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Cell-Cycle Reentry and Cell Death in Transgenic Mice Expressing Nonmutant Human Tau Isoforms
Open accessAbstract
Mutations in the microtubule-associated protein tau gene have been linked to neurofibrillary tangle (NFT) formation in several neurodegenerative diseases known as tauopathies; however, no tau mutations occur in Alzheimer's disease, although this disease is also characterized by NFT formation and cell death. Importantly, the mechanism of tau-mediated neuronal death remains elusive. Aged mice expressing nonmutant human tau in the absence of mouse tau (htau mice) developed NFTs and extensive cell death. The mechanism of neuron death was investigated in htau mice, and surprisingly, the presence of tau filaments did not correlate directly with death within individual cells, suggesting that cell death can occur independently of NFT formation. Our observations show that the mechanism of neurodegeneration involved reexpression of cell-cycle proteins and DNA synthesis, indicating that nonmutant tau pathology and neurodegeneration may be linked via abnormal, incomplete cell-cycle reentry.
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“However, neuronal loss appears to be independent of tangle formation in some transgenic mouse models (12)(13)(14).”
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Items 301–400 of 466
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Lo, C. H., & Sachs, J. N. (2020) · JoLS Journal of Life Sciences · doi:10.36069/jols/20201201 · Cited by 15
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Endogenous Tau Aggregates in Oligodendrocytes of rTg4510 Mice Induced by Human P301L Tau
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Modèles animaux des maladies neuro-dégénératives
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Tangles and Plaques: A deep dive into the pathological hallmarks of Alzheimer’s disease
Vanya, Kumari, S., Bagri, K., & Deshmukh, R. R. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.10.050 · Cited by 18
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“Additionally, mice overexpressing the mutant microtubule-associated protein tau ( MAPT ) develop AD-like pathology of neurofibrillary tangles in neurons (tauop-athy) (Andorfer et al., 2005; Goedert et al., 2017; McGowan et al., 2006).”
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Sivanantharajah, L., & Mudher, A. K. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.903119 · Cited by 22
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MethodWobst, H. J., Denk, F., Oliver, P., Livieratos, A., Taylor, T. N., Knudsen, M. H., Bengoa-Vergniory, N., Bannerman, D., & Wade-Martins, R. (2017) · Scientific Reports · doi:10.1038/srep43198 · Cited by 17
Pin1 inhibition activates cyclin D and produces neurodegenerative pathology
Atabay, K. D., & Karabay, A. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07259.x · Cited by 17
“Various causes have been linked to neurodegenerative cell cycle dysregulation process, such as excess amount of mitogenic signals (Yang and Herrup 2007), changes in microtubule dynamics (Andorfer et al. 2005), CNS injury (Stoica et al.”
BackgroundSex effects of Interleukin-6 deficiency on neuroinflammation in aged C57Bl/6 mice
Miller, V. M., Lawrence, D. A., Coccaro, G. A., Mondal, T. K., Andrews, K., Dreiem, A., & Seegal, R. F. (2010) · Brain Research · doi:10.1016/j.brainres.2009.12.091 · Cited by 17
“…we quantified markers directed against; glial-fibrillary acidic protein (GFAP), lipid peroxidation (MDA), IFNγ; a cytokine regulated by IL-6, myelin-basic protein (MBP) and SNAP25, a synaptic protein in mid age (18 month) and old age (24 months) IL-6−/− and WT C57Bl/6 mice [Andorfer et al. 2005].”
MethodBowles, K. R., Pedicone, C., Pugh, D. A., Oja, L.-M., Sousa, F. H., Keavey, L. K., Fulton-Howard, B., Weitzman, S. A., Liu, Y., Chen, J. L., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115013 · Cited by 20
“47 In contrast, increased MAPT exon 10 PSI was significantly associated with downregulation of glutamate receptor signaling and ion channel activity (Figure 5G), indicating that in astrocytes, increased exon 10 inclusion may be interfering with neuronal-glial cellular signaling and communication.”
Gamache, J., Kemper, L. J., Steuer, E. L., Leinonen-Wright, K., Choquette, J. M., Hlynialuk, C. J. W., Benzow, K. A., Vossel, K. A., Xia, W., Koob, M. D., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1256-19.2019 · Cited by 19
“, 2009), neurodegeneration (Andorfer et al., 2005), progressive tauopathy (Ishihara et al.”
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“These implicated calcium signaling dysregulation, mitochondrial dysfunction, cell cycle reentry, and insulin signaling as pathogenic [4–9].”
Self-citationRodriguez, L., Mdzomba, J. B., Joly, S., Boudreau-Laprise, M., Planel, E., & Pernet, V. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00293 · Cited by 16
“Indeed, it has been shown that replacing murine Tau by hTau induced NFTs and cell death in the enthorinal cortex and in the hippocampus of so-called hTau transgenic mice (Andorfer et al., 2003; Andorfer, 2005).”
BackgroundInfluentialLlorens-Martı́n, M., Hernández, F., & Ávila, J. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.08.057 · Cited by 13
“In addition, alterations to tau involving increase in its expression (Andorfer et al., 2005), modification by phosphorylation (Alonso et al.”
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Self-citationConditionally inducible tau mice – designing a better mouse model of neurodegenerative diseases
Janus, C. (2008) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00375.x · Cited by 16
“Interestingly, pathological analysis of these mice showed that the number of NFTs did not correlate directly with observed cell death, strongly suggesting that cell death occurred independent of the observed accumulation of hyperphosphorylated tau (Andorfer et al. 2005).”
BackgroundZhu, K., Pieber, M., Han, J., Blomgren, K., Zhang, X., Harris, R. A., & Lund, H. (2020) · Glia · doi:10.1002/glia.23794 · Cited by 16
“However, we did not detect any difference in soluble oligomers between depleted and nondepleted hTau mice (Figure 4e). hTau mice develop more severe pathology with age, leading to accumulation of neurofibrillary tangles by 15 months (Andorfer et al., 2003, 2005).”
BackgroundOjo, J. O., Crynen, G. C., Algamal, M., Vallabhaneni, P., Leary, P., Mouzon, B., Reed, J. M., MULLAN, M. J., & Crawford, F. (2020) · ASN NEURO · doi:10.1177/1759091420914768 · Cited by 12
“The distribution and pathology of hyperphosphorylation, aggregation of paired helical filaments, and neurofibrillary tangles in these mice develops in an age-dependent manner and is evident 9 to 15 months of age (Andorfer et al., 2003; Andorfer, 2005; Polydoro et al., 2009).”
Ojo, J. O., Crynen, G. C., Reed, J. M., Ajoy, R., Vallabhaneni, P., Algamal, M., Leary, P., Rafi, N. G., Mouzon, B., MULLAN, M. J., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00405 · Cited by 13
Untangling the role of tau in Alzheimer’s disease: A unifying hypothesis
Bhatia, N. S., & Hall, G. F. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0114-5 · Cited by 11
“Many of these kinases have also been shown to play important roles in regulating mitotic activity and/or early stages of neuronal differentiation [131,155-158].”
BackgroundTherapeutic Targets in Alzheimer's Disease and Related Tauopathies
Corbo, C. P., & Alonso, A. D. C. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385506-0.00002-8 · Cited by 13
Hyperphosphorylated Tau Inflicts Intracellular Stress Responses that Are Mitigated by Apomorphine
Song, Z., Wang, K., Hagar, H. C., Chen, H., Kuan, C.-Y., Zhang, K., & Kuo, M. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03689-x · Cited by 23
“While neurofibrillary tangles are a conspicuous pathological characteristic of AD and tauopathies, accumulating evidence argues against a causal role of these large tau conformers in neurodegeneration.”
Sinnige, T., Stroobants, K., Dobson, C. M., & Vendruscolo, M. (2020) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583520000025 · Cited by 18
“The mice suffer significant neuronal loss at old age, between 8 and 18 months, but the majority of dying neurons does not appear to contain fibrillar aggregates (Andorfer et al., 2005).”
BackgroundIn Vivo Validation of a Small Molecule Inhibitor of Tau Self-Association in htau Mice
Davidowitz, E. J., Krishnamurthy, P., Lopez, P. L. D. C., Jimenez, H. T., Adrien, L. R., Davies, P., & Moe, J. G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190465 · Cited by 18
“The result that the male htau mice developed significantly more tau pathology than the females at the end of the study was unexpected as the initial characterization of the htau model did not indicate sex-based differences [11, 36].”
MethodResultSelf-citationExpression, phosphorylation, localization, and microtubule binding of tau in colorectal cell lines
Huda, M. N., Kim, D. H., Erdene-Ochir, E., Kim, Y. S., & Pan, C. (2016) · Applied Biological Chemistry · doi:10.1007/s13765-016-0228-x · Cited by 14
“…Korea University of Science and Technology (UST), Daejeon 34113, Republic of Korea 3 Department of Biomedical Laboratory Science, College of Health Sciences Yonsei University, Wonju 26493, Republic of Korea anomalous tau responsible for the imperfect cell cycle reentry (Andorfer et al. 2005).”
BackgroundUnderly, R. G., Song, M.-S., Dunbar, G. L., & Weaver, C. L. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00259 · Cited by 10
“…conformational change (Alz-50) and specific phosphorylations of tau protein (CP13; phospho-Serine 202) have been shown to label pre-tangle neurons; and therefore, are suitable markers of early signs of Alzheimer’s degeneration (Jicha et al., 1997; Weaver et al., 2001; Andorfer et al., 2003, 2005).”
BackgroundAxonal transport rates in vivo are unaltered in htau mice
Yuan, A., Kumar, A. R., Sasaki, T., Duff, K., & Nixon, R. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-130671 · Cited by 13
“Some retinal ganglion cell neurons also showed perikaryal redistribution and aggregation of tau as previously reported in the brain [17, 22].”
Self-citationTau Protein: Function and Pathology
Rosenmann, H., Blum, D. L., Kayed, R., & Ittner, L. M. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/707482 · Cited by 12
Hypoxic ischemia and proteasome dysfunction alter tau isoform ratio by inhibiting exon 10 splicing
Suh, J., Im, D. S., Moon, G. J., Ryu, K.-S., de Silva, R., Choi, I. S., Lees, A. J., Guénette, S. Y., Tanzi, R. E., & Gwag, B. J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06732.x · Cited by 13
Yetman, M. J., Fowler, S., & Jankowsky, J. L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153724 · Cited by 14
“We tested mice at 13–14 months of age because htau mice had been reported to develop somatodendritic CP13- and PHF1-positive pre-tangles by this age that would serve as a reference for any change in severity with the addition of Aβ [16, 41, 42].”
BackgroundHe, Z. (2009) · Current Neurovascular Research · doi:10.2174/156720209787466055 · Cited by 9
Effects of Cell Cycle Inhibitors on Tau Phosphorylation in N2aTau3R Cells
Conejero-Goldberg, C., Townsend, K. P., & Davies, P. (2008) · Journal of Molecular Neuroscience · doi:10.1007/s12031-008-9044-z · Cited by 12
“Reappearance of cell cycle proteins has been reported in neurons exhibiting tau aggregation, suggesting that an aberrant cell cycle occurs before neurons die (Andorfer et al. 2005).”
BackgroundSelf-citationCytoplasmic cytochrome c immunolabelling in dystrophic neurites in Alzheimer’s disease
Woodhouse, A., Vickers, J. C., & Dickson, T. C. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0107-3 · Cited by 13
Therapeutic Approaches for the Treatment of Alzheimer's Disease: An Overview
Lau, L., & Brodney, M. A. (2007) · Springer eBooks · doi:10.1007/7355_2007_017 · Cited by 8
Gao, Y., Wang, Y., Lei, H., Xu, Z., Li, S., Yu, H., Xie, J., Zhang, Z., Liu, G., Zhang, Y., et al. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00379-5 · Cited by 13
“…[12]; (2) Tg mice with expression of full-length WT or mutant hTau in the absence of endogenous murine tau, such as the hTau line (JAX005491) [13–15]; and (3) mice with expression of WT or mutant full-length hTau under the induction of tetracycline, such as rTg4510 (CaMK2a:P301L) [16] and…”
BackgroundDavidowitz, E. J., Lopez, P., Jimenez, H. T., Adrien, L. R., Davies, P., & Moe, J. G. (2023) · PLoS ONE · doi:10.1371/journal.pone.0286523 · Cited by 13
“3-repeat tau isoforms are relatively more abundant in the htau model [20].”
Self-citationMitotic phosphorylation of Tau/MAPT modulates cell cycle progression in prostate cancer cells
Clementi, L., Sabetta, S., Zelli, V., Compagnoni, C., Tessitore, A., Mattei, V., & Angelucci, A. (2023) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-023-04721-2 · Cited by 11
“Conversely, forced expression of non-mutant human Tau in mouse model was associated with the aberrant appearance of cell-cycle and the initiation of DNA synthesis (Andorfer et al. 2005).”
BackgroundAndrés‐Benito, P., Carmona, M., Jordán, M., Fernández‐Irigoyen, J., Santamaría, E., del Rı́o, J. A., & Ferrer, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020718 · Cited by 14
“33,34; MAPT transgene is driven by a tau promoter that causes these mice to over-express human 3Rtau and 4Rtau in the absence of endogenous mouse Mapt) [27,28].”
BackgroundMethodInfluentialThe NLRP3 Inflammasome in the Pathogenesis and Treatment of Alzheimer’s Disease
Golzari-Sorkheh, M., Brown, C. E., Weaver, D. F., & Reed, M. A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210660 · Cited by 21
Expression of 1N3R-Tau Isoform Inhibits Cell Proliferation by Inducing S Phase Arrest in N2a Cells
Li, L., Xu, Z., Liu, G., Xu, C., Wang, Z.-H., Li, X., Liu, E.-J., Zeng, J., Chai, D., Yao, W., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119865 · Cited by 9
Plant-based vaccines for Alzheimer's disease: an overview
Rosales‐Mendoza, S., Rubio‐Infante, N., Zarazúa, S., Govea‐Alonso, D. O., Martel‐Gallegos, G., & Moreno‐Fierros, L. (2014) · Expert Review of Vaccines · doi:10.1586/14760584.2014.874948 · Cited by 11
“Similar results have been observed in the following models: the transgenic rat model of Tauopathy [75]; mice expressing the six human tau isoforms on an (microtubule-associated protein tau) MAPT/ background, a mice model for human tau pathology [76]; and the PS1-M146L mice mutant model [74].”
ResultEyes on the prize: Federal Alzheimer's research effort aims to facilitate interventions
Hodes, R. J., Buckholtz, N. S., Cahan, V., & Morrison‐Bogorad, M. (2007) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2007.11.002 · Cited by 9
Role of WWOX WOX1 in Alzheimer s disease pathology and in cell death signaling
Teng, C.-C. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s358 · Cited by 22
Advances in our Understanding of Neurodegeneration
Jellinger, K. A. (2007) · Elsevier eBooks · doi:10.1016/b978-044452809-4/50142-3 · Cited by 9
Castle (2016) · doi:10.1007/978-1-4939-3271-9 · Cited by 10
Singhaarachchi, P. H., Antal, P., Calon, F., Culmsee, C., Delpech, J.-C., Feldotto, M., Geertsema, J., Hoeksema, E. E., Kőrösi, A., Layé, S., et al. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102821 · Cited by 13
The Role of Aβ and Tau Oligomers in the Pathogenesis of Alzheimer’s Disease
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Alzheimers Disease: Review of Emerging Treatment Role for Intravenous Immunoglobulins
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Animal Models for the Study of Human Neurodegenerative Diseases
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Mammalian Models in Alzheimer’s Research: An Update
Sharma, H., Chang, K., Hulme, J., & An, S. S. A. (2023) · Cells · doi:10.3390/cells12202459 · Cited by 12
“hTau-These mouse models were developed by crossing 8c mice (mice that express tau trans-gene derived from human PAC, H1 haplotype) [82] with tau exon 1 knockout mice [83,84].”
BackgroundMethodThe toxin MPTP generates similar cognitive and locomotor deficits in hTau and tau knock-out mice
Gratuze, M., Josset, N., Petry, F. R., Pflieger, M., Jong, L. E., Truchetti, G., Poitras, I., Julien, J., Bezeau, F., Morin, F., et al. (2019) · Brain Research · doi:10.1016/j.brainres.2019.01.016 · Cited by 10
Kallhoff, V., Hu, L., Chen, X., Pautler, R. G., & Zheng, H. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2873-08.2008 · Cited by 13
“This phenomenon, termed cell cycle events (CCEs), has also been replicated in AD mouse models with amyloid or tau pathologies (Andorfer et al., 2005; Yang et al., 2006).”
BackgroundNormal and Abnormal Tau Neurobiology
Duff, K. (2006) · Alzheimer Disease & Associated Disorders · doi:10.1097/01.wad.0000213881.01289.d9 · Cited by 7
Self-citationOptical Coherence Tomography in Alzheimer’s Disease
Coppola, G., Parisi, V., Manni, G., Pierelli, F., & Sadun, A. A. (2016) · Springer eBooks · doi:10.1007/978-3-319-24085-5_7 · Cited by 2
Gratuze, M., Joly‐Amado, A., Buée, L., Vieau, D., & Blum, D. L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_21 · Cited by 8
Maphis, N. M., Hulse, J. P., Peabody, J., Dadras, S., Whelpley, M. J., Kandath, M., Wilson, C. M., Hobson, S., Thompson, J., Poolsup, S., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70101 · Cited by 10
Li, S., Roy, E. R., Wang, Y., Watkins, T. A., & Cao, W. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03720-1 · Cited by 14
“AD and tauopathies are associated with numerous nuclear irregularities, which include excessive DNA damage [51, 52], altered DNA repair [27, 53], cell cycle re-entry [25, 54], chromosomal defects [55] and senescence [56, 57].”
Benskey, M. J., Panoushek, S., Saito, T., Saido, T. C., Grabinski, T. M., & Kanaan, N. M. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1265151 · Cited by 13
Ferrer, I., Andrés‐Benito, P., Carmona, M., & del Rı́o, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415940 · Cited by 10
Constant Levels of Tau Phosphorylation in the Brain of htau Mice
Neddens, J., Daurer, M., Loeffler, T., Aldamizetxebarria, S. A., Flunkert, S., & Hutter-Paier, B. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00136 · Cited by 8
de Gérando, A. M., Khasnavis, A., Welikovitch, L. A., Bhavsar, H., Glynn, C. A., Quittot, N., Perbet, R., & Hyman, B. T. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01849-1 · Cited by 6
“Previous studies showed that hTau mice develop spontaneous tau hyperphosphorylation by 6 months and tau aggregates by 13 months of age [3, 5].”
BackgroundSharallah, O. A., Poddar, N. K., & Alwadan, O. A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102394 · Cited by 7
Emmerson, J. T., Malcolm, J. C., Carmo, S. D., Nguyen, P., Breuillaud, L., Martínez-Trujillo, J., & Cuello, A. C. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106317 · Cited by 11
Diagnostic and therapeutic targeting of pathological tau proteins in neurodegenerative disorders
Sahara, N., & Higuchi, M. (2023) · FEBS Open Bio · doi:10.1002/2211-5463.13711 · Cited by 9
Hyperphosphorylated tau Inflicts Intracellular Stress Responses That Are Mitigated by Apomorphine
Song, Z., Wang, K.-W., Hagar, H., Chen, H.-R., Kuan, C., Zhang, K.-Z., & Kuo, M.-H. (2023) · bioRxiv · doi:10.1101/2023.05.13.540661 · Cited by 7
“7 correlate directly with cell death[27].”
Tau Loss of Function, by Deletion or Aggregation, Contributes to Peripheral Insulin Resistance
Al‐Lahham, R., & Méndez, N. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230392 · Cited by 13
Current Conceptual View of Alzheimer’s Disease
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Sieradzki, A., Yendluri, B. B., Palacios, H. H., Parvathaneni, K., Reddy, V. P., Obrenovich, M. E., Gąsiorowski, K., Leszek, J., & Aliev, G. M. (2011) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152711794480410 · Cited by 7
“It was observed in transgenic mice expressing nonmutant human tau isoforms that the mechanism of neurodegeneration involved reexpression of cell-cycle proteins and DNA synthesis, indicating that nonmutant tau pathology and neurodegeneration may be linked via abnormal, incomplete cell-cycle reentry [1].”
BackgroundCell cycle proteins preceded neuronal death after chronic cerebral hypoperfusion in rats
Xu, L.-G., Di, Q., & Zhang, Y.-D. (2008) · Neurological Research · doi:10.1179/174313208x327937 · Cited by 7
A long trek down the pathways of cell death in Alzheimer's disease
Davies, P. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9s329 · Cited by 7
“Details of the pathology that develops in these mice have been published [39,40], but most notable was the extensive cortical neuronal loss, which exceeded 50% in the piriform cortex.”
Self-citationThe Biology and Pathobiology of Tau Protein
Hall, G. F. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-788-0_15 · Cited by 6
Bukhari, H., Nithianandam, V., Battaglia, R. A., Cicalo, A., Sarkar, S., Comjean, A., Hu, Y.-H., Leventhal, M., Dong, X.-J., & Feany, M. (2024) · bioRxiv · doi:10.1101/2024.02.02.578624 · Cited by 6
“Inappropriate neuronal cycle reentry is a feature of human tauopathy (Husseman et al. 2000) and human tau transgenic animals (Andorfer et al. 2005; Khurana et al. 2006).”
Tau Fibrillation Induced by Heparin or a Lysophospholipid Show Different Initial Oligomer Formation
Rasmussen, H. Ø., Nielsen, J., de Poli, A., Otzen, D. E., & Pedersen, J. S. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168194 · Cited by 7
Zhou, Z., Bai, J., Zhong, S., Zhang, R., Kang, K., Zhang, X., Xu, Y., Zhao, C., & Zhao, M. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/5552623 · Cited by 9
“This unscheduled event in turn facilitates Aβ toxicity and tau hyperphosphorylation, thus to the formation of AD neuropathology [9, 10].”
BackgroundIs tau a suitable therapeutical target in tauopathies?
de Barreda, E. G. (2010) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v1.i5.81 · Cited by 5
Diaz-Corrales, F. J. J., Asanuma, M., Miyazaki, I., Miyoshi, K., Hattori, N., & Ogawa, N. (2008) · Neurotoxicity Research · doi:10.1007/bf03033854 · Cited by 8
“There is ample evidence of dysregulation of cell cycle-regulatory proteins and aberrant neuronal cell-cycle reentry in neurodegenerative disorders including PD (Husseman et al., 2000; El-Khodor et al., 2003; Lee et al., 2003; Andorfer et al., 2005).”
BackgroundAkhter, F., Akhter, A., & Ahmad, S. (2017) · Environmental science and engineering · doi:10.1007/978-3-319-46248-6_5 · Cited by 5
Immunotherapy and Biomarkers in Neurodegenerative Disorders
Ingelsson, M., & Lannfelt, L. (2016) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-3560-4 · Cited by 6
“It is now important to clarify if and how effi cacy versus toxicity of the tau antibodies or immunogen depend on: (1) which epitope(s) are being targeted; (2) affi nity/avidity towards the target; (3) targeting single versus multiple epitopes; (4) the isotype of the antibody; (5) whole antibody versus antibody fragmen…”
BackgroundInfluentialMolecular Aspects of Memory Dysfunction in Alzheimer’s Disease
Chin, J., Roberson, E. D., & Mucke, L. (2008) · Elsevier eBooks · doi:10.1016/b978-012370509-9.00015-2 · Cited by 5
Hagar, H. C., Fernández-Vega, V., Wang, K., Jordan, L. M. O., Shumate, J., Scampavia, L. D., Tapayan, A. S., Nguyen, H. M., Spicer, T., & Kuo, M. (2025) · SLAS DISCOVERY · doi:10.1016/j.slasd.2025.100235 · Cited by 6
Effects of heterologous human tau protein expression in yeast models of proteotoxic stress response
Zubčić, K., Franić, D., Pravica, M., Hof, P. R., Šimić, G., & Boban, M. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14304 · Cited by 5
“7– 9 Accordingly, tau oligomers were found elevated in post-mortem samples of the AD brain.”
BackgroundSelf-citationPlasma MicroRNAs Are Altered Early and Consistently in a Mouse Model of Tauopathy.
Ryan, B., Williams, J. M., & Curtis, M. (2019) · Neuroscience · doi:10.1016/j.neuroscience.2019.05.036 · Cited by 5
Więdłocha, M., Stańczykiewicz, B., Jakubik, M., & Rymaszewska, J. (2012) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/17322693.1001098 · Cited by 5
“Badacze skłaniają się raczej ku temu, że śmierć komórek jest spowodowana przez utratę funkcji zmutowanego białka tau, co znajduje potwierdzenie w wynikach badań GomezIsla i wsp., którzy stwierdzili, że do utraty neuronów może dochodzić przy nieobecności NFT [6,55].”
InfluentialKanaan, N. M., Himmelstein, D. S., Ward, S., Combs, B., & Binder, L. I. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00056-1 · Cited by 9
Neurofibrillary Tangle Formation as a Protective Response to Oxidative Stress in Alzheimer’s Disease
Nunomura, A., Takeda, A., Moreira, P. I., Castellani, R. J., Lee, H., Zhu, X., Smith, M. A., & Perry, G. L. (2009) · Springer eBooks · doi:10.1007/978-0-387-87995-6_9 · Cited by 3
Metadata
- Authors
- Andorfer, C., Acker, C. M., Kress, Y., Hof, P. R., Duff, K., & Davies, P.
- Affiliations
- Albert Einstein College of Medicine (US)
- Icahn School of Medicine at Mount Sinai (US)
- Nathan Kline Institute for Psychiatric Research (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2005-06-01
- Volume
- 25
- Issue
- 22
- Pages
- 5446-5454
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6725006
- OpenAlex
- W2016758992
- Cited by
- 511
- References
- 74
- Citations by year
- 2026: 9 · 2025: 12 · 2024: 10 · 2023: 28 · 2022: 18 · 2021: 16 · 2020: 26 · 2019: 17 · 2018: 20 · 2017: 20 · 2016: 17 · 2015: 22 · 2014: 29 · 2013: 25 · 2012: 26
- FWCI
- 20.26
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (38623)
- National Institute on Aging (R37AG022102, AG022102, R01AG022102)
- National Institute of Mental Health (38623)
- 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 › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- tau protein, cell cycle re-entry, neuronal cell death, neurofibrillary tangles, tauopathy, Alzheimer's disease, transgenic mice, neurodegeneration, DNA synthesis, tau filaments
- MeSH terms
- Aging, Animals, Brain, Bromodeoxyuridine, Cell Cycle, Humans, Mice, Transgenic, Nerve Degeneration, Nerve Tissue Proteins, Neurons, Neurofibrillary Tangles, tau Proteins, Cell Death, Protein Isoforms, Mice, DNA Fragmentation
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