. A., Orr, A. G., Cirrito, J. R., Devidze, N., Ho, K., Yu, G.-Q., Palop, J. J., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121081109 · Cited by 638 · see citing works
Dendritic Spine Structural Anomalies in Fragile-X Mental Retardation Syndrome
Irwin, S. A. (2000) · Cerebral Cortex · doi:10.1093/cercor/10.10.1038 · Cited by 626 · see citing works
Microglial activation by Alzheimer amyloid precursor protein and modulation by apolipoprotein E
Barger, S. W., & Harmon, A. D. (1997) · Nature · doi:10.1038/42257 · Cited by 622 · see citing works
Kuchibhotla, K. V., Goldman, S. T., Lattarulo, C. R., Wu, H.-Y., Hyman, B. T., & Bacskai, B. J. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.008 · Cited by 614 · see citing works
Functional Alterations in Memory Networks in Early Alzheimer’s Disease
Sperling, R. A., Dickerson, B. C., Pihlajamaki, M. M., Vannini, P., LaViolette, P. S., Vitolo, O. V., Hedden, T., Becker, J. A., Rentz, D. M., Selkoe, D. J., et al. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8109-7 · Cited by 587 · see citing works
Um, J. W., Kaufman, A. C., Kostylev, M., Heiss, J. K., Stagi, M., Takahashi, H., Kerrisk, M. E., Vortmeyer, A., Wisniewski, T., Koleske, A. J., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.036 · Cited by 572 · see citing works
Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer's disease
D'Amelio, M., Cavallucci, V., Middei, S., Marchetti, C., Pacioni, S., Ferri, A., Diamantini, A., De Zio, D., Carrara, P., Battistini, L., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2709 · Cited by 572 · see citing works
Synapse Formation and Function Is Modulated by the Amyloid Precursor Protein
Priller, C., Bauer, T., Mitteregger, G., Krebs, B., Kretzschmar, H. A., & Herms, J. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1450-06.2006 · Cited by 548 · see citing works
Self-citationLee, S., Varvel, N. H., Konerth, M. E., Xu, G., Cardona, A. E., Ransohoff, R. M., & Lamb, B. T. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.100265 · Cited by 539 · see citing works
Akt/GSK3 Signaling in the Action of Psychotropic Drugs
Beaulieu, J., Gainetdinov, R. R., & Caron, M. G. (2008) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.011008.145634 · Cited by 523 · see citing works
Caspase activation precedes and leads to tangles
de Calignon, A., Fox, L. M., Pitstick, R., Carlson, G. A., Bacskai, B. J., Spires-Jones, T. L., & Hyman, B. T. (2010) · Nature · doi:10.1038/nature08890 · Cited by 517 · see citing works
Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494 · see citing works
Occurrence of T cells in the brain of Alzheimer's disease and other neurological diseases
Togo, T., Akiyama, H., Iseki, E., Kondo, H., Ikeda, K., Kato, M., Oda, T., Tsuchiya, K., & Kosaka, K. (2002) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(01)00496-9 · Cited by 481 · see citing works
Deleterious Effects of Amyloid β Oligomers Acting as an Extracellular Scaffold for mGluR5
Renner, M., Lacor, P. N., Velasco, P. T., Xu, J., Contractor, A., Klein, W. L., & Triller, A. (2010) · Neuron · doi:10.1016/j.neuron.2010.04.029 · Cited by 468 · see citing works
Tai, H., Serrano‐Pozo, A., Hashimoto, T., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.06.033 · Cited by 456 · see citing works
Sorra, K. E., & Harris, K. M. (2000) · Hippocampus · doi:10.1002/1098-1063(2000)10:5 · Cited by 456 · see citing works
Cheung, K., Shineman, D. W., Müller, M., Cárdenas, C., Mei, L., Yang, J., Tomita, T., Iwatsubo, T., Lee, V. M. ‐., & Foskett, J. K. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.015 · Cited by 449 · see citing works
A Plaque-Specific Antibody Clears Existing β-amyloid Plaques in Alzheimer's Disease Mice
DeMattos, R. B., Lu, J., Tang, Y., Racke, M. M., DeLong, C. A., Tzaferis, J. A., Hole, J. T., Forster, B. M., McDonnell, P. C., Liu, F., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.10.029 · Cited by 442 · see citing works
Eimer, W. A., & Vassar, R. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-2 · Cited by 425 · see citing works
Chicurel, M. E., & Harris, K. M. (1992) · Journal of Comparative Neurology · doi:10.1002/cne.903250204 · Cited by 417 · see citing works
Regulation of F-Actin Stability in Dendritic Spines by Glutamate Receptors and Calcineurin
Halpain, S., Hipolito, A., & Saffer, L. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-23-09835.1998 · Cited by 408 · cited 1× · see citing works
“Pathological activation of NMDA receptors during excitotoxicity [78, 82] or disruption of dendritic transport both lead to spine loss and can be considered neuron-autonomous causes.”
BackgroundBrain amyloid-β oligomers in ageing and Alzheimer’s disease
Lesné, S., Sherman, M. A., Grant, M. K. O., Kuskowski, M. A., Schneider, J. A., Bennett, D. A., & Ashe, K. H. (2013) · Brain · doi:10.1093/brain/awt062 · Cited by 407 · see citing works
Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
Lashuel, H. A., & Lansbury, P. T. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004422 · Cited by 398 · see citing works
Tomiyama, T., Matsuyama, S., Iso, H., Umeda, T., Takuma, H., Ohnishi, K., Ishibashi, K., Teraoka, R., Sakama, N., Yamashita, T., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5825-09.2010 · Cited by 396 · see citing works
Falkenberg, T., Mohammed, A. K., Henriksson, B. G., Persson, H., Winblad, B. G., & Lindefors, N. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90494-r · Cited by 388 · see citing works
Masliah, E., Sisk, A., Mallory, M. E., Mucke, L., Schenk, D., & Games, D. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05795.1996 · Cited by 387 · see citing works
Altered brain functional connectivity and impaired short-term memory in Alzheimer's disease
Grady, C. L. (2001) · Brain · doi:10.1093/brain/124.4.739 · Cited by 367 · see citing works
Wu, H.-Y., Hudry, E., Hashimoto, T., Kuchibhotla, K., Rozkalne, A., Fan, Z., Spires-Jones, T., Xie, H., Arbel-Ornath, M., Grosskreutz, C. L., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4456-09.2010 · Cited by 367 · see citing works
Immunohistochemical quantification of the synapse-related protein synaptophysin in Alzheimer disease
Masliah, E., Terry, R. D., DeTeresa, R. M., & Hansen, L. A. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90582-x · Cited by 363 · see citing works
Soluble Aβ oligomer production and toxicity
Larson, M. E., & Lesné, S. E. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07478.x · Cited by 356 · see citing works
Centonze, D., Muzio, L., Rossi, S., Cavasinni, F., De Chiara, V., Bergami, A., Musella, A., D'Amelio, M., Cavallucci, V., Martorana, A., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.5804-08.2009 · Cited by 352 · see citing works
Absence of C1q Leads to Less Neuropathology in Transgenic Mouse Models of Alzheimer's Disease
Fonseca, M. I., Zhou, J., Botto, M., & Tenner, A. J. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.0901-04.2004 · Cited by 345 · see citing works
Truncated and modified amyloid-beta species
Kummer, M. P., & Heneka, M. T. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt258 · Cited by 338 · 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
Stutzmann, G. E., Smith, I. F., Caccamo, A., Oddo, S., LaFerla, F. M., & Parker, I. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0739-06.2006 · Cited by 327 · see citing works
Neuronal cytoskeletal changes are an early consequence of repetitive head injury
Geddes, J. F., Vowles, G. H., Nicoll, J. A. R., & Révész, T. (1999) · Acta Neuropathologica · doi:10.1007/s004010051066 · Cited by 323 · see citing works
Experience-dependent structural plasticity in the cortex
Fu, M., & Zuo, Y. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.02.001 · Cited by 322 · see citing works
Šišková, Z., Justus, D., Kaneko, H., Friedrichs, D., Henneberg, N., Beutel, T., Pitsch, J., Schoch, S., Becker, A., von der Kammer, H., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.024 · Cited by 320 · see citing works
Evironmental effects on cortical dendritic fields. I. Rearing in the dark.
Coleman, P. D., & Riesen, A. H. (1968) · PubMed · Cited by 315 · see citing works
Massive restructuring of neuronal circuits during functional reorganization of adult visual cortex
Keck, T., Mrsic-Flogel, T. D., Vaz Afonso, M., Eysel, U. T., Bonhoeffer, T., & Hübener, M. (2008) · Nature Neuroscience · doi:10.1038/nn.2181 · Cited by 315 · see citing works
Wright, A. L., Zinn, R., Hohensinn, B., Konen, L. M., Beynon, S. B., Tan, R. P., Clark, I. A., Abdipranoto, A., & Vissel, B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059586 · Cited by 310 · see citing works
Synaptic changes in Alzheimer’s disease and its models
Pozueta, J., Lefort, R., & Shelanski, M. L. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.050 · Cited by 305 · see citing works
Amyloid‐beta oligomerization in Alzheimer dementia versus high‐pathology controls
Esparza, T. J., Zhao, H., Cirrito, J. R., Cairns, N. J., Bateman, R. J., Holtzman, D. M., & Brody, D. L. (2012) · Annals of Neurology · doi:10.1002/ana.23748 · Cited by 304 · see citing works
Synaptic Loss in the Inferior Temporal Gyrus in Mild Cognitive Impairment and Alzheimer's Disease
Scheff, S. W., PRICE, D. A., Schmitt, F. A., Scheff, M. A., & Mufson, E. J. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101782 · Cited by 301 · see citing works
Synaptic structural abnormalities in the Ts65Dn mouse model of down syndrome
Belichenko, P. V., Masliah, E., Kleschevnikov, A. M., Villar, A. J., Epstein, C. J., Salehi, A., & Mobley, W. C. (2004) · Journal of Comparative Neurology · doi:10.1002/cne.20337 · Cited by 297 · see citing works
RAGE-mediated signaling contributes to intraneuronal transport of amyloid-β and neuronal dysfunction
Takuma, K., Fang, F., Zhang, W., Yan, S., Fukuzaki, E., Du, H., Sosunov, A., McKhann, G., Funatsu, Y., Nakamichi, N., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905686106 · Cited by 290 · see citing works
Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., & Mandelkow, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.207 · Cited by 283 · see citing works
Maezawa, I., Zimin, P. I., Wulff, H., & Jin, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135244 · Cited by 279 · see citing works
Liu, Z., Condello, C., Schain, A., Harb, R., & Grutzendler, J. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4403-10.2010 · Cited by 276 · see citing works
Sun, S., Zhang, H., Liu, J., Александровна, П. Е., Xu, N., Feske, S., White, C. L., & Борисович, Б. И. (2014) · Neuron · doi:10.1016/j.neuron.2014.02.019 · Cited by 273 · see citing works
Mondragón-Rodríguez, S., Trillaud-Doppia, E., Dudilot, A., Bourgeois, C., Lauzon, M., Leclerc, N., & Boehm, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.401240 · Cited by 272 · see citing works
Dujardin, S., Lécolle, K., Caillierez, R., Bégard, S., Zommer, N., Lachaud, C., Carrier, S., Dufour, N., Aurégan, G., Winderickx, J., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-14 · Cited by 259 · see citing works
The multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foes
Nhan, H. S., Chiang, K., & Koo, E. H. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1347-2 · Cited by 256 · see citing works
Intraneuronal Aβ42 accumulation in Down syndrome brain: Original Articles
Mori, C., Spooner, E. T., Wisniewski, K. E., Wisniewski, T. M., Yamaguchi, H., Saido, T. C., Tolan, D. R., Selkoe, D. J., & Lemere, C. A. (2002) · Amyloid · doi:10.3109/13506120208995241 · Cited by 255 · see citing works
Tong, L., Prieto, G. A., Kramár, E. A., Smith, E. D., Cribbs, D. H., Lynch, G., & Cotman, C. W. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1253-12.2012 · Cited by 254 · see citing works
On the Seeding and Oligomerization of pGlu-Amyloid Peptides (<i>in vitro</i>)
Schilling, S., Lauber, T., Schaupp, M., Manhart, S., Scheel, E., Böhm, G., & Demuth, H.-U. (2006) · Biochemistry · doi:10.1021/bi0612667 · Cited by 254 · see citing works
Magdesian, M. H., Carvalho, M., Mendes, F. A., Saraiva, L. M., Juliano, M. A., Juliano, L., Garcia-Abreu, J., & Ferreira, S. T. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707108200 · Cited by 251 · see citing works
Resenberger, U. K., Harmeier, A., Woerner, A. C., Goodman, J. L., Müller, V., Krishnan, R., Vabulas, R. M., Kretzschmar, H. A., Lindquist, S. L., Hartl, F. U., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.86 · Cited by 244 · see citing works
Local Pruning of Dendrites and Spines by Caspase-3-Dependent and Proteasome-Limited Mechanisms
Ertürk, A., Wang, Y., & Sheng, M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3121-13.2014 · Cited by 231 · see citing works
Down’s syndrome, neuroinflammation, and Alzheimer neuropathogenesis
Wilcock, D. M., & Griffin, W. S. T. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-84 · Cited by 230 · see citing works
Lanz, T. A., Carter, D. B., & Merchant, K. M. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00079-2 · Cited by 227 · see citing works
Presenilin-1 Knockin Mice Reveal Loss-of-Function Mechanism for Familial Alzheimer’s Disease
Xia, D., Watanabe, H., Wu, B., Lee, S. H., Li, Y., Tsvetkov, E., Bolshakov, V. Y., Shen, J., & Kelleher, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2015.02.010 · Cited by 226 · see citing works
Neurotoxic protein oligomers — what you see is not always what you get
Bitan, G., Fradinger, E. A., Spring, S. M., & Teplow, D. B. (2005) · Amyloid · doi:10.1080/13506120500106958 · Cited by 221 · see citing works
Ferguson, A. R., Christensen, R. N., Gensel, J. C., Miller, B. A., Sun, F., Beattie, E. C., Bresnahan, J. C., & Beattie, M. S. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.3708-08.2008 · Cited by 219 · see citing works
Bellucci, A., Westwood, A. J., Ingram, E., Casamenti, F., Goedert, M., & Spillantini, M. G. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63421-9 · Cited by 215 · see citing works
Neurofibrillary tangles in Niemann—Pick disease type C
Love, S., Bridges, L., & Case, C. P. (1995) · Brain · doi:10.1093/brain/118.1.119 · Cited by 211 · see citing works
Chakroborty, S., Goussakov, I. V., Miller, M. B., & Stutzmann, G. E. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2047-09.2009 · Cited by 209 · see citing works
Cheung, K., Mei, L., Mak, D. D., Hayashi, I., Iwatsubo, T., Kang, D. E., & Foskett, J. K. (2010) · Science Signaling · doi:10.1126/scisignal.2000818 · Cited by 208 · see citing works
Hasbani, M. J., Schlief, M. L., Fisher, D. A., & Goldberg, M. P. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-07-02393.2001 · Cited by 208 · see citing works
Bordji, K., Becerril-Ortega, J., Nicole, O., & Buisson, A. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3021-10.2010 · Cited by 195 · see citing works
Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo
Kuchibhotla, K. V., Wegmann, S., Kopeikina, K. J., Hawkes, J., Rudinskiy, N., Andermann, M. L., Spires-Jones, T. L., Bacskai, B. J., & Hyman, B. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318807111 · Cited by 193 · see citing works
Structural and functional changes in tau mutant mice neurons are not linked to the presence of NFTs
Rocher, A. B., Crimins, J. L., Amatrudo, J. M., Kinson, M. S., Todd-Brown, M. A., Lewis, J., & Luebke, J. I. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.07.029 · Cited by 187 · see citing works
Neurofibrillary tangles in Niemann-Pick disease type C
Suzuki, K., Parker, C. C., Pentchev, P. G., Katz, D., Ghetti, B. F., D’Agostino, A. N., & Carstea, E. D. (1995) · Acta Neuropathologica · doi:10.1007/bf00309338 · Cited by 186 · see citing works
Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model
Xie, H., Guan, J., Borrelli, L. A., Xu, J., Serrano-Pozo, A., & Bacskai, B. J. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1836-13.2013 · Cited by 185 · cited 1× · see citing works
“dynamics [38, 100] or mitochondrial integrity [216].”
Pathological Tau Disrupts Ongoing Network Activity
Menkes-Caspi, N., Yamin, H. G., Kellner, V., Spires-Jones, T. L., Cohen, D., & Stern, E. A. (2015) · Neuron · doi:10.1016/j.neuron.2015.01.025 · Cited by 184 · see citing works
Role of Presenilins in Neuronal Calcium Homeostasis
Zhang, H., Sun, S., Herreman, A., Strooper, B. D., & Борисович, Б. И. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1554-10.2010 · Cited by 181 · see citing works
Solution State Characterization of Amyloid β-Derived Diffusible Ligands
Hepler, R. W., Grimm, K. M., Nahas, D. D., Breese, R., Chen-Dodson, E., Acton, P. J., Keller, P. M., Yeager, M. D., Wang, H., Shughrue, P. J., et al. (2006) · Biochemistry · doi:10.1021/bi061850f · Cited by 181 · see citing works
Electrical compartmentalization in dendritic spines
Yuste, R. (2013) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-062111-150455 · Cited by 180 · see citing works
Severely dystrophic axons at amyloid plaques remain continuous and connected to viable cell bodies
Adalbert, R., Nogradi, A., Babetto, E., Janeckova, L., Walker, S. A., Kerschensteiner, M., Misgeld, T., & Coleman, M. P. (2009) · Brain · doi:10.1093/brain/awn312 · Cited by 177 · see citing works
Enhanced caffeine‐induced Ca2+release in the 3xTg‐AD mouse model of Alzheimer's disease
Smith, I. F., Hitt, B. D., Green, K. N., Oddo, S., & LaFerla, F. M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03332.x · Cited by 164 · see citing works
Synaptic Change in the Posterior Cingulate Gyrus in the Progression of Alzheimer's Disease
Scheff, S. W., PRICE, D. A., Ansari, M. A., Roberts, K. N., Schmitt, F. A., Ikonomović, M. D., & Mufson, E. J. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-141518 · Cited by 163 · see citing works
Leroy, K., Ando, K., Laporte, V., Dedecker, R., Suain, V., Authelet, M., Héraud, C., Pierrot, N., Yilmaz, Z., Octave, J.-N., et al. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.08.012 · Cited by 161 · see citing works
Neuronal driven pre-plaque inflammation in a transgenic rat model of Alzheimer's disease
Hanzel, C. E., Binette, A. P., Pimentel, L. S. B., Iulita, M. F., Allard, S. T. M., Ducatenzeiler, A., Carmo, S. D., & Cuello, A. C. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.026 · Cited by 159 · see citing works
Morawski, M., Brückner, G., Jäger, C., Seeger, G., Matthews, R. T., & Arendt, T. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00557.x · Cited by 157 · see citing works
Co-occurrence of Alzheimer's disease β-amyloid and tau pathologies at synapses
Takahashi, R. H., Capetillo-Zarate, E., Lin, M. T., Milner, T. A., & Gouras, G. K. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.07.021 · Cited by 150 · see citing works
Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Sengupta, U., Hernandez, C., Barrett, A. D. T., Dineley, K., & Kayed, R. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.4989-14.2015 · Cited by 149 · see citing works
Multiple events lead to dendritic spine loss in triple transgenic Alzheimer’s disease mice
Bittner, T., Fuhrmann, M., Burgold, S., Ochs, S. M., Hoffmann, N., Mitteregger, G., Kretzschmar, H., LaFerla, F. M., & Herms, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015477 · Cited by 149 · see citing works
Self-citationTai, H., Wang, B. Y., Serrano‐Pozo, A., Frosch, M. P., Spires‐Jones, T. L., & Hyman, B. T. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0146-2 · Cited by 142 · see citing works
Aggressive amyloidosis in mice expressing human amyloid peptides with the Arctic mutation
Cheng, I. H.-J., Palop, J. J., Esposito, L., Bien‐Ly, N., Yan, F., & Mucke, L. (2004) · Nature Medicine · doi:10.1038/nm1123 · Cited by 138 · see citing works
Diminished perisomatic GABAergic terminals on cortical neurons adjacent to amyloid plaques
Garcia-Marin, V. (2009) · Frontiers in Neuroanatomy · doi:10.3389/neuro.05.028.2009 · Cited by 136 · see citing works
Harris, J. A., Koyama, A., Maeda, S., Ho, K., Devidze, N., Dubal, D. B., Yu, G.-Q., Masliah, E., & Mucke, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045881 · Cited by 135 · see citing works
Merino-Serrais, P., Benavides-Piccione, R., Blazquez-Llorca, L., Kastanauskaite, A., Rábano, A., Avila, J., & DeFelipe, J. (2013) · Brain · doi:10.1093/brain/awt088 · Cited by 134 · see citing works
Schneider, I., Reversé, D., Dewachter, I., Ris, L., Caluwaerts, N., Kuipéri, C., Gilis, M., Geerts, H., Kretzschmar, H. A., Godaux, E., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010977200 · Cited by 134 · see citing works
Self-citationLeonoudakis, D., Zhao, P., & Beattie, E. C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5159-07.2008 · Cited by 131 · see citing works
Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131 · see citing works
Changes in the dendritic organization of neurons in the cerebral cortex following deafferentation.
Wh, J., & Db, T. (1962) · PubMed · Cited by 128 · see citing works
Tampellini, D., Rahman, N., Gallo, E. F., Huang, Z., Dumont, M., Capetillo-Zarate, E., Ma, T., Zheng, R., Lu, B., Nanus, D. M., et al. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2292-09.2009 · Cited by 127 · see citing works
Bittner, T., Fuhrmann, M., Burgold, S., Jung, C. K. E., Volbracht, C., Steiner, H., Mitteregger, G., Kretzschmar, H. A., Haass, C., & Herms, J. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2288-09.2009 · Cited by 123 · see citing works
Self-citationMultiple sclerosis and Alzheimer's disease
Dal Bianco, A., Bradl, M., Frischer, J., Kutzelnigg, A., Jellinger, K., & Lassmann, H. (2008) · Annals of Neurology · doi:10.1002/ana.21240 · Cited by 123 · see citing works
Some observations on transneuronal cell degeneration in the olfactory bulb of the rabbit.
Matthews, M. R., & Powell, T. P. S. (1962) · PubMed · Cited by 122 · see citing works
Polydoro, M., Dzhala, V. I., Pooler, A. M., Nicholls, S. B., McKinney, A. P., Sanchez, L., Pitstick, R., Carlson, G. A., Staley, K. J., Spires-Jones, T. L., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1215-5 · Cited by 117 · see citing works
Walsh, D. M., Hartley, D. M., Condron, M. M., Selkoe, D. J., & Teplow, D. B. (2001) · Biochemical Journal · doi:10.1042/bj3550869 · Cited by 114 · see citing works
Parent, A., Linden, D. J., Sisodia, S. S., & Borchelt, D. (1999) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0207 · Cited by 114 · see citing works
Kendziorra, K., Wolf, H., Meyer, P., Barthel, H., Hesse, S., Becker, G., Luthardt, J., Schildan, A., Patt, M., Sorger, D., et al. (2010) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-010-1644-5 · Cited by 111 · see citing works
Kumar‐Singh, S., Dewachter, I., Moechars, D., Lübke, U., Jonghe, C. D., Ceuterick, C., Checler, F., Naidu, A., Cordell, B., Cras, P. P., et al. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0272 · Cited by 105 · see citing works
Jung, C. K. E., & Herms, J. W. (2012) · Cerebral Cortex · doi:10.1093/cercor/bhs317 · Cited by 105 · see citing works
Self-citationActin filaments and microtubules in dendritic spines
Shirao, T., & González-Billault, C. E. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12313 · Cited by 103 · see citing works
Caspase-2 is required for dendritic spine and behavioural alterations in J20 APP transgenic mice
Pozueta, J., Lefort, R., Ribé, E. M., Troy, C. M., Arancio, O., & Shelanski, M. L. (2013) · Nature Communications · doi:10.1038/ncomms2927 · Cited by 100 · see citing works
Villar, A. J., Belichenko, P. V., Gillespie, A. M., Kozy, H. M., Mobley, W. C., & Epstein, C. J. (2005) · Mammalian Genome · doi:10.1007/s00335-004-2428-7 · Cited by 96 · see citing works
Wang, D., Govindaiah, G., Liu, R., Arcangelis, V. D., Cox, C. L., & Xiang, Y. K. (2010) · The FASEB Journal · doi:10.1096/fj.10-156661 · Cited by 95 · see citing works
Amyloid plaque formation precedes dendritic spine loss
Bittner, T., Burgold, S., Dorostkar, M. M., Fuhrmann, M., Wegenast‐Braun, B. M., Schmidt, B., Kretzschmar, H. A., & Herms, J. W. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1047-8 · Cited by 94 · see citing works
Self-citationDickstein, D. L., Brautigam, H., Stockton, S. D., Schmeidler, J., & Hof, P. R. (2010) · Brain Structure and Function · doi:10.1007/s00429-010-0245-1 · Cited by 94 · see citing works
Dewachter, I., Ris, L., Jaworski, T., Seymour, C. M., Kremer, A., Borghgraef, P., Vijver, H. D., Godaux, E., & LEUVEN, F. V. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.04.003 · Cited by 94 · see citing works
Aβ alters the connectivity of olfactory neurons in the absence of amyloid plaques in vivo
Cao, L., Schrank, B. R., Rodriguez, S., Benz, E. G., Moulia, T. W., Rickenbacher, G. T., Gomez, A. C., Levites, Y., Edwards, S. R., Golde, T. E., et al. (2012) · Nature Communications · doi:10.1038/ncomms2013 · Cited by 93 · see citing works
McGeer, P. L., Akiyama, H., Kawamata, T., Yamada, T., Walker, D. G., & Ishii, T. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310305 · Cited by 90 · see citing works
Zempel, H., & Mandelkow, E. (2011) · Neurodegenerative Diseases · doi:10.1159/000332816 · Cited by 90 · see citing works
The complexities of the pathology–pathogenesis relationship in Alzheimer disease
Castellani, R. J., & Perry, G. L. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.009 · Cited by 89 · see citing works
Mutant huntingtin alters Tau phosphorylation and subcellular distribution
Blum, D. L., Herrera, F., Francelle, L., Mendes, T., Basquin, M., Obriot, H., Demeyer, D., Sergeant, N., Gerhardt, E., Brouillet, E., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu421 · Cited by 87 · see citing works
Ochs, S. M., Dorostkar, M. M., Aramuni, G., Schön, C., Filser, S., Pöschl, J., Kremer, A., Leuven, F. V., Ovsepian, S. V., & Herms, J. W. (2014) · Molecular Psychiatry · doi:10.1038/mp.2014.55 · Cited by 86 · see citing works
Self-citationRichardson, J. C., Kendal, C., Anderson, R., Priest, F., Gower, E., Soden, P. E., Gray, R., Topps, S., Howlett, D. R., Lavender, D., et al. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00389-0 · Cited by 85 · see citing works
Akram, A., Christoffel, D. J., Rocher, A. B., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Herrmann, F. R., Haroutunian, V. H., Giannakopoulos, P., et al. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.03.007 · Cited by 84 · see citing works
Early intraneuronal Aβ deposition in the hippocampus of APP transgenic mice
Shie, F., LeBoeur, R. C., & Jin, L. (2003) · Neuroreport · doi:10.1097/00001756-200301200-00023 · Cited by 83 · see citing works
Intraneuronal amyloid β accumulation and oxidative damage to nucleic acids in Alzheimer disease
Nunomura, A., Tamaoki, T., Tanaka, K., Motohashi, N., Nakamura, M., Hayashi, T., Yamaguchi, H., Shimohama, S., Lee, H., Zhu, X., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.12.012 · Cited by 80 · see citing works
Umeda, T., Tomiyama, T., Kitajima, E., Idomoto, T., Nomura, S., Lambert, M. P., Klein, W. L., & Mori, H. (2012) · Life Sciences · doi:10.1016/j.lfs.2011.12.022 · Cited by 78 · see citing works
Fowler, S., Chiang, A. C. A., Savjani, R. R., Larson, M., Sherman, M. A., Schuler, D. R., Cirrito, J. R., Lesné, S., & Jankowsky, J. L. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0572-14.2014 · Cited by 77 · see citing works
Burnouf, S., Martire, A., Derisbourg, M. J., Laurent, C., Bélarbi, K., Leboucher, A., Fernández-Gómez, F.-J., Troquier, L., Eddarkaoui, S., Grosjean, M., et al. (2012) · Aging Cell · doi:10.1111/acel.12018 · Cited by 77 · see citing works
Functional Phenotype in Transgenic Mice Expressing Mutant Human Presenilin-1
Barrow, P. A., Empson, R. M., Gladwell, S. J., Anderson, C. M., Killick, R., Yu, X., Jefferys, J. G. R., & Duff, K. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0276 · Cited by 76 · see citing works
Role of HIV in Amyloid Metabolism
Ortega, M., & Ances, B. M. (2014) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-014-9546-0 · Cited by 75 · see citing works
Cerebral Serotonin 4 Receptors and Amyloid-β in Early Alzheimer's Disease
Madsen, K., Neumann, W., Holst, K. K., Marner, L., Haahr, M. E., Lehel, S., Knudsen, G. M., & Hasselbalch, S. G. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110056 · Cited by 72 · see citing works
Neurofibrillary tangle formation by introducing wild-type human tau into APP transgenic mice
Umeda, T., Maekawa, S., Kimura, T., Takashima, A., Tomiyama, T., & Mori, H. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1259-1 · Cited by 72 · see citing works
Alterations in α4β2 nicotinic receptors in cognitive decline in Alzheimer’s aetiopathology
Okada, H., Ouchi, Y., Ogawa, M., Futatsubashi, M., Saito, Y., Yoshikawa, E., Terada, T., Oboshi, Y., Tsukada, H., Ueki, T., et al. (2013) · Brain · doi:10.1093/brain/awt195 · Cited by 72 · see citing works
Pathological Tau Tangles Localize to Focal Cortical Dysplasia in Older Patients
Sen, A., Thom, M., Martinian, L., Harding, B. N., Cross, J. H., Nikolić, M., & Sisodiya, S. M. (2007) · Epilepsia · doi:10.1111/j.1528-1167.2007.01107.x · Cited by 71 · see citing works
Campbell, J. N., Register, D., & Churn, S. B. (2012) · Journal of Neurotrauma · doi:10.1089/neu.2011.1761 · Cited by 70 · cited 1× · see citing works
“Trauma causes initial spine loss mediated by calcineurin, followed by an overgrowth of spines [31].”
BackgroundIn vivo type 1 cannabinoid receptor availability in Alzheimer's disease
Ahmad, R. U., Goffin, K. E., den Stock, J. V., Winter, F. D., Cleeren, E., Bormans, G. M., Tournoy, J., Persoons, P., Laere, K. V., & Vandenbulcke, M. (2013) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2013.10.002 · Cited by 70 · see citing works
Early calcium dysregulation in Alzheimer’s disease: setting the stage for synaptic dysfunction
Chakroborty, S., & Stutzmann, G. E. (2011) · Science China Life Sciences · doi:10.1007/s11427-011-4205-7 · Cited by 70 · see citing works
Plaque complement activation and cognitive loss in Alzheimer's disease
Loeffler, D. A., Camp, D. M., & Bennett, D. A. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-9 · Cited by 68 · see citing works
Promiscuous Alzheimer's Amyloid: Yet Another Partner
Benilova, I., & De Strooper, B. (2013) · Science · doi:10.1126/science.1244166 · Cited by 67 · see citing works
Zaman, S. H., Parent, A., Laskey, A., Lee, M. K., Borchelt, D., Sisodia, S. S., & Malinow, R. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0271 · Cited by 67 · see citing works
Price, K. A., Varghese, M., Sowa, A., Yuk, F., Brautigam, H., Ehrlich, M. E., & Dickstein, D. L. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-41 · Cited by 65 · see citing works
Impaired plasticity of cortical dendritic spines in P301S tau transgenic mice
Hoffmann, N. A., Dorostkar, M. M., Blumenstock, S., Goedert, M., & Herms, J. W. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-82 · Cited by 64 · see citing works
Self-citation
Flagged first, then by citations
1 of the 232 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [133]Mori C Spooner ET Wisniewsk KE Wisniewski TM Yamaguch H Saido TC Tolan DR Selkoe DJ Lemere CA Intraneuronal Abeta42 accumulation in Down syndrome brain Amyloid 2002 9 88 102 12440481
Cited by
Sorted by citations
Synaptic basis of Alzheimer’s disease: Focus on synaptic amyloid beta, P-tau and mitochondria
John, A., & Reddy, P. H. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101208 · Cited by 359 · see citing works
Yarjanli, Z., Ghaedi, K., Esmaeili, A., Rahgozar, S., & Zarrabi, A. (2017) · BMC Neuroscience · doi:10.1186/s12868-017-0369-9 · Cited by 300 · see citing works
Neuropathology of amyotrophic lateral sclerosis and its variants
Saberi, S., Stauffer, J. E., Schulte, D. J., & Ravits, J. (2015) · Neurologic Clinics · doi:10.1016/j.ncl.2015.07.012 · Cited by 282 · see citing works
Maestú, F., de Haan, W., Busche, M. A., & DeFelipe, J. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101372 · Cited by 235 · see citing works
Poor sleep is associated with CSF biomarkers of amyloid pathology in cognitively normal adults
Sprecher, K. E., Koscik, R. L., Carlsson, C. M., Zetterberg, H., Blennow, K., Okonkwo, O. C., Sager, M. A., Asthana, S., Johnson, S. C., Benca, R. M., et al. (2017) · Neurology · doi:10.1212/wnl.0000000000004171 · Cited by 221 · see citing works
Role of p38/MAPKs in Alzheimer's Disease: Implications for Amyloid Beta Toxicity Targeted Therapy
Kheiri, G., Dolatshahi, M., Rahmani, F., & Rezaei, N. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2018-0008 · Cited by 211 · see citing works
de Pins, B., Cifuentes-Díaz, C., Farah, A. T., López-Molina, L., Montalban, E., Sancho‐Balsells, A., López, A. V., Ginés, S., Delgado-Garcia, J. M., Alberch, J., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.2121-18.2019 · Cited by 197 · see citing works
Chronic 2P-STED imaging reveals high turnover of dendritic spines in the hippocampus in vivo
Pfeiffer, T., Poll, S., Bancelin, S., Angibaud, J., Inavalli, V. K., Keppler, K., Mittag, M., Fuhrmann, M., & Nägerl, U. V. (2018) · eLife · doi:10.7554/elife.34700 · Cited by 192 · see citing works
Structural and functional plasticity of dendritic spines – root or result of behavior?
Gipson, C. D., & Olive, M. F. (2016) · Genes Brain & Behavior · doi:10.1111/gbb.12324 · Cited by 192 · see citing works
Cellular mechanisms and treatments for chemobrain: insight from aging and neurodegenerative diseases
Nguyen, L. D., & Ehrlich, B. E. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012075 · Cited by 176 · see citing works
Bustamante-Barrientos, F. A., Méndez-Ruette, M., Ortloff, A., Luz‐Crawford, P., Rivera, F. J., Figueroa, C. D., Molina, L., & Bátiz, L. F. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.636176 · Cited by 174 · see citing works
Mathematical model on Alzheimer’s disease
Hao, W., & Friedman, A. (2016) · BMC Systems Biology · doi:10.1186/s12918-016-0348-2 · Cited by 153 · see citing works
Contribution of Tau Pathology to Mitochondrial Impairment in Neurodegeneration
Maria Jose Perez, J., Jara, C., & Quintanilla, R. A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00441 · Cited by 153 · see citing works
BDNF signaling during the lifetime of dendritic spines
Zagrebelsky, M., Tacke, C., & Korte, M. (2020) · Cell and Tissue Research · doi:10.1007/s00441-020-03226-5 · Cited by 147 · see citing works
Dendritic Spines as Tunable Regulators of Synaptic Signals
Tønnesen, J., & Nägerl, U. V. (2016) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2016.00101 · Cited by 136 · see citing works
Tan, C., Lu, N., Wang, C., Chen, D.-Y., Sun, N.-H., Lyu, H., Körbelin, J., Shi, W., Fukunaga, K., Lu, Y., et al. (2019) · Neuron · doi:10.1016/j.neuron.2018.12.036 · Cited by 126 · see citing works
Piirainen, S., Youssef, A. M., Song, C., Kalueff, A. V., Landreth, G. E., Malm, T., & Tian, L. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.01.046 · Cited by 125 · see citing works
Nand, S., Mishra, D., Singh, P., Vamanu, E., & Singh, M. P. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111377 · Cited by 116 · see citing works
Mukherjee, A., & Williams, D. W. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.64 · Cited by 96 · see citing works
Yang, L., Wu, C., Li, Y., Dong, Y., Wu, C. Y., Lee, R. H., Brann, D. W., Lin, H. W., & Zhang, Q. (2022) · GeroScience · doi:10.1007/s11357-022-00534-2 · Cited by 93 · see citing works
Apaijai, N., Moisescu, D. M., Palee, S., McSweeney, C. M., Saiyasit, N., Maneechote, C., Boonnag, C., Chattipakorn, N., & Chattipakorn, S. C. (2019) · Journal of the American Heart Association · doi:10.1161/jaha.118.010838 · Cited by 90 · see citing works
Montero‐Crespo, M., Domínguez-Álvaro, M., Alonso‐Nanclares, L., DeFelipe, J., & Blázquez‐Llorca, L. (2020) · Brain · doi:10.1093/brain/awaa406 · Cited by 88 · see citing works
Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies
Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 87 · see citing works
Ongnok, B., Khuanjing, T., Chunchai, T., Pantiya, P., Kerdphoo, S., Arunsak, B., Nawara, W., Jaiwongkam, T., Apaijai, N., Chattipakorn, N., et al. (2021) · Neurotherapeutics · doi:10.1007/s13311-021-01092-9 · Cited by 84 · see citing works
The Impact of Estradiol on Neurogenesis and Cognitive Functions in Alzheimer’s Disease
Negah, S. S., Hajali, V., Moradi, H. R., & Gorji, A. (2019) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-019-00733-0 · Cited by 83 · see citing works
Three-dimensional analysis of synapses in the transentorhinal cortex of Alzheimer’s disease patients
Domínguez-Álvaro, M., Montero-Crespo, M., Blazquez-Llorca, L., Insausti, R., DeFelipe, J., & Alonso-Nanclares, L. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0520-6 · Cited by 79 · see citing works
Dendritic Spine and Synaptic Plasticity in Alzheimer’s Disease: A Focus on MicroRNA
Reza-Zaldívar, E. E., Hernández-Sapiéns, M. A., Minjarez, B. D., Gómez‐Pinedo, U., Sánchez-González, V., Márquez-Aguirre, A. L., & Canales-Aguirre, A. A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00255 · Cited by 77 · see citing works
Krishtal, J., Bragina, O., Metsla, K., Palumaa, P., & Tõugu, V. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186636 · Cited by 76 · see citing works
Geloso, M. C., & D’Ambrosi, N. (2021) · Cells · doi:10.3390/cells10030686 · Cited by 74 · see citing works
Cortese, G. P., & Bürger, C. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.08.027 · Cited by 74 · see citing works
Reed, S., Taka, E., Darling‐Reed, S., & Soliman, K. F. A. (2025) · Cells · doi:10.3390/cells14141064 · Cited by 71 · see citing works
The Cognitive Effects of Radiotherapy for Brain Metastases
Lehrer, E. J., Jones, B. M., Dickstein, D. R., Green, S., Germano, I. M., Palmer, J. D., Laack, N. N., Brown, P. D., Gondi, V., Wefel, J. S., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.893264 · Cited by 70 · see citing works
van Nifterick, A. M., Gouw, A. A., van Kesteren, R. E., Scheltens, P., Stam, C. J., & de Haan, W. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-01041-4 · Cited by 70 · see citing works
Furcila, D., DeFelipe, J., & Alonso‐Nanclares, L. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180173 · Cited by 70 · see citing works
Lebouvier, T., Pasquier, F., & Buée, L. (2017) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000502 · Cited by 68 · see citing works
Imaging Synaptic Density: The Next Holy Grail of Neuroscience?
Serrano, M. E., Kim, E., Petrinovic, M. M., Turkheimer, F., & Cash, D. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.796129 · Cited by 67 · see citing works
Impact of Tau on Neurovascular Pathology in Alzheimer's Disease
Canepa, E., & Fossati, S. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.573324 · Cited by 65 · see citing works
Psychedelic‐inspired approaches for treating neurodegenerative disorders
Saeger, H. N., & Olson, D. E. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15544 · Cited by 65 · see citing works
Domínguez-Álvaro, M., Montero‐Crespo, M., Blázquez‐Llorca, L., DeFelipe, J., & Alonso‐Nanclares, L. (2019) · eNeuro · doi:10.1523/eneuro.0140-19.2019 · Cited by 64 · see citing works
Fan, C., Zhu, X., Song, Q., Wang, P., Liu, Z., & Yu, S. Y. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.01.009 · Cited by 63 · see citing works
Mitigating Alzheimer’s Disease with Natural Polyphenols: A Review
Gaudreault, R., & Mousseau, N. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666190315093520 · Cited by 63 · see citing works
Compta, Y., & Révész, T. (2020) · Journal of Parkinson s Disease · doi:10.3233/jpd-202323 · Cited by 61 · see citing works
AbuelEzz, N. Z., Nasr, F. E., Abdulkader, M. A., Bassiouny, A. R., & Zaky, A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.743573 · Cited by 60 · see citing works
The Role of Mitochondrial Impairment in Alzheimer´s Disease Neurodegeneration: The Tau Connection
Quntanilla, R. A., & Tapia-Monsalves, C. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200525020259 · Cited by 59 · see citing works
Pedrazzoli, M., Losurdo, M., Paolone, G., Medelin, M., Jaupaj, L., Cisterna, B., Slanzi, A., Malatesta, M., Coco, S., & Buffelli, M. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104568 · Cited by 58 · see citing works
Ongnok, B., Khuanjing, T., Chunchai, T., Kerdphoo, S., Jaiwongkam, T., Chattipakorn, N., & Chattipakorn, S. C. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165975 · Cited by 55 · see citing works
Dong, Q., Teng, S.-W., Wang, Y., Qin, F., Li, Y., Ai, L., & Yu, H. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.12.041 · Cited by 54 · see citing works
Singh, R., Bartók, Á., Paillard, M., Tyburski, A. L., Elliott, M. B., & Hajnóczky, G. (2022) · Science Advances · doi:10.1126/sciadv.abj4716 · Cited by 53 · see citing works
Ishii, T., Furuoka, H., Kaya, M., & Kuhara, T. (2021) · Biomedicines · doi:10.3390/biomedicines9020167 · Cited by 50 · see citing works
Shaw, A. E., & Bamburg, J. R. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.031 · Cited by 50 · see citing works
VEGF counteracts amyloid-β-induced synaptic dysfunction
Martin, L., Bouvet, P., Chounlamountri, N., Watrin, C., Besançon, R., Pinatel, D., Meyronet, D., Honnorat, J., Buisson, A., Salin, P. A., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109121 · Cited by 49 · see citing works
Gong, W.-G., Wang, Y., Zhou, H., Li, X.-L., Bai, F., Ren, Q., & Zhang, Z. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9781-x · Cited by 49 · see citing works
Chu, S., Liu, S., Duan, W., Cheng, Y., Jiang, X., Zhu, C., Tang, K. L., Wang, R., Xu, L., Wang, X., et al. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.01.002 · Cited by 49 · see citing works
siRNA drug delivery across the blood–brain barrier in Alzheimer's disease
Sajid, M. I., Sheikh, F. S., Anis, F., Nasim, N., Sumbria, R. K., Nauli, S. M., & Tiwari, R. K. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.114968 · Cited by 45 · see citing works
Jiang, T., Handley, E. E., Brizuela, M., Dawkins, E., Lewis, K. E. A., Clark, R. M., Dickson, T. C., & Blizzard, C. A. (2019) · Disease Models & Mechanisms · doi:10.1242/dmm.038109 · Cited by 45 · see citing works
Actin Cytoskeleton Role in the Maintenance of Neuronal Morphology and Long-Term Memory
Lamprecht, R. (2021) · Cells · doi:10.3390/cells10071795 · Cited by 45 · see citing works
Neuronal sphingosine kinase 2 subcellular localization is altered in Alzheimer’s disease brain
Dominguez, G., Maddelein, M.-L., Pucelle, M., Nicaise, Y., Maurage, C.-A., Duyckaerts, C., Cuvillier, O., & Delisle, M.-B. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0527-z · Cited by 43 · see citing works
Ma, G., Liu, M., Du, K., Zhong, X., Gong, S., Jiao, L., & Wei, M. (2019) · BioMed Research International · doi:10.1155/2019/8179145 · Cited by 41 · see citing works
Corsetti, V., Borreca, A., Latina, V., Giacovazzo, G., Pignataro, A., Krashia, P., Natale, F., Cocco, S., Rinaudo, M., Malerba, F., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa039 · Cited by 41 · see citing works
Ouellette, A. R., Neuner, S. M., Dumitrescu, L. C., Anderson, L. C., Gatti, D. M., Mahoney, E. R., Bubier, J. A., Churchill, G. A., Peters, L. L., Huentelman, M. J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108091 · Cited by 40 · see citing works
Rudobeck, E., Bellone, J. A., Szűcs, A. L., Bonnick, K., Mehrotra, S., Badaut, J., Nelson, G. A., Hartman, R. E., & Vlkolinský, R. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186168 · Cited by 39 · see citing works
Garcia, G., Pinto, S., Cunha, M., Fernandes, A., Koistinaho, J., & Brites, D. (2021) · Cells · doi:10.3390/cells10092424 · Cited by 39 · see citing works
Sreenivasmurthy, S. G., Iyaswamy, A., Krishnamoorthi, S., Reddi, R. N., Kammala, A. K., Vasudevan, K., Senapati, S., Zhu, Z., Su, C.-F., Liu, J., et al. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1030534 · Cited by 38 · see citing works
Lynx1 Limits Dendritic Spine Turnover in the Adult Visual Cortex
Sajo, M., Ellis‐Davies, G. C. R., & Morishita, H. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0580-16.2016 · Cited by 38 · see citing works
DMSO modulates CNS function in a preclinical Alzheimer's disease model
Penazzi, L., Lorengel, J., Sündermann, F., Golovyashkina, N., Marre, S., Mathis, C., Lewejohann, L., Brandt, R., & Bakota, L. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.10.020 · Cited by 38 · see citing works
Sengupta, U., Puangmalai, N., Bhatt, N. N., García, S., Zhao, Y., & Kayed, R. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01913-6 · Cited by 38 · see citing works
In vivo coupling of dendritic complexity with presynaptic density in primary tauopathies
Mak, E., Holland, N., Jones, P. S., Savulich, G., Low, A., Malpetti, M., Kaalund, S. S., Passamonti, L., Rittman, T., Romero-García, R., et al. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.01.016 · Cited by 38 · see citing works
Current druggable targets for therapeutic control of Alzheimer's disease
Gupta, G. L., & Samant, N. P. (2021) · Contemporary Clinical Trials · doi:10.1016/j.cct.2021.106549 · Cited by 38 · see citing works
Sanchez-Varo, R. M., Sánchez‐Mejías, E., Fernandez-Valenzuela, J. J., Castro, V. D., Mejias‐Ortega, M., Gómez-Arboledas, Á., Jiménez, S., Sanchez-Mico, M. V., Trujillo‐Estrada, L., Moreno‐González, I., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.752594 · Cited by 38 · see citing works
Schaefer, T. L., Davenport, M. H., Grainger, L. M., Robinson, C. K., Earnheart, A. T., Stegman, M., Lang, A. L., Ashworth, A. A., Molinaro, G., Huber, K. M., et al. (2017) · Journal of Neurodevelopmental Disorders · doi:10.1186/s11689-017-9184-y · Cited by 37 · see citing works
Dynamic presenilin 1 and synaptotagmin 1 interaction modulates exocytosis and amyloid β production
Zoltowska, K. M., Maesako, M., Lushnikova, I., Takeda, S., Keller, L. J., Skibo, G., Hyman, B. T., & Berezovska, O. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0159-y · Cited by 36 · see citing works
Solis‐Gaspar, C., Vázquez‐Roque, R. A., Gómez-Villalobos, M. D. J., & Flores, G. (2016) · Synapse · doi:10.1002/syn.21912 · Cited by 36 · see citing works
Iron and Targeted Iron Therapy in Alzheimer’s Disease
Wang, J., Fu, J., Zhao, Y., Liu, Q., Yan, X., & Su, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216353 · Cited by 35 · see citing works
If Human Brain Organoids Are the Answer to Understanding Dementia, What Are the Questions?
Ooi, L., Dottori, M., Cook, A. L., Engel, M., Gautam, V., Grubman, A., Hernández, D., King, A. E., Maksour, S., Anastacio, H. T. D., et al. (2020) · The Neuroscientist · doi:10.1177/1073858420912404 · Cited by 34 · see citing works
Gender and Neurosteroids: Implications for Brain Function, Neuroplasticity and Rehabilitation
Raciti, L., Formica, C., Raciti, G., Quartarone, A., & Calabrò, R. S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054758 · Cited by 33 · see citing works
Glennon, E. B. C., Lau, D. H. W., Gabriele, R. M. C., Taylor, M. F., Troakes, C., Opie-Martin, S., Elliott, C., Killick, R., Hanger, D. P., Perez‐Nievas, B. G., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa011 · Cited by 33 · see citing works
The effects of astaxanthin treatment on a rat model of Alzheimer’s disease
Chen, M.-H., Wang, T., Chen, L.-J., Jiang, M.-Y., Wang, Y., Tseng, G., & Chen, J. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.04.020 · Cited by 33 · see citing works
Recent Insights into the Neurobiology of Alzheimer’s Disease and Advanced Treatment Strategies
Anitha, K., Singh, M. K., Kohat, K., Varshini, T. S., Chenchula, S., Padmavathi, R., Amerneni, L. S., Vishnu Vardhan, K., Mythili Bai, K., Chavan, M. R., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04384-1 · Cited by 32 · see citing works
Hernández‐Hernández, E. M., Hernandez, K. C., Vázquez‐Roque, R. A., Díaz, A., de la Cruz, F., Florán, B., & Flores, G. (2018) · Synapse · doi:10.1002/syn.22036 · Cited by 30 · see citing works
Ongnok, B., Maneechote, C., Chunchai, T., Pantiya, P., Arunsak, B., Nawara, W., Chattipakorn, N., & Chattipakorn, S. C. (2022) · FEBS Journal · doi:10.1111/febs.16474 · Cited by 30 · see citing works
Bello-Medina, P. C., Prado-Alcalá, R. A., & Rivas-Arancibia, S. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.01.018 · Cited by 29 · see citing works
Heiss, J. K., Barrett, J., Yu, Z., Haas, L. T., Kostylev, M. A., & Strittmatter, S. M. (2016) · Cerebral Cortex · doi:10.1093/cercor/bhw188 · Cited by 29 · see citing works
Parajuli, L. K., Wako, K., Maruo, S., Kakuta, S., Taguchi, T., Ikuno, M., Yamakado, H., Takahashi, R., & Koike, M. (2020) · eNeuro · doi:10.1523/eneuro.0072-20.2020 · Cited by 29 · see citing works
Pin1 mediates Aβ 42 -induced dendritic spine loss
Stallings, N. R., O’Neal, M. A., Hu, J., Kavalali, E. T., Борисович, Б. И., & Malter, J. S. (2018) · Science Signaling · doi:10.1126/scisignal.aap8734 · Cited by 29 · see citing works
Ettcheto, M., Abad, S., Petrov, D., Pedrós, I., Busquets, O., Sánchez‐López, E., Casadesús, G., Beas‐Zárate, C., Carro, E., Auladell, C., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0690-4 · Cited by 28 · see citing works
Chae, S., Lee, H., Lee, H.-E., Kim, J., Jeong, Y. J., Lin, Y., Kim, H. Y., Leriche, G., Ehrlich, R. S., Lingl, S. C., et al. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03180-x · Cited by 26 · see citing works
Expansion of the neocortex and protection from neurodegeneration by in vivo transient reprogramming
Shen, Y.-R., Zaballa, S., Bech, X., Sancho‐Balsells, A., Rodríguez-Navarro, I., Cifuentes-Díaz, C., Seyit-Bremer, G., Chun, S. H., Straub, T., Abante, J., et al. (2024) · Cell stem cell · doi:10.1016/j.stem.2024.09.013 · Cited by 26 · see citing works
Synapse vulnerability and resilience across the clinical spectrum of dementias
Taddei, R. N., & Duff, K. (2025) · Nature Reviews Neurology · doi:10.1038/s41582-025-01094-7 · Cited by 26 · see citing works
Ren, Q., Gong, W.-G., Zhou, H., Shu, H., Wang, Y., & Zhang, Z. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-00698-w · Cited by 26 · see citing works
Villalobos-Acosta, D. M. Á., Chimal‐Vega, B., Correa‐Basurto, J., Morales, L. G. F., & Rosales‐Hernández, M. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082415 · Cited by 25 · see citing works
Vasilopoulou, F., Bellver‐Sanchís, A., Companys‐Alemany, J., Jarné‐Ferrer, J., Irisarri, A., Palomera‐Ávalos, V., González-Castillo, C., Ortuño‐Sahagún, D., Sanfeliu, C., Pallàs, M., et al. (2022) · Cells · doi:10.3390/cells11162603 · Cited by 25 · see citing works
Li, S., Li, W., Wu, X., Li, J., Yang, J., Tu, C., Ye, X., & Ling, S. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.03.006 · Cited by 24 · see citing works
Rasia‐Filho, A. A., Guerra, K. T. K., Vásquez, C. E., Dall’Oglio, A., Reberger, R., Jung, C. R., & Calcagnotto, M. E. (2021) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2021.616607 · Cited by 24 · see citing works
Nazere, K., Takahashi, T., Hara, N., Muguruma, K., Nakamori, M., Yamazaki, Y., Morino, H., & Maruyama, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.804702 · Cited by 24 · see citing works
Cyclosporine A (CsA) prevents synaptic impairment caused by truncated tau by caspase-3
Tapia-Monsalves, C., Olesen, M. A., Villavicencio-Tejo, F., & Quintanilla, R. A. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103861 · Cited by 24 · see citing works
Neuroinflammation and Alzheimer's disease: Unravelling the molecular mechanisms
Kakkar, A., Singh, H., Singh, B. K., Kumar, A., Mishra, A. K., & Chopra, H. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251374353 · Cited by 23 · see citing works
Stachowicz, K. (2018) · Acta Neurobiologiae Experimentalis · doi:10.21307/ane-2018-019 · Cited by 23 · see citing works
NODDI in gray matter is a sensitive marker of aging and early AD changes
Yu, X., Przybelski, S. A., Reid, R. I., Lesnick, T. G., Raghavan, S., Graff‐Radford, J., Lowe, V. J., Kantarci, K., Knopman, D. S., Petersen, R. C., et al. (2024) · Alzheimer's & Dementia: Diagnosis, Assessment & Disease Monitoring · doi:10.1002/dad2.12627 · Cited by 23 · see citing works
Neurogranin Levels in Cerebrospinal Fluid
Zetterberg, H., & Blennow, K. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.2075 · Cited by 22 · see citing works
Lu, J., Florio, D. N. D., Boya, P., Maday, S., Springer, W., & Chu, C. T. (2025) · Autophagy · doi:10.1080/15548627.2025.2581217 · Cited by 21 · see citing works
- Authors
- Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J.
- Affiliations
- Institut für Neuropathologie (DE)
- German Center for Neurodegenerative Diseases (DE)
- Corresponding author
- Herms, Jochen
- Venue
- Acta Neuropathologica
- Published
- 2015-06-11
- Volume
- 130
- Issue
- 1
- Pages
- 1-19
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC4469300
- OpenAlex
- W622376569
- Cited by
- 235
- References
- 232
- Citations by year
- 2026: 15 · 2025: 30 · 2024: 34 · 2023: 20 · 2022: 25 · 2021: 29 · 2020: 23 · 2019: 19 · 2018: 13 · 2017: 13 · 2016: 12 · 2015: 2
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Acta Neuropathologica (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DZNE Pub (submittedVersion, cc-by)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- dendritic spine loss, Alzheimer's disease, synaptic dysfunction, amyloid-beta, amyloid oligomers, tau hyperphosphorylation, microglial activation, animal models of Alzheimer's disease, cognitive decline, memory impairment
- MeSH terms
- Alzheimer Disease, Amyloid, Animals, Brain, Humans, Dendritic Spines
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review