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Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
Open accessAbstract
Neurofibrillary tangles (NFTs) are composed of abnormal aggregates of the cytoskeletal protein tau. Together with amyloid β (Aβ) plaques and neuronal and synaptic loss, NFTs constitute the primary pathological hallmarks of Alzheimer disease (AD). Recent evidence also suggests that caspases are activated early in the progression of AD and may play a role in neuronal loss and NFT pathology. Here we demonstrate that tau is cleaved at D421 (ΔTau) by executioner caspases. Following caspase-cleavage, ΔTau facilitates nucleation-dependent filament formation and readily adopts a conformational change recognized by the early pathological tau marker MC1. ΔTau can be phosphorylated by glycogen synthase kinase-3β and subsequently recognized by the NFT antibody PHF-1. In transgenic mice and AD brains, ΔTau associates with both early and late markers of NFTs and is correlated with cognitive decline. Additionally, ΔTau colocalizes with Aβ1–42 and is induced by Aβ1–42 in vitro. Collectively, our data imply that Aβ accumulation triggers caspase activation, leading to caspase-cleavage of tau, and that this is an early event that may precede hyperphosphorylation in the evolution of AD tangle pathology. These results suggest that therapeutics aimed at inhibiting tau caspase-cleavage may prove beneficial not only in preventing NFT formation, but also in slowing cognitive decline.
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“This is consistent with the observation that C-terminal truncated forms of Tau show increased polymerization capacity in vitro and are associated with NFTs formation in the brain of AD patients (Gamblin et al., 2003; Rissman et al., 2004).”
From Emerging Alternative Proteinases in APP Metabolism and Alzheimer’s Disease Pathogenesis: A Focus on MT1-MMP and MT5-MMP (2019) · cites this paper as Rissman et al., 2004
In the citing paper
“Δtau levels were below the detectable level in our 7-month-old, untreated 3xTg-AD mice”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Rissman et al., 2004
In the citing paper
“Recent evidence suggests that executioner caspases 3 and 7 may contribute to tau, the protein responsible for forming NFTs, pathology by cleaving tau after Asp421 to yield a cytotoxic Δtau fragment (Rissman et al., 2004; Rohn et al., 2008; de Calignon et al., 2010).”
From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Rissman et al., 2004
In the citing paper
“only caspase-2, 3 and 6 cleaved tau products have been linked to AD [190–193].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [192]
In the citing paper
“Although tau can be cleaved by caspase-1, 2, 3, 6 and 7 in vitro”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [192]
In the citing paper
“Tau-421 colocalizes with NFTs in human AD brain, and correlates with NFT formation and cognitive impairment in aged mice [191, 192, 194].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [192]
In the citing paper
“Elevated levels of caspase-3 and tau-421 have been observed in AD, as well as PSP [130, 191, 192].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [192]
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Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673
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
Mild Cognitive Impairment: Clinical Characterization and Outcome
Petersen, R. C., Smith, G. E., Waring, S. C., Ivnik, R. J., Tangalos, E. G., & Kokmen, E. (1999) · Archives of Neurology · doi:10.1001/archneur.56.3.303 · Cited by 8,980
Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
Self-citationLee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,142
Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.
Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526
Research works printed but not linked: 1
- Yang, 1998, Am. J. Pathol., 152, 379
Cited by
Sorted by citations
Items 301–400 of 544
Elsonbaty, S. M., & Ismail, A. F. M. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108382 · Cited by 32
Luna‐Muñoz, J., Charles, R., Claude, M., Flores-Rodríguez, P., Ávila, J., Sergio, R., de la Cruz, F., Mena, R., Meraz‐Ríos, M. A., & Florán, B. (2013) · InTech eBooks · doi:10.5772/54228 · Cited by 43
Ávila, J. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.157 · Cited by 33
Yang, J., Shen, N., Shen, J., Yang, Y., & Li, H.-L. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03867-x · Cited by 32
Spencer, B. J., Brüschweiler, S., Sealey‐Cardona, M., Rockenstein, E. M., Adame, A., Florio, J. B., Mante, M., Trinh, I., Rissman, R. A., Konrat, R., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1869-0 · Cited by 30
Self-citationKLVFF peptide functionalized nanoparticles capture Aβ42 by co-assembly for decreasing cytotoxicity
Yang, P., Yang, C., Zhang, K., Wang, L., & Wang, H. (2018) · Chinese Chemical Letters · doi:10.1016/j.cclet.2018.10.003 · Cited by 29
Wu, B.-K., Yuan, R.-Y., Lien, H.-W., Hung, C., Hwang, P., Chen, R. P.-Y., Chang, C., Liao, Y., & Huang, C. (2016) · Journal of Biomedical Science · doi:10.1186/s12929-016-0237-4 · Cited by 29
Ding, H., & Johnson, G. V. W. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14413 · Cited by 29
Martin, S. P., & Leeman-Markowski, B. A. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2023.1287545 · Cited by 30
Ayala‐Grosso, C. A., Tam, J. P., Roy, S., Xanthoudakis, S., Costa, D. D., Nicholson, D. W., & Robertson, G. S. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.04.041 · Cited by 28
Sillen, A., Wieruszeski, J., Leroy, A., Younes‐Chennoufi, A. B., Landrieu, I., & Lippens, G. M. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0516211 · Cited by 31
Song, H., Liu, J., Wang, L., Hu, X., Li, J., Zhu, L., Pang, R., & Zhang, A. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1348844 · Cited by 26
Ludvigson, A. E., Luebke, J. I., Lewis, J. M., & Peters, A. (2010) · Brain Structure and Function · doi:10.1007/s00429-010-0295-4 · Cited by 27
Studying tauopathies in Drosophila: A fruitful model
Sun, M., & Chen, L. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.03.029 · Cited by 27
Quantitative and combinatory determination of in situ phosphorylation of tau and its FTDP-17 mutants
Kimura, T., Hosokawa, T., Taoka, M., Tsutsumi, K., Ando, K., Ishiguro, K., Hosokawa, M., Hasegawa, M., & Hisanaga, S. (2016) · Scientific Reports · doi:10.1038/srep33479 · Cited by 28
Girling, K., Demers, M., Lainé, J., Zhang, S., Wang, Y. T., & Graham, R. K. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24153 · Cited by 26
Ellis, M. J., Lekka, C., Holden, K. L., Tulmin, H., Seedat, F., O'Brien, D. P., Dhayal, S., Zeissler, M., Knudsen, J. G., Kessler, B. M., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02729-7 · Cited by 26
Post-Translational Modifications in Alzheimer's Disease and the Potential for New Biomarkers
Russell, C. L., Končarević, S., & Ward, M. A. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132312 · Cited by 26
Halting of Caspase Activity Protects Tau from MC1-Conformational Change and Aggregation
Mead, E., Kestoras, D., Gibson, Y., Hamilton, L., Goodson, R. J., Jones, S., Eversden, S., Davies, P., O’Neill, M. J., Hutton, M. L., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150960 · Cited by 26
Aberrant septin 11 is associated with sporadic frontotemporal lobar degeneration
Gozal, Y. M., Seyfried, N. T., Gearing, M., Glass, J. D., Heilman, C. J., Wuu, J., Duong, D. M., Cheng, D., Xia, Q., Rees, H. D., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-82 · Cited by 26
Oxidation of thiol-proteases in the hippocampus of Alzheimer’s disease
Marcum, J. L., Mathenia, J. K., Chan, R., & Guttmann, R. P. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.06.089 · Cited by 26
HSV-1 cellular model reveals links between aggresome formation and early step of Alzheimer’s disease
Albaret, M. A., Textoris, J., Dalzon, B., Lambert, J., Linard, M., Helmer, C., Hacot, S., Ghayad, S. E., Ferréol, M., Mertani, H. C., et al. (2023) · Translational Psychiatry · doi:10.1038/s41398-023-02376-8 · Cited by 25
Tau accumulates in Crohn's disease gut
Prigent, A., Chapelet, G., de Lataillade, A. D. G., Oullier, T., Durieu, E., Bourreille, A., Duchalais, É., Hardonnière, K., Neunlist, M., Noble, W. J., et al. (2020) · The FASEB Journal · doi:10.1096/fj.202000414r · Cited by 25
The Significance of Tau Aggregates in the Human Brain
Castellani, R. J. (2020) · Brain Sciences · doi:10.3390/brainsci10120972 · Cited by 25
Maria Jose Perez, J., Ibarra‐García‐Padilla, R., Tang, M., Porter, G. A., Johnson, G. V. W., & Quintanilla, R. A. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166898 · Cited by 25
Sandhu, P., Naeem, M. M., Lu, C., Kumarathasan, P., Gomes, J., & Basak, A. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.11.087 · Cited by 25
Caspase-Mediated Truncation of Tau Potentiates Aggregation
Lee, S., & Shea, T. B. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731063 · Cited by 25
Olesen, M. A., Pradenas, E., Villavicencio-Tejo, F., Porter, G. A., Johnson, G. V. W., & Quintanilla, R. A. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.03.017 · Cited by 24
Hamano, T., Gendron, T. F., Ko, L., & Yen, S.-H. C. (2009) · Europe PMC (PubMed Central) · Cited by 24
Garringer, H. J., Murrell, J. R., Sammeta, N., Gnezda, A., Ghetti, B. F., & Vidal, R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056426 · Cited by 24
Biundo, F., d’Abramo, C., Tambini, M. D., Zhang, H., Prete, D. D., Vitale, F., Giliberto, L., Arancio, O., & D'adamio, L. (2017) · Translational Psychiatry · doi:10.1038/tp.2017.165 · Cited by 25
Aberrant role of ALK in tau proteinopathy through autophagosomal dysregulation
Park, J., Choi, H., Kim, Y. D., Kim, S.-H., Kim, Y., Gwon, Y., Lee, D. Y., Park, S., Heo, W. D., & Jung, Y. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-01003-y · Cited by 23
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
Alzheimer’s Disease—A Panorama Glimpse
Zhao, L. N., Lu, L., Chew, L. Y., & Mu, Y. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms150712631 · Cited by 23
Kimura, T., Hatsuta, H., Masuda‐Suzukake, M., Hosokawa, M., Ishiguro, K., Akiyama, H., Murayama, S., Hasegawa, M., & Hisanaga, S. (2015) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.10.009 · Cited by 23
Terron, H. M., Parikh, S. J., Abdul‐Hay, S. O., Sahara, T., Kang, D., Dickson, D. W., Säftig, P., LaFerla, F. M., Lane, S., & Leissring, M. A. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01443-6 · Cited by 22
Self-citationMustaly-Kalimi, S., Gallegos, W., Steinbrenner, D., Gupta, S. N., Houcek, A., Bennett, D. A., Marr, R. A., Peterson, D. A., Sekler, I., & Stutzmann, G. E. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02023-x · Cited by 25
Nanobiotechnology in Neurodegenerative Diseases
Jampílek, J., Kráľová, K., Novák, P., & Novák, M. (2019) · Springer eBooks · doi:10.1007/978-3-030-30930-5_4 · Cited by 22
Targeting Tau to Treat Clinical Features of Huntington's Disease
Masnata, M., Salem, S., Jacquet, A. D. R., Anwer, M., & Cicchetti, F. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.580732 · Cited by 25
Kelliny, S., Lin, L., Deng, I. B., Xiong, J., Zhou, F. H., Al‐Hawwas, M., Bobrovskaya, L., & Zhou, X. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02338-5 · Cited by 23
Theofilas, P., Piergies, A. M. H., Oh, I. M., Lee, Y. B., Li, S. H., Pereira, F. L., Petersen, C., Ehrenberg, A. J., Eser, R. A., Ambrose, A. J., et al. (2022) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12819 · Cited by 22
Olesen, M. A., & Quintanilla, R. A. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03434-4 · Cited by 23
Catalina, M. O., Bermejo, M. C., Argent, R., Alonso, J. C., Centeno, F., & Lorenzo, M. J. V. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.11.004 · Cited by 23
Kelliny, S., Zhou, X., & Bobrovskaya, L. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70046 · Cited by 27
Magnetic Fields Reduce Apoptosis by Suppressing Phase Separation of Tau-441
Lin, W.-J., Shi, W., Ge, W., Chen, L., Guo, W., Shang, P., & Yin, D. (2023) · Research · doi:10.34133/research.0146 · Cited by 21
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25
Role of caspase‐3 in tau truncation at D421 is restricted in transgenic mouse models for tauopathies
Zhang, Q., Zhang, X., Chen, J., Miao, Y., & Sun, A. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05959.x · Cited by 21
Movassat, J., Delangre, E., Liu, J., Gu, Y., & Janel, N. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00649 · Cited by 21
Ávila, J. (2009) · Frontiers in Aging Neuroscience · doi:10.3389/neuro.24.001.2009 · Cited by 23
Means, J. C., Lopez, A. A., & Koulen, P. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00859-6 · Cited by 20
Activity-dependent tau cleavage by caspase-3 promotes neuronal dysfunction and synaptotoxicity
Opland, C. K., Bryan, M. R., Harris, B., McGillion-Moore, J., Tian, X., Chen, Y., Itano, M. S., Diering, G. H., Meeker, R. B., & Cohen, T. J. (2023) · iScience · doi:10.1016/j.isci.2023.106905 · Cited by 21
Chemoproteomics Identifies State-Dependent and Proteoform-Selective Caspase-2 Inhibitors
Castellón, J. O., Ofori, S., Burton, N. R., Julio, A. R., Turmon, A. C., Armenta, E., Sandoval, C., Boatner, L. M., Takayoshi, E. E., Faragalla, M., et al. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12240 · Cited by 21
Tau Is Truncated in Five Regions of the Normal Adult Human Brain
Friedrich, M. G., Skora, A. S., Hancock, S. E., Mitchell, T. W., Else, P. L., & Truscott, R. J. W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073521 · Cited by 21
Kim, S.-I., Lee, W. K., Kang, S.-S., Lee, S.-Y., Jeong, M.-J., Lee, H. J., Kim, S. S., Johnson, G. V. W., & Chun, W. (2011) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2011.15.2.107 · Cited by 20
Taoka, R., Jinesh, G. G., Xue, W., Safe, S. H., & Kamat, A. M. (2017) · APOPTOSIS · doi:10.1007/s10495-017-1359-1 · Cited by 19
Caspase-cleaved TAR DNA-binding protein-43 in Pick's disease.
Rohn, T. T., & Kokoulina, P. (2009) · PubMed Central · Cited by 19
Self-citationKelley, C. M., Perez, S. E., & Mufson, E. J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0861-9 · Cited by 19
Tau proteins and senescent Cells: Targeting aging pathways in Alzheimer’s disease
Singh, M., Ali, H., Jyothi, S. R., Kaur, I., Kumar, S., Sharma, N., Prasad, G. V. S., Pramanik, A., Almalki, W. H., & Imran, M. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149165 · Cited by 18
Hromádková, L., Kolarova, M., Jankovičová, B., Bartoš, A., Říčný, J., Bı́lková, Z., & Řı́pová, D. (2015) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2015.10.017 · Cited by 18
The sea urchin embryo: A model to study Alzheimer’s beta amyloid induced toxicity
Pellicano, M., Picone, P., Cavalieri, V., Carrotta, R., Spinelli, G., & Carlo, M. D. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.12.006 · Cited by 18
Gupta, V. B., Hegde, M. L., & Rao, K. S. J. (2006) · Current Alzheimer Research · doi:10.2174/156720506778249452 · Cited by 18
The role of death receptors in neural injury
Lorz, C. (2009) · Frontiers in bioscience · doi:10.2741/3265 · Cited by 18
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
Sui, H., Zhang, L., Liu, Z., & Jin, Y. (2015) · Acta Pharmacologica Sinica · doi:10.1038/aps.2014.161 · Cited by 17
Lin, W.-L., Dickson, D. W., & Sahara, N. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31822ac9c9 · Cited by 19
The Balance between Life and Death: Defining a Role for Apoptosis in Aging
Cooper, D. (2012) · Journal of Clinical & Experimental Pathology · doi:10.4172/2161-0681.s4-001 · Cited by 17
Neergaard, J. S., Dragsbæk, K., Christiansen, C., Karsdal, M. A., Brix, S., & Henriksen, K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194802 · Cited by 17
Mondragón‐Rodríguez, S., Basurto‐Islas, G., Binder, L. I., & García‐Sierra, F. (2008) · Future Neurology · doi:10.2217/14796708.4.1.39 · Cited by 17
Early‐life exposure to high‐fat diet influences brain health in aging mice
Meco, A. D., & Praticò, D. (2019) · Aging Cell · doi:10.1111/acel.13040 · Cited by 16
Chi, H., Lee, S., Shiu, R.-H., Han, R., Hsieh, C.-P., Wei, T.-M., Lo, C., Chang, H.-Y., & Sang, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-70423-1 · Cited by 17
Tau in the gut, does it really matter?
Derkinderen, P., Rolli‐Derkinderen, M., Chapelet, G., Neunlist, M., & Noble, W. J. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15320 · Cited by 16
Noël, A., Foveau, B., & LeBlanc, A. C. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03506-0 · Cited by 16
Targeting caspase-2 interactions with tau in Alzheimer's disease and related dementias
Pockes, S., Walters, M. A., & Ashe, K. H. (2022) · Translational research · doi:10.1016/j.trsl.2022.10.009 · Cited by 15
Rather, M. A., Khan, A., Jahan, S., Siddiqui, A. J., & Wang, L. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.05.042 · Cited by 18
Intracellular tau fragment droplets serve as seeds for tau fibrils
Soeda, Y., Yoshimura, H., Bannai, H., Koike, R., Shiiba, I., & Takashima, A. (2024) · Structure · doi:10.1016/j.str.2024.06.018 · Cited by 15
Road to Alzheimer’s Disease: The Pathomechanism Underlying
Anand, R., Kaushal, A., Wani, W. Y., & Gill, K. D. (2011) · Pathobiology · doi:10.1159/000332218 · Cited by 16
Macchi, B., Marino‐Merlo, F., Frezza, C., Cuzzocrea, S., & Mastino, A. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8641-9 · Cited by 15
Cheng, Y.-H., Lai, S., Chen, P.-Y., Chang, J., & Chang, N. W. (2014) · Neurotoxicity Research · doi:10.1007/s12640-014-9485-9 · Cited by 15
Protein Truncation as a Common Denominator of Human Neurodegenerative Foldopathies
Jadhav, S., Žilka, N., & Novák, M. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8440-8 · Cited by 15
A critical overview of therapeutic strategy and advancement for Alzheimer's disease treatment
Kuo, Y., & Rajesh, R. (2017) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2017.05.011 · Cited by 15
Tau mRNA Metabolism in Neurodegenerative Diseases: A Tangle Journey
da Costa, P. J., Hamdane, M., Buée, L., & Martin, F. (2022) · Biomedicines · doi:10.3390/biomedicines10020241 · Cited by 16
Bernardo, M. D., & Carlo, M. D. (2017) · InTech eBooks · doi:10.5772/intechopen.70301 · Cited by 13
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Hintermayer, M. A., Volkening, K., Moszczynski, A. J., Donison, N. S., & Strong, M. J. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14942 · Cited by 14
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Cytoplasmic inclusions of TDP-43 in neurodegenerative diseases: a potential role for caspases.
Rohn, T. T. (2009) · PubMed · doi:10.14670/hh-24.1081 · Cited by 13
Self-citationKhezri, M. R., & Ghasemnejad-Berenji, M. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220873 · Cited by 12
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Wang, Y., Sørensen, M. G., Zheng, Q., Zhang, C., Karsdal, M. A., & Henriksen, K. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/209409 · Cited by 13
Loon, A. R., Zamudio, F., Sanneh, A., Brown, B., Smeltzer, S., Brownlow, M. L., Quadri, Z., Peters, M. M., Weeber, E. J., Nash, K. R., et al. (2021) · GeroScience · doi:10.1007/s11357-021-00408-z · Cited by 12
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Campo, M. D., Oliveira, C. R., Scheper, W., Zwart, R., Korth, C., Müller‐Schiffmann, A., Kostallas, G., Biverstål, H., Presto, J., Johansson, J., et al. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1769-y · Cited by 12
Gene- and Cell-Based Approaches for Neurodegenerative Disease
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Rizzi, L., & Grinberg, L. T. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01744-9 · Cited by 12
Metadata
- Authors
- Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W.
- Affiliations
- University of California, Irvine (US)
- Duke Medical Center (US)
- Boise State University (US)
- Corresponding author
- Cotman, Carl W.
- ORCID
- Venue
- Journal of Clinical Investigation
- Published
- 2004-07-01
- Volume
- 114
- Issue
- 1
- Pages
- 121-130
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC437967
- OpenAlex
- W1989856924
- Cited by
- 543
- References
- 82
- Citations by year
- 2026: 10 · 2025: 20 · 2024: 20 · 2023: 20 · 2022: 20 · 2021: 23 · 2020: 32 · 2019: 28 · 2018: 33 · 2017: 24 · 2016: 30 · 2015: 26 · 2014: 19 · 2013: 27 · 2012: 30
- FWCI
- 13.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ScholarWorks (Boise State University) (submittedVersion)
- Funders
- National Institutes of Health (1r03ag019386-01, AG016573, AG000096, AG000538)
- National Institute on Aging (P01AG000538, AG19386, AG19780, AG-000538, AG17968, AG000096, R01AG017968, P50AG016573, F32AG023433, AG023433, R01AG019780, T32AG000096)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau cleavage, caspase activation, neurofibrillary tangles, Alzheimer's disease, amyloid-beta, glycogen synthase kinase-3β, tau phosphorylation, PHF1, cognitive decline, mild cognitive impairment, traumatic brain injury, triple transgenic mouse model
- MeSH terms
- Alzheimer Disease, Animals, Humans, Membrane Proteins, Mice, Transgenic, Phosphorylation, Reference Values, Neurofibrillary Tangles, tau Proteins, Pyramidal Cells, Mice, Knockout, Caspases, Mice, Presenilin-1
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