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Active Caspase-6 and Caspase-6-Cleaved Tau in Neuropil Threads, Neuritic Plaques, and Neurofibrillary Tangles of Alzheimer's Disease
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Previously, we have shown that caspase-6 but not caspase-3 is activated by serum deprivation and induces a protracted cell death in primary cultures of human neurons (LeBlanc AC, Liu H, Goodyer C, Bergeron C, Hammond J: Caspase-6 role in apoptosis of human neurons, amyloidogenesis and Alzheimer's disease. J Biol Chem 1999, 274:23426-23436 and Zhang Y, Goodyer C, LeBlanc A: Selective and protracted apoptosis in human primary neurons microinjected with active caspase-3, -6, -7, and -8. J Neurosci 2000, 20:8384-8389). Here, we show with neoepitope antibodies that the p20 subunit of active caspase-6 increases twofold to threefold in the affected temporal and frontal cortex but not in the unaffected cerebellum of Alzheimer's disease brains and is present in neurofibrillary tangles, neuropil threads, and the neuritic plaques. Furthermore, a neoepitope antibody to caspase-6-cleaved Tau strongly detects intracellular tangles, extracellular tangles, pretangles, neuropil threads, and neuritic plaques. Immunoreactivity with both antibodies in pretangles indicates that the caspase-6 is active early in the pathogenesis of Alzheimer's disease. In contrast to the nuclear and cytosolic localization of active caspase-6 in apoptotic neurons of fetal and adult ischemic brains, the active caspase-6 in Alzheimer's disease brains is sequestered into the tangles or neurites. The localization of active caspase-6 may strongly jeopardize the structural integrity of the neuronal cytoskeletal system leading to inescapable neuronal dysfunction and eventual cell death in Alzheimer's disease neurons. Our results suggest that active caspase-6 is strongly implicated in human neuronal degeneration and apoptosis.
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“Active caspase-6 and tau-402 were observed in NFTs and neuritic plaques in AD brain [193].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [193]
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“Mice expressing the mutant variant exhibit well characterized age-dependant increases in neuronal tau pathology within cell bodies, dendrites and axons mimicking pathology observed in AD 23.”
From Amyloid-beta induced retrograde axonal degeneration in a mouse tauopathy model (2019) · cites this paper as [23]
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“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 [193]
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“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 [193]
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“Tau can be cleaved by caspase-6 at Asp13 (tau-13) and Asp402 (tau-402) [193, 198].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [193]
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Cites
Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
Kuida, K., Zheng, T. S., Na, S., Kuan, C.-Y., Yang, D., Karasuyama, H., RAKIC, P. T., & Flavell, R. A. (1996) · Nature · doi:10.1038/384368a0 · Cited by 1,881
A Unified Model for Apical Caspase Activation
Boatright, K. M., Renatus, M., Scott, F. L., Sperandio, S., Shin, H., Pedersen, I. M., Ricci, J., Edris, W. A., Sutherlin, D. P., Green, D. R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00051-0 · Cited by 986
Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831
Gervais, F. G., Xu, D., Robertson, G. S., Vaillancourt, J. P., Zhu, Y., Huang, J., LeBlanc, A., Smith, D., Rigby, M., Shearman, M. S., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80748-5 · Cited by 674
Self-citationEffects of environmental enrichment on gene expression in the brain
Rampon, C., Jiang, C. H., Dong, H., Tang, Y., Lockhart, D. J., Schultz, P. G., Tsien, J. Z., & Hu, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.23.12880 · Cited by 614
Caulı́n, C., Salvesen, G. S., & Oshima, R. G. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.6.1379 · Cited by 596
Stadelmann, C., Deckwerth, T. L., Srinivasan, A. N., Bancher, C., Brück, W., Jellinger, K. A., & Lassmann, H. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65460-0 · Cited by 432
Kim, T., Pettingell, W. H., Jung, Y., Kovacs, D. M., & Tanzi, R. E. (1997) · Science · doi:10.1126/science.277.5324.373 · Cited by 340
Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis
Byun, Y., Chen, F., Chang, R., Trivedi, M., Green, K. J., & Cryns, V. L. (2001) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400840 · Cited by 339
The effects of aging on gene expression in the hypothalamus and cortex of mice
Jiang, C. H., Tsien, J. Z., Schultz, P. G., & Hu, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1930 · Cited by 318
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Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
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Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994
RETRACTED ARTICLE: APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
Nikolaev, A., McLaughlin, T., O’Leary, D. D. M., & Tessier-Lavigne, M. (2009) · Nature · doi:10.1038/nature07767 · Cited by 992
RetractedCaspases in Cell Death, Inflammation, and Pyroptosis
Kesavardhana, S., Malireddi, R. K. S., & Kanneganti, T. (2020) · Annual Review of Immunology · doi:10.1146/annurev-immunol-073119-095439 · Cited by 954
Post-translational modifications of tau protein: Implications for Alzheimer's disease
Martin, L., Latypova, X., & Terro, F. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2010.12.023 · Cited by 683
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
Structure and Pathology of Tau Protein in Alzheimer Disease
Kolarova, M., García‐Sierra, F., Bartoš, A., Říčný, J., & Řípová, D. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731526 · Cited by 526
Olsson, M., & Zhivotovsky, B. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.30 · Cited by 419
Neuronal Cell Death Mechanisms in Major Neurodegenerative Diseases
Chi, H., Chang, H.-Y., & Sang, T.-K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103082 · Cited by 412
Intrinsic and extrinsic pathways of apoptosis: Role in cancer development and prognosis
Kashyap, D., Garg, V. K., & Goel, N. (2021) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2021.01.003 · Cited by 439
Microtubule-associated protein tau in development, degeneration and protection of neurons
Wang, J., & Liu, F. (2008) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.03.002 · Cited by 405
A Review on Caspases: Key Regulators of Biological Activities and Apoptosis
Sahoo, G., Samal, D., Khandayataray, P., & Murthy, M. K. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03433-5 · Cited by 414
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367
Characterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease
Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 369
Salminen, A., Ojala, J. O., Kauppinen, A., Kaarniranta, K., & Suuronen, T. (2009) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2009.01.001 · Cited by 360
Caspase Substrates and Cellular Remodeling
Crawford, E. D., & Wells, J. A. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-121639 · Cited by 349
Kaushal, V, Dye, R., Pakavathkumar, P., Foveau, B., Flores, J., Hyman, B., Ghetti, B., Koller, B. H., & LeBlanc, A. C. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.16 · Cited by 297
Self-citationFlores, J., Noël, A., Foveau, B., Lynham, J., Lecrux, C., & LeBlanc, A. C. (2018) · Nature Communications · doi:10.1038/s41467-018-06449-x · Cited by 288
Self-citationWhitmore, A. V., Libby, R. T., & John, S. W. M. (2005) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2005.04.004 · Cited by 257
Apoptotic and non-apoptotic roles of caspases in neuronal physiology and pathophysiology
Hyman, B. T., & Yuan, J. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3228 · Cited by 261
Tau Proteins and Tauopathies in Alzheimer’s Disease
Chong, F. P., Ng, K. Y., Koh, R. Y., & Chye, S. M. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0574-1 · Cited by 260
Calon, F., Lim, G. P., Morihara, T., Yang, F., Ubeda, O. J., Salem, N., Frautschy, S. A., & Cole, G. M. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04253.x · Cited by 253
Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies
Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220
Tau clearance mechanisms and their possible role in the pathogenesis of Alzheimer disease.
Chesser, A. S., Pritchard, S. M., & Johnson, G. V. W. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00122 · Cited by 219
Caspase-3 Is Enriched in Postsynaptic Densities and Increased in Alzheimer's Disease
Louneva, N., Cohen, J. W., Han, L., Talbot, K., Wilson, R. S., Bennett, D. A., Trojanowski, J. Q., & Arnold, S. E. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080434 · Cited by 213
Mitochondrial and Cell Death Mechanisms in Neurodegenerative Diseases
Martin, L. J. (2010) · Pharmaceuticals · doi:10.3390/ph3040839 · Cited by 213
The Role of Caspase Cleavage of Tau in Alzheimer Disease Neuropathology
Cotman, C. W., Poon, W. W., Rissman, R. A., & Blurton-Jones, M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.104 · Cited by 199
Bousiges, O., de Vasconcelos, A. P., Neidl, R., Cosquer, B., Herbeaux, K., Panteleeva, I., Loeffler, J., Cassel, J., & Boutillier, A. (2010) · Neuropsychopharmacology · doi:10.1038/npp.2010.117 · Cited by 202
Inflammasome signaling at the heart of central nervous system pathology
Chakraborty, S., Kaushik, D. K., Gupta, M., & Basu, A. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22343 · Cited by 189
Distinct pathways mediate axon degeneration during apoptosis and axon-specific pruning
Cusack, C. L., Swahari, V., Henley, W. H., Ramsey, J. M., & Deshmukh, M. (2013) · Nature Communications · doi:10.1038/ncomms2910 · Cited by 176
Tau Proteolysis in the Pathogenesis of Tauopathies: Neurotoxic Fragments and Novel Biomarkers
Quinn, J. P., Corbett, N. J., Kellett, K. A. B., & Hooper, N. M. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-170959 · Cited by 170
Microinjection as a tool of mechanical delivery
Zhang, Y., & Yu, L. (2008) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2008.07.005 · Cited by 175
Zhao, T., Zou, S., & Knapp, P. E. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.09.092 · Cited by 165
Neuronal Apoptosis and Autophagy Cross Talk in Aging PS/APP Mice, a Model of Alzheimer's Disease
Yang, D., Kumar, A. R., Stavrides, P. H., Peterson, J. N., Peterhoff, C., Pawlik, M., Levy, E., Cataldo, A. M., & Nixon, R. A. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.071176 · Cited by 164
Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168
Amyloid‐β oligomers set fire to inflammasomes and induce Alzheimer's pathology
Salminen, A., Ojala, J. O., Suuronen, T., Kaarniranta, K., & Kauppinen, A. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00496.x · Cited by 167
Silva, T., Reis, J., Teixeira, J., & Borges, F. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.03.008 · Cited by 158
Caspase and calpain function in cell death: bridging the gap between apoptosis and necrosis
Harwood, S., Yaqoob, M. M., & Allen, D. A. (2005) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/000456305774538238 · Cited by 157
Activation of Caspase-6 in Aging and Mild Cognitive Impairment
Albrecht, S., Bourdeau, M., Bennett, D. A., Mufson, E. J., Bhattacharjee, M. B., & LeBlanc, A. C. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060974 · Cited by 155
Self-citationSingle‐cell microinjection technology in cell biology
Zhang, Y., & Yu, L. (2008) · BioEssays · doi:10.1002/bies.20759 · Cited by 134
Millan, M. J. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.004 · Cited by 151
Funk, K. E., Thomas, S. N., Schafer, K. N., Cooper, G. L., Liao, Z., Clark, D. J., Yang, A. J., & Kuret, J. (2014) · Biochemical Journal · doi:10.1042/bj20140372 · Cited by 142
Wang, Y., Garg, S., Mandelkow, E., & Mandelkow�, E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380955 · Cited by 145
Roberts, M., Sevastou, I., Imaizumi, Y., Mistry, K., Talma, S., Dey, M., Gartlon, J., Ochiai, H., Zhou, Z., Akasofu, S., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-0884-2 · Cited by 135
Theofilas, P., Ehrenberg, A. J., Nguy, A. K., Thackrey, J. M., Dunlop, S. R., Mejia, M. B., Alho, A. T. D. L., Leite, R. E. P., Rodriguez, R. D., Suemoto, C. K., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.007 · Cited by 134
Warby, S. C., Doty, C. N., Graham, R. K., Carroll, J. B., Yang, Y., Singaraja, R. R., Overall, C. M., & Hayden, M. R. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn139 · Cited by 143
Derisbourg, M. J., Leghay, C., Chiappetta, G., Fernández-Gómez, F.-J., Laurent, C., Demeyer, D., Carrier, S., Buée‐Scherrer, V., Blum, D. L., Vinh, J., et al. (2015) · Scientific Reports · doi:10.1038/srep09659 · Cited by 149
Yap, J. K. Y., Pickard, B. S., Chan, E. W. L., & Gan, S. Y. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1638-7 · Cited by 130
Caspase-6 and neurodegeneration
Graham, R. K., Ehrnhoefer, D. E., & Hayden, M. R. (2011) · Trends in Neurosciences · doi:10.1016/j.tins.2011.09.001 · Cited by 127
Mouser, P. E., Head, E., Ha, K.-H., & Rohn, T. T. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.050798 · Cited by 121
Madeira, A., Pommet, J., Prochiantz, A., & Allinquant, B. (2005) · The FASEB Journal · doi:10.1096/fj.05-3839fje · Cited by 102
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Apoptosis and in vitro Alzheimer’s disease neuronal models
Calissano, P., Matrone, C., & Amadoro, G. (2009) · Communicative & Integrative Biology · doi:10.4161/cib.7704 · Cited by 111
Ferreira, A., & Bigio, E. H. (2011) · Molecular Medicine · doi:10.2119/molmed.2010.00220 · Cited by 112
Therapeutic strategies for the treatment of tauopathies: Hopes and challenges
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Bile acids and apoptosis modulation: an emerging role in experimental Alzheimer's disease
Ramalho, R. M., Viana, R. J. S., Low, W. C., Steer, C. J., & Rodrigues, C. M. P. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.001 · Cited by 107
Graham, R. K., Deng, Y., Carroll, J. A., Vaid, K., Cowan, C., Pouladi, M. A., Metzler, M., Bissada, N., Wang, L., Faull, R. L. M., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2071-10.2010 · Cited by 106
Vohra, B. P. S., Sasaki, Y., Miller, B. R., Chang, J., DiAntonio, A., & Milbrandt, J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2939-10.2010 · Cited by 103
Truncation of Tau Protein and its Pathological Significance in Alzheimer's Disease
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Caspase-2 is required for dendritic spine and behavioural alterations in J20 APP transgenic mice
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Flores, J., Noël, A., Foveau, B., Beauchet, O., & LeBlanc, A. C. (2020) · Nature Communications · doi:10.1038/s41467-020-18405-9 · Cited by 103
Self-citationAggregation of Disordered Proteins Associated with Neurodegeneration
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Activation and Regulation of Caspase-6 and Its Role in Neurodegenerative Diseases
Wang, X., Cao, Q., Zhang, Y., & Su, X. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124414 · Cited by 101
Klaiman, G., Champagne, N., & LeBlanc, A. C. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.12.004 · Cited by 97
Self-citationApoptotic mechanisms involved in neurodegenerative diseases: Experimental and therapeutic approaches
Camins, A., Pallàs, M., & Silvestre, J. S. (2008) · Methods and Findings in Experimental and Clinical Pharmacology · doi:10.1358/mf.2008.30.1.1090962 · Cited by 95
Wang, X., Cao, Q., Liu, X., Wang, K., Mi, W., Zhang, Y., Li, L.-F., LeBlanc, A. C., & Su, X. (2010) · EMBO Reports · doi:10.1038/embor.2010.141 · Cited by 91
Self-citationAkpan, N., Serrano‐Saiz, E., Zacharia, B. E., Otten, M. L., Ducruet, A. F., Snipas, S. J., Liu, W., Velloza, J., Cohen, G., Sosunov, S. A., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0698-11.2011 · Cited by 90
The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics
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Ray, M., & Zhang, W. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-136 · Cited by 92
D’Souza, Y., Elharram, A., Soon-Shiong, R., Andrew, R. D., & Bennett, B. M. (2015) · Molecular Brain · doi:10.1186/s13041-015-0117-y · Cited by 87
Noorbakhsh, F., Ramachandran, R., Barsby, N. L., Ellestad, K. K., LeBlanc, A. C., Dickie, P., Baker, G. B., Hollenberg, M. D., Cohen, É. A., & Power, C. (2010) · The FASEB Journal · doi:10.1096/fj.09-147819 · Cited by 87
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Boese, A. C., Hamblin, M. H., & Lee, J. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.113112 · Cited by 89
Combs, B., Hamel, C., & Kanaan, N. M. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.016 · Cited by 93
Mitochondrial Abnormalities in Alzheimer’s Disease
Silva, D. F., Selfridge, J. E., Lu, J., E, L., Cardoso, S. M., & Swerdlow, R. H. (2012) · Advances in Pharmacology · doi:10.1016/b978-0-12-394816-8.00003-9 · Cited by 86
Zinc-mediated Allosteric Inhibition of Caspase-6
Velázquez-Delgado, E. M., & Hardy, J. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.397752 · Cited by 84
Lee, S. C., Chan, J. Y., Clement, M., & Pervaiz, S. (2006) · PROTEOMICS · doi:10.1002/pmic.200500366 · Cited by 83
Caspase-1 activation of caspase-6 in human apoptotic neurons
Guo, H., Petrin, D., Zhang, Y., Bergeron, C., Goodyer, C. G., & LeBlanc, A. C. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401753 · Cited by 82
Self-citationAlbrecht, S., Bogdanović, N., Ghetti, B. F., Winblad, B. G., & LeBlanc, A. C. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181c1da10 · Cited by 80
Self-citationFeurstein, D., Stemmer, K., Kleinteich, J., Speicher, T., & Dietrich, D. R. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr243 · Cited by 79
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Ravalin, M., Theofilas, P., Basu, K., Opoku-Nsiah, K., Assimon, V. A., Medina-Cleghorn, D., Chen, Y., Bohn, M., Arkin, M. R., Grinberg, L. T., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0322-6 · Cited by 80
Ehrnhoefer, D. E., Wong, B. K. Y., & Hayden, M. R. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3556 · Cited by 78
Human Tau Isoforms and Proteolysis for Production of Toxic Tau Fragments in Neurodegeneration
Boyarko, B., & HOOK, V. Y. H. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.702788 · Cited by 81
Tau Phosphorylation and Cleavage in Ethanol-Induced Neurodegeneration in the Developing Mouse Brain
Saito, M., Chakraborty, G., Mao, R.-F., Paik, S.-M., Vadász, C., & Saito, M. (2010) · Neurochemical Research · doi:10.1007/s11064-009-0116-4 · Cited by 72
Higuchi, M., Iwata, N., & Saido, T. C. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.02.013 · Cited by 73
Battaglia, R. A., Beltrán, A. S., Delic, S., Dumitru, R., Robinson, J. A., Kabiraj, P., Herring, L. E., Madden, V. J., Ravinder, N., Willems, E., et al. (2019) · eLife · doi:10.7554/elife.47789 · Cited by 69
Sokolowski, J. D., Gamage, K. K., Heffron, D. S., LeBlanc, A. C., Deppmann, C. D., & Mandell, J. W. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-16 · Cited by 69
Self-citationC‐terminal truncation modulates both nucleation and extension phases of τ fibrillization
Yin, H., & Kuret, J. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.11.077 · Cited by 72
Inflammasome Involvement in Alzheimer’s Disease
Olsen, I., & Singhrao, S. K. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160197 · Cited by 66
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 67
Corsetti, V., Amadoro, G., Gentile, A., Capsoni, S., Ciotti, M. T., Cencioni, M. T., Atlante, A., Canu, N., Rohn, T. T., Cattaneo, A., et al. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2008.03.011 · Cited by 68
Caspase-Mediated Degeneration in Alzheimer's Disease
Cribbs, D. H., Poon, W. W., Rissman, R. A., & Blurton-Jones, M. M. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63302-0 · Cited by 64
Caspases as therapeutic targets in Alzheimer's disease: is it time to "cut" to the chase?
Rohn, T. T., & Head, E. (2009) · PubMed Central · Cited by 63
Differential regulation of Abeta42-induced neuronal C1q synthesis and microglial activation.
Fan, R., & Tenner, A. J. (2005) · Journal of Neuroinflammation · doi:10.1186/1742-2094-2-1 · Cited by 63
Targeting caspase-6 and caspase-8 to promote neuronal survival following ischemic stroke
Shabanzadeh, A. P., D’Onofrio, P. M., Monnier, P. P., & Koeberle, P. D. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.272 · Cited by 62
Glushakova, O., Glushakov, A. V., Glushakov, A. O., Wijesinghe, D. S., Valadka, A. B., & Hayes, R. (2017) · Brain Circulation · doi:10.4103/bc.bc_27_16 · Cited by 65
Flores, J., Noël, A., Fillion, M.-L., & LeBlanc, A. C. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00881-1 · Cited by 59
Self-citation
Metadata
- Authors
- Guo, H., Albrecht, S., Bourdeau, M., Petzke, T., Bergeron, C., & LeBlanc, A. C.
- Affiliations
- Jewish General Hospital (CA)
- University of Toronto (CA)
- Corresponding author
- LeBlanc, Andrea C.
- Venue
- The American Journal of Pathology
- Publisher
- Elsevier BV
- Published
- 2004-08
- Volume
- 165
- Issue
- 2
- Pages
- 523-531
- ISSN
- 0002-9440 (ISSN-L)
- PMC
- PMC1618555
- OpenAlex
- W1997426613
- Cited by
- 287
- References
- 32
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 10 · 2023: 9 · 2022: 8 · 2021: 21 · 2020: 11 · 2019: 16 · 2018: 13 · 2017: 10 · 2016: 10 · 2015: 10 · 2014: 11 · 2013: 19 · 2012: 19
- FWCI
- 6.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal Of Pathology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- McGill University
- National Institutes of Health (1r03mh040965-01)
- National Institute of Neurological Disorders and Stroke (NS/MH40965)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- caspase-6, Alzheimer's disease, neurofibrillary tangles, neuropil threads, neuritic plaques, neuronal apoptosis, tau cleavage, neurodegeneration, caspase-3
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Autopsy, Cell Nucleus, Cerebellum, Cerebral Cortex, Cytosol, Humans, Middle Aged, Neurofibrillary Tangles, tau Proteins, Apoptosis, Neuropil Threads, Caspases, Caspase 6, Plaque, Amyloid
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