The DOI matches its Crossref record; 185 of the 186 references it cites were found in a registry or an index.
Amyloid Oligomers Exacerbate Tau Pathology in a Mouse Model of Tauopathy
Open accessAbstract
BACKGROUND: We aimed to investigate the influence of oligomeric forms of β-amyloid (Aβ) and the influence of the duration of exposure on the development of tau phosphorylation. METHODS: Aβ oligomers were injected intracranially either acutely into 5-month-old rTg4510 mice and tissue was collected 3 days later, or chronically into 3-month-old mice and tissue was collected 2 months later. Several forms of phosphorylated tau (p-tau), GSK3 (glycogen synthase kinase-3) and microglial and astrocyte activation were measured. RESULTS: Acute injections of Aβ oligomers had no effect on p-tau epitopes but did result in elevation of phosphorylated/activated GSK3 (pGSK3). Chronic infusion of Aβ oligomers into the right hippocampus resulted in 3- to 4-fold elevations in several p-tau isoforms with no changes in total tau levels. A significant elevation in pGSK3 accompanied these changes. Microglial staining with CD68 paralleled the increase in tau phosphorylation, however, CD45 staining was unaffected by Aβ. Control experiments revealed that the infusion of Aβ from the minipumps was largely complete by 10 days after implantation. Thus, the elevation in p-tau 2 months after implantation implies that the changes are quite persistent. CONCLUSION: Soluble Aβ(1-42) oligomers have long-lasting effects on tau phosphorylation in the rTg4510 model, possibly due to elevations in GSK3. These data suggest that even brief elevations in Aβ production, may have enduring impact on the risk for tauopathy.
Overview
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
Verification
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?
The check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“The relationship between DTI-detected WM changes and histologically detected axonal loss has been observed in several animal and human studies 25, 51–54”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [52]
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Similar to our findings, reductions in FA and increases in RAD were found to correlate with axon loss in abnormal WM in both MCI and AD patients 25,51–54”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [52]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498
A simplified system for generating recombinant adenoviruses
He, T., Zhou, S., da Costa, L. T., Yu, J., Kinzler, K. W., & Vogelstein, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.5.2509 · Cited by 3,209
Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse
Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Cited by
Sorted by citations
Items 1,501–1,600 of 1,639
Extracellular vesicle proteome unveils cathepsin B connection to Alzheimer’s disease pathogenesis
Yuyama, K., Sun, H., Fujii, R., Hemmi, I., Ueda, K., & Igeta, Y. (2024) · Brain · doi:10.1093/brain/awad361 · Cited by 47
The Role of Amyloid-Beta and Tau in the Early Pathogenesis of Alzheimer’s Disease
Yin, X., Qiu, Y., Zhao, C., Zhou, Z., Bao, J., & Qian, W. (2021) · Medical Science Monitor · doi:10.12659/msm.933084 · Cited by 48
Giannopoulos, P. F., Chu, J., Sperow, M., Li, J.-G., Yu, W. H., Kirby, L. G., Abood, M., & Praticò, D. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2015.01.015 · Cited by 48
RetractedPetrushina, I., Hovakimyan, A., Harahap-Carrillo, I. S., Davtyan, H., Antonyan, T., Chailyan, G., Kazarian, K., Antonenko, M., Jullienne, A., Hamer, M. M., et al. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104823 · Cited by 48
Sharma, A. K., Kim, J., Prior, J. T., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2014) · Inorganic Chemistry · doi:10.1021/ic500926c · Cited by 48
McFarland, K. N., & Chakrabarty, P. (2022) · Neurotherapeutics · doi:10.1007/s13311-021-01179-3 · Cited by 48
Sabbagh, J. J., Cordova, R. A., Zheng, D., Criado-Marrero, M., Lemus, A., Li, P., Baker, J. D., Nordhues, B. A., Darling, A. L., Martinez-Licha, C., et al. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00454 · Cited by 48
Self-citationNPT088 reduces both amyloid‐β and tau pathologies in transgenic mice
Levenson, J. M., Schroeter, S., Carroll, J. C., Cullen, V., Asp, E., Proschitsky, M., Chung, C. H. ‐., Gilead, S., Nadeem, M., Dodiya, H. B., et al. (2016) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2016.06.004 · Cited by 47
Heuer, H. W., Wang, P., Rascovsky, K., Wolf, A., Appleby, B., Bove, J., Bordelon, Y., Brannelly, P., Brushaber, D. E., Caso, C., et al. (2020) · Alzheimer's & Dementia · doi:10.1002/alz.12046 · Cited by 43
Bernard-Gauthier, V., Mossine, A. V., Knight, A., Patnaik, D., Zhao, W.-N., Cheng, C., Krishnan, H. S., Xuan, L. L., Chindavong, P. S., Reis, S. A., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01030 · Cited by 49
Matsumoto, K., Chiba, Y., Fujihara, R., Kubo, H., Sakamoto, H., & Ueno, M. (2015) · Histochemistry and Cell Biology · doi:10.1007/s00418-015-1366-7 · Cited by 46
Comparative pathobiology of β-amyloid and the unique susceptibility of humans to Alzheimer's disease
Rosen, R. F., Tomidokoro, Y., Farberg, A. S., Dooyema, J., Ciliax, B., Preuss, T. M., Neubert, T. A., Ghiso, J. A., LeVine, H., & Walker, L. C. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.04.019 · Cited by 46
Insights on the Use of Transgenic Mice Models in Alzheimer’s Disease Research
Pádua, M. S., Guil-Guerrero, J. L., Prates, J. A. M., & Lopes, P. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052805 · Cited by 46
HtrA1 Proteolysis of ApoE In Vitro Is Allele Selective
Chu, Q., Diedrich, J. K., Vaughan, J. M., Donaldson, C. J., Nunn, M. F., Lee, K.-F., & Saghatelian, A. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03463 · Cited by 46
Parp mutations protect from mitochondrial toxicity in Alzheimer’s disease
Yu, Y., Fedele, G., Celardo, I., Loh, S. H. Y., & Martins, L. M. (2021) · Cell Death & Disease · doi:10.1038/s41419-021-03926-y · Cited by 46
Kasica, N. P., Zhou, X., Yang, Q., Wang, X., Yang, W., Zimmermann, H. R., Holland, C. E., Koscielniak, E., Wu, H., Cox, A. O., et al. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15562 · Cited by 34
Advanced Overview of Biomarkers and Techniques for Early Diagnosis of Alzheimer’s Disease
Rani, S., Dhar, S. B., Khajuria, A., Gupta, D., Jaiswal, P. K., Singla, N., Kaur, M., Singh, G., & Barnwal, R. P. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01330-y · Cited by 48
Altered DNA base excision repair profile in brain tissue and blood in Alzheimer’s disease
Lillenes, M. S., Rabano, A., Støen, M., Riaz, T., Misaghian, D., Møllersen, L., Esbensen, Y., Günther, C.-C., Selnes, P., Stenset, V. T. V., et al. (2016) · Molecular Brain · doi:10.1186/s13041-016-0237-z · Cited by 46
Meilandt, W. J., Maloney, J. A., Imperio, J., Lalehzadeh, G., Earr, T., Crowell, S., Bainbridge, T. W., Lu, Y., Ernst, J. A., Fuji, R. N., et al. (2019) · Alzheimer's Research & Therapy · doi:10.1186/s13195-019-0553-5 · Cited by 45
Mechanisms of tau and Aβ-induced excitotoxicity
Pallo, S. P., DiMaio, J., Cook, A., Nilsson, B., & Johnson, G. V. W. (2016) · Brain Research · doi:10.1016/j.brainres.2015.12.048 · Cited by 46
Spiegel, J., Pirraglia, E., Osorio, R. S., Glodzik, L., Li, Y., Tsui, W., Saint Louis, L. A., Randall, C., Butler, T., Xu, J., et al. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150167 · Cited by 45
Apolipoprotein E decreases tau kinases and phospho-tau levels in primary neurons.
Hoe, H.-S., Freeman, J., & Rebeck, G. W. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-18 · Cited by 45
Genetically modified large animal models for investigating neurodegenerative diseases
Yang, W., Chen, X., Li, S., & Li, X.-J. (2021) · Cell & Bioscience · doi:10.1186/s13578-021-00729-8 · Cited by 45
Monitoring phagocytic uptake of amyloid β into glial cell lysosomes in real time
Prakash, P., Jethava, K. P., Korte, N., Izquierdo, P., Favuzzi, E., Rose, I. V. L., Guttenplan, K. A., Manchanda, P., Dutta, S., Rochet, J.-C., et al. (2021) · Chemical Science · doi:10.1039/d1sc03486c · Cited by 45
Han, G., Bai, K., Yang, X., Sun, C., Ji, Y., Zhou, J., Zhang, H., & Ding, Y. (2022) · Advanced Science · doi:10.1002/advs.202106072 · Cited by 46
Early and sustained altered expression of aging-related genes in young 3xTg-AD mice
Gatta, V, D'Aurora, M., Granzotto, A., Stuppia, L., & Sensi, S. L. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.11 · Cited by 44
Verheijden, S., Beckers, L., Casazza, A., Butovsky, O., Mazzone, M., & Baes, M. (2015) · Glia · doi:10.1002/glia.22831 · Cited by 40
Faulty splicing and cytoskeleton abnormalities in Huntington's disease
Fernández‐Nogales, M., Santos‐Galindo, M., Hernández, I. H., Cabrera, J. R., & Lucas, J. J. (2016) · Brain Pathology · doi:10.1111/bpa.12430 · Cited by 41
Suelves, N., Saleki, S., Ibrahim, T., Palomares, D., Moonen, S., Koper, M. J., Vrancx, C., Vadukul, D. M., Papadopoulos, N., Viceconte, N., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01578-x · Cited by 43
Cavieres, V. A., González, A., Muñoz, V. C., Yefi, C. P., Bustamante, H. A., Barraza, R. R., Tapia-Rojas, C., Otth, C., Barrera, M. J., González, C., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0136313 · Cited by 43
Aloi, M. S., Prater, K. E., Sánchez, R. E. A., Beck, A., Pathan, J. L., Davidson, S., Wilson, A., Keene, C. D., de la Iglesia, H., Jayadev, S., et al. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02745-6 · Cited by 43
Expression of Translocator Protein and [18F]-GE180 Ligand Uptake in Multiple Sclerosis Animal Models
Nack, A., Brendel, M., Nedelcu, J., Daerr, M., Nyamoya, S., Beyer, C., Focke, C., Deussing, M., Hoornaert, C., Ponsaerts, P., et al. (2019) · Cells · doi:10.3390/cells8020094 · Cited by 43
Microglia Phenotypes Following the Induction of Alcohol Dependence in Adolescent Rats
Peng, H., & Nixon, K. (2021) · Alcoholism: Clinical and Experimental Research · doi:10.1111/acer.14504 · Cited by 43
Spreading Depression Transiently Disrupts Myelin via Interferon-Gamma Signaling
Pusic, A. D., Mitchell, H. M., Kunkler, P. E., Klauer, N., & Kraig, R. P. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2014.12.001 · Cited by 42
Carosi, J. M., & Sargeant, T. J. (2023) · Autophagy · doi:10.1080/15548627.2023.2175569 · Cited by 41
Naito, Y., Tanabe, Y., Lee, A. K., Hamel, E., & Takahashi, H. (2017) · Scientific Reports · doi:10.1038/srep42548 · Cited by 42
Unified theory of Alzheimer’s disease (UTAD): implications for prevention and curative therapy
Nehls, M. (2016) · Journal of Molecular Psychiatry · doi:10.1186/s40303-016-0018-8 · Cited by 41
Gan, K. J., & Silverman, M. A. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-12-1612 · Cited by 41
Bidirectional modulation of Alzheimer phenotype by alpha-synuclein in mice and primary neurons
Khan, S. S., LaCroix, M., Boyle, G., Sherman, M. A., Brown, J. L., Amar, F., Aldaco, J., Lee, M. K., Bloom, G. S., & Lesné, S. E. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1886-z · Cited by 41
Colon-Perez, L. M., Ibanez, K. R., Suarez, M., Torroella, K., Acuna, K., Ofori, E., Levites, Y., Vaillancourt, D. E., Golde, T. E., Chakrabarty, P., et al. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.116138 · Cited by 41
Chronic Effects of Mild Neurotrauma: Putting the Cart Before the Horse?
Castellani, R. J., Perry, G., & Iverson, G. L. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000193 · Cited by 40
Testing the amyloid cascade hypothesis: Prevention trials in autosomal dominant Alzheimer disease
Levin, J., Vöglein, J., Quiroz, Y. T., Bateman, R. J., Ghisays, V., Lopera, F., McDade, E., Reiman, E., Tariot, P. N., & Morris, J. C. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12624 · Cited by 40
Amyloid‐β induces sleep fragmentation that is rescued by fatty acid binding proteins in Drosophila
Gerstner, J. R., Lenz, O., Vanderheyden, W. M., Chan, M. T., Pfeiffenberger, C., & Pack, A. I. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.23778 · Cited by 40
Selenica, M.-L. B., Davtyan, H., Housley, S. B., Blair, L. J., Gillies, A., Nordhues, B. A., Zhang, B., Liu, J., Gestwicki, J. E., Lee, D. C., et al. (2014) · Journal of Neuroinflammation · doi:10.1186/s12974-014-0152-0 · Cited by 40
Self-citationHeiner, F., Feistel, B., & Wink, M. (2018) · PeerJ · doi:10.7717/peerj.4683 · Cited by 40
A Promising Approach: Magnetic Nanosystems for Alzheimer’s Disease Theranostics
Chaparro, C. I. P., Simões, B. T., Borges, J. P., Castanho, M. A. R. B., Soares, P. I. P., & Neves, V. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15092316 · Cited by 40
Human stem cell-derived neurons: a system to study human tau function and dysfunction
Iovino, M., Patani, R., Watts, C., Chandran, S., & Spillantini, M. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013947 · Cited by 40
Neuroprotective Effects of PARP Inhibitors in Drosophila Models of Alzheimer’s Disease
Maggiore, A., Casale, A. M., Toscanelli, W., Cappucci, U., Rotili, D., Grieco, M., Gagné, J.-P., Poirier, G. G., d’Erme, M., & Piacentini, L. (2022) · Cells · doi:10.3390/cells11081284 · Cited by 40
Marcatti, M., Fracassi, A., Montalbano, M., Natarajan, C., Krishnan, B., Kayed, R., & Taglialatela, G. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04255-9 · Cited by 38
GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein
Nakamura, M., Li, Y., Choi, B.-R., Matas-Rico, E., Troncoso, J., Takahashi, C., & Sockanathan, S. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe6178 · Cited by 38
Sekiya, M., Wang, M., Fujisaki, N., Sakakibara, Y., Quan, X., Ehrlich, M. E., De Jager, P. L., Bennett, D. A., Schadt, E. E., Gandy, S., et al. (2018) · Genome Medicine · doi:10.1186/s13073-018-0530-9 · Cited by 38
Schlegel, K., Awwad, K., Heym, R. G., Holzinger, D., Doell, A., Barghorn, S., Jahn, T. R., Klein, C., Mordashova, Y., Schulz, M., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0831-2 · Cited by 30
Chen, G., Chen, P., Tan, H., Ma, D., Dou, F., Feng, J., & Yan, Z. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.023 · Cited by 36
Yang, C., Li, X., Gao, W., Wang, Q., Zhang, L., Li, Y., Li, L., & Zhang, L. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00682 · Cited by 36
Ma, D., Holmes, H. E., Cardoso, M. J., Modat, M., Harrison, I. F., Powell, N. M., O’Callaghan, J. M., Ismail, O., Johnson, R. A., O’Neill, M. J., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00011 · Cited by 36
Salfi, F., D’Atri, A., Tempesta, D., De Gennaro, L., & Ferrara, M. (2020) · Brain Sciences · doi:10.3390/brainsci10050300 · Cited by 36
Therapeutic Targeting Strategies for Early- to Late-Staged Alzheimer’s Disease
Kang, Y. J., Diep, Y. N., Tran, M., & Cho, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249591 · Cited by 36
Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer’s disease
Gurses, M. S., Ural, M. N., Gulec, M. A., Akyol, O., & Akyol, S. (2016) · Aging and disease · doi:10.14336/ad.2016.0111 · Cited by 35
Wu, Z., Chen, C., Kang, S. S., Liu, X., Gu, X., Yu, S. P., Keene, C. D., Cheng, L., & Ye, K. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100986118 · Cited by 34
Regional associations of white matter hyperintensities and early cortical amyloid pathology
Lorenzini, L., Ansems, L. T., Lopes Alves, I., Ingala, S., Vállez García, D., Tomassen, J., Sudre, C., Salvadó, G., Shekari, M., Operto, G., et al. (2022) · Brain Communications · doi:10.1093/braincomms/fcac150 · Cited by 36
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
AZP2006, a new promising treatment for Alzheimer’s and related diseases
Callizot, N., Estrella, C., Burlet, S., Henriques, A., Brantis, C., Barrier, M., Campanari, M. L., & Verwaerde, P. (2021) · Scientific Reports · doi:10.1038/s41598-021-94708-1 · Cited by 35
Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms
Hwang, K., Vaknalli, R. N., Addo-Osafo, K., Vicente, M., & Vossel, K. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.903973 · Cited by 35
Vallés-Saiz, L., Ávila, J., & Hernández, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241311144 · Cited by 35
C/EBPβ/AEP Signaling Drives Alzheimer’s Disease Pathogenesis
Xiong, J., Zhang, Z., & Ye, K. (2023) · Neuroscience Bulletin · doi:10.1007/s12264-023-01025-w · Cited by 37
Gossye, H., Van Broeckhoven, C., & Engelborghs, S. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00757 · Cited by 34
Jagust, W. J., Koeppe, R. A., Rabinovici, G. D., Villemagne, V. L., Harrison, T. M., Landau, S. M., & Initiative, T. A. D. N. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.14165 · Cited by 34
Reelin proteolysis affects signaling related to normal synapse function and neurodegeneration
Lussier, A. L., Weeber, E. J., & Rebeck, G. W. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00075 · Cited by 31
Tau as a mediator of neurotoxicity associated to cerebral amyloid angiopathy
You, Y., Perkins, A., Cisternas, P., Muñoz, B., Taylor, X., You, Y., Garringer, H. J., Oblak, A. L., Atwood, B. K., Vidal, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0680-z · Cited by 33
Tau; One Protein, So Many Diseases
Tabeshmehr, P., & Eftekharpour, E. (2023) · Biology · doi:10.3390/biology12020244 · Cited by 33
Cheran, G., Silverman, H., Manoochehri, M., Goldman, J., Lee, S., Wu, L., Cines, S., Fallon, E., Kelly, B. D., Olszewska, D. A., et al. (2018) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2017-317263 · Cited by 32
Shaw, A. D., Hughes, L. E., Moran, R., Coyle-Gilchrist, I., Rittman, T., & Rowe, J. B. (2021) · Cerebral Cortex · doi:10.1093/cercor/bhz024 · Cited by 30
Preserved autophagy in cognitively intact non‐demented individuals with Alzheimer's neuropathology
Tumurbaatar, B., Fracassi, A., Scaduto, P., Guptarak, J., Woltjer, R., Jupiter, D., & Taglialatela, G. (2023) · Alzheimer's & Dementia · doi:10.1002/alz.13074 · Cited by 32
The metamorphic nature of the Tau protein: dynamic flexibility comes at a cost
Sabbagh, J. J., & Dickey, C. A. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00003 · Cited by 31
Self-citationAcute neuroinflammation induces AIS structural plasticity in a NOX2-dependent manner
Benusa, S. D., George, N. M., Sword, B. A., DeVries, G. H., & Dupree, J. L. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0889-3 · Cited by 31
The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer's disease
Qureshi, Y. H., Berman, D. E., Marsh, S. E., Klein, R. L., Patel, V. M., Simoes, S., Kannan, S., Petsko, G. A., Stevens, B., & Small, S. A. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110262 · Cited by 31
Chen, X., He, X., Sun, J., & Wang, Z. (2022) · Molecules · doi:10.3390/molecules27082420 · Cited by 30
Katsumata, Y., Nelson, P. T., Estus, S., & Fardo, D. W. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.10.017 · Cited by 30
Davtyan, H., Chen, W. W., Zagorski, K., Davis, J., Petrushina, I., Kazarian, K., Cribbs, D. H., Agadjanyan, M. G., Blurton-Jones, M., & Ghochikyan, A. (2017) · Vaccine · doi:10.1016/j.vaccine.2017.03.020 · Cited by 30
Circadian control of heparan sulfate levels times phagocytosis of amyloid beta aggregates
Clark, G. T., Yu, Y., Urban, C. A., Fu, G., Wang, C., Zhang, F., Linhardt, R. J., & Hurley, J. M. (2022) · PLOS Genetics · doi:10.1371/journal.pgen.1009994 · Cited by 31
Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model
Nishioka, C., Liang, H.-F., Barsamian, B., & Sun, S.-W. (2019) · NeuroImage · doi:10.1016/j.neuroimage.2019.01.007 · Cited by 30
Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity
Dworzak, J., Renvoisé, B., Habchi, J., Yates, E. V., Combadière, C., Knowles, T. P., Dobson, C. M., Blackstone, C., Paulsen, O., & Murphy, P. M. (2015) · PLOS ONE · doi:10.1371/journal.pone.0127730 · Cited by 30
Tikhonova, M. A., Amstislavskaya, T. G., Belichenko, V. M., Fedoseeva, L. A., Kovalenko, S. P., Pisareva, E. E., Avdeeva, A. S., Kolosova, N. G., Belyaev, N. D., & Aftanas, L. I. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0412-5 · Cited by 30
Rates of lobar atrophy in asymptomatic MAPT mutation carriers
Chen, Q., Boeve, B. F., Senjem, M., Tosakulwong, N., Lesnick, T. G., Brushaber, D., Dheel, C., Fields, J., Forsberg, L., Gavrilova, R., et al. (2019) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2019.05.010 · Cited by 28
Speech patterns during memory recall relates to early tau burden across adulthood
Young, C. B., Smith, V., Karjadi, C., Grogan, S., Ang, T. F. A., Insel, P. S., Henderson, V. W., Sumner, M., Poston, K. L., Au, R., et al. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13731 · Cited by 27
The Multifaceted Role of Neuroprotective Plants in Alzheimer’s Disease Treatment
Zieneldien, T., Kim, J., & Cao, C. (2022) · Geriatrics · doi:10.3390/geriatrics7020024 · Cited by 29
Sáez-Orellana, F., Leroy, T., Ribeiro, F., Kreis, A., Leroy, K., Lalloyer, F., Baugé, E., Staels, B., Duyckaerts, C., Brion, J.-P., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.150099 · Cited by 29
Bachstetter, A. D., Morganti, J. M., Bodnar, C. N., Webster, S. J., Higgins, E. K., Roberts, K. N., Snider, H., Meier, S. E., Nation, G. K., Goulding, D. S., et al. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113180 · Cited by 29
Multicenter 18F-PI-2620 PET for In Vivo Braak Staging of Tau Pathology in Alzheimer’s Disease
Rullmann, M., Brendel, M., Schroeter, M. L., Saur, D., Levin, J., Perneczky, R. G., Tiepolt, S., Patt, M., Mueller, A., Villemagne, V. L., et al. (2022) · Biomolecules · doi:10.3390/biom12030458 · Cited by 29
Modulation of L-type calcium channels in Alzheimer’s disease: A potential therapeutic target
Crossley, C. A., Rajani, V., & Yuan, Q. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.11.049 · Cited by 28
Tarawneh, R. (2023) · Biomolecules · doi:10.3390/biom13050830 · Cited by 29
Stone, D. B., Ryman, S. G., Hartman, A. P., Wertz, C. J., Vakhtin, A. A., & Initiative, A. D. N. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.711579 · Cited by 28
Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy
Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28
Experimental evidence for temporal uncoupling of brain Aβ deposition and neurodegenerative sequelae
Rother, C., Uhlmann, R. E., Müller, S. A., Schelle, J., Skodras, A., Obermüller, U., Häsler, L. M., Lambert, M., Baumann, F., Xu, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34538-5 · Cited by 28
Llibre-Guerra, J. J., Fernandez, M. V., Joseph-Mathurin, N., Bian, S., Carter, K., Li, Y., Aschenbrenner, A. J., Pottier, C., Sigurdson, W., McDade, E., et al. (2025) · Nature Medicine · doi:10.1038/s41591-025-03494-0 · Cited by 28
Xie, C., Miyasaka, T., Yoshimura, S., Hatsuta, H., Yoshina, S., Kage-Nakadai, E., Mitani, S., Murayama, S., & Ihara, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089796 · Cited by 28
Trojan, E., Tylek, K., Schröder, N., Kahl, I., Brandenburg, L.-O., Mastromarino, M., Leopoldo, M., Basta-Kaim, A., & Lacivita, E. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02543-2 · Cited by 26
Fernández Zapata, C., Giacomello, G., Spruth, E. J., Middeldorp, J., Gallaccio, G., Dehlinger, A., Dames, C., Leman, J. K. H., van Dijk, R. E., Meisel, A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34719-2 · Cited by 27
Lutz, B. M., & Peng, J. (2018) · Proteomes · doi:10.3390/proteomes6040046 · Cited by 27
Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice
Walker, C. K., Greathouse, K. M., Boros, B. D., Poovey, E. H., Clearman, K. R., Ramdas, R., Muhammad, H. M., & Herskowitz, J. H. (2021) · Neuroscience · doi:10.1016/j.neuroscience.2020.12.006 · Cited by 27
Metadata
- Authors
- Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D.
- Affiliations
- University of South Florida (US)
- Venue
- Neurodegenerative Diseases
- Publisher
- S. Karger AG
- Published
- 2012-07-10
- Volume
- 11
- Issue
- 4
- Pages
- 165-181
- ISSN
- 1660-2854 (ISSN-L)
- 1660-2862
- PMC
- PMC3739054
- OpenAlex
- W2082429191
- Cited by
- 10,359
- References
- 186
- Citations by year
- 2026: 7 · 2025: 280 · 2024: 673 · 2023: 878 · 2022: 924 · 2021: 753 · 2020: 704 · 2019: 697 · 2018: 812 · 2017: 836 · 2016: 793 · 2015: 823 · 2014: 330 · 2013: 215 · 2012: 191
- FWCI
- 334.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Neurodegenerative Diseases (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (AG 15490, R01AG015490, R29AG010282)
- National Institute of Neurological Disorders and Stroke (R01NS030352, NS76308, R01NS076308, R01NS073899)
- National Center for Research Resources (S10RR025633)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta oligomers, tau phosphorylation, tauopathy, glycogen synthase kinase-3, rTg4510 mice, microglial activation, astrocyte activation, hippocampus, Alzheimer's disease
- MeSH terms
- CD68 Molecule, Animals, Disease Models, Animal, Hippocampus, Mice, Transgenic, Neurons, Peptide Fragments, Phosphorylation, Antigens, Differentiation, Myelomonocytic, Antigens, CD, Amyloid beta-Peptides, tau Proteins, Leukocyte Common Antigens, Microglia, Tauopathies, Glycogen Synthase Kinase 3, Mice
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