Oxidative stress mediates tau-induced neurodegeneration in Drosophila
Open accessAbstract
Markers of oxidative damage have been detected in brain tissue from patients with Alzheimer disease (AD) and other neurodegenerative disorders. These findings implicate oxidative injury in the neurodegenerative process, but whether oxidative stress is a cause or a consequence of neurotoxicity remains unclear. We used a Drosophila model of human tauopathies to investigate the role of oxidative stress in neurodegeneration. Genetic and pharmacological manipulation of antioxidant defense mechanisms significantly modified neurodegeneration in our model, suggesting that oxidative stress plays a causal role in neurotoxicity. We demonstrate that the JNK signaling pathway is activated in our model, which is in agreement with previous findings in AD tissue. Furthermore, we show that the extent of JNK activation correlates with the degree of tau-induced neurodegeneration. Finally, our findings suggest that oxidative stress acts not to promote tau phosphorylation, but to enhance tau-induced cell cycle activation. In summary, our study identifies oxidative stress as a causal factor in tau-induced neurodegeneration in Drosophila.
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Pan-neuronal transgenic expression of an FTDP-17 mutant form of human tau, tauR406W, in Drosophila causes progressive neurodegeneration and provides a well-characterized in vivo genetic model of tau neurotoxicity.
“Pan-neuronal transgenic expression of an FTDP-17 mutant form of human tau, tauR406W, in Drosophila causes progressive neurodegeneration and provides a well-characterized in vivo genetic model of tau neurotoxicity7,15,16.”
From Tau promotes neurodegeneration through global chromatin relaxation (2014) · cites this paper as [16]
No statistical methods were used to predetermine sample sizes but our sample sizes are similar to those reported in previous publications.
“No statistical methods were used to predetermine sample sizes but our sample sizes are similar to those reported in previous publications 7,16,44.”
From Tau promotes neurodegeneration through global chromatin relaxation (2014) · cites this paper as [16]
Neuronal phenotypes of tau transgenic Drosophila mimic features of human Alzheimer's disease and associated tauopathies.
“In addition, neuronal phenotypes of tau transgenic Drosophila mimic features of human Alzheimer’s disease and associated tauopathies, including but not limited to aberrant tau phosphorylation13, oxidative stress14, DNA damage15,16, decondensation of constitutive heterochromatin10, synaptic dysfunction17 and activation of the cell cycle in post-mitotic neurons18.”
From Pathogenic tau-induced piRNA depletion promotes neuronal death through transposable element dysregulation in neurodegenerative tauopathies (2018) · cites this paper as [14]
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Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269 · see citing works
Lee, 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 · see citing works
Cellular response to oxidative stress: Signaling for suicide and survival *
Martindale, J., & Holbrook, N. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10119 · Cited by 2,392 · see citing works
Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869 · see citing works
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724 · see citing works
Orr, W. C., & Sohal, R. S. (1994) · Science · doi:10.1126/science.8108730 · Cited by 1,461 · see citing works
Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409 · see citing works
Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease
Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239 · see citing works
Cummings, J. L. (2004) · New England Journal of Medicine · doi:10.1056/nejmra040223 · Cited by 1,152 · see citing works
Tauopathy in <i>Drosophila</i> : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · see citing works
Self-citationExtension of Drosophila lifespan by overexpression of human SOD1 in motorneurons
Parkes, T. L., Elia, A., Dickinson, D., Hilliker, A. J., Phillips, J. P., & Boulianne, G. L. (1998) · Nature Genetics · doi:10.1038/534 · Cited by 862 · see citing works
Markesbery, W. R., & Lovell, M. A. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00009-8 · Cited by 680 · see citing works
Martı́n-Blanco, E., Gampel, A., Ring, J., Virdee, K., Kirov, N., Tolkovsky, A. M., & Martínez-Arias, A. (1998) · Genes & Development · doi:10.1101/gad.12.4.557 · Cited by 673 · see citing works
The harlequin mouse mutation downregulates apoptosis-inducing factor
Klein, J. A., Longo-Guess, C. M., Rossmann, M. P., Seburn, K. L., Hurd, R. E., Frankel, W. N., Bronson, R. T., & Ackerman, S. L. (2002) · Nature · doi:10.1038/nature01034 · Cited by 605 · see citing works
Ectopic Cell Cycle Proteins Predict the Sites of Neuronal Cell Death in Alzheimer’s Disease Brain
Busser, J., Geldmacher, D. S., & Herrup, K. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-08-02801.1998 · Cited by 543 · see citing works
Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms
Andorfer, C., Acker, C. M., Kress, Y., Hof, P. R., Duff, K., & Davies, P. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4637-04.2005 · Cited by 511 · cited 1× · see citing works
“Interestingly, hallmarks of both apoptotic and necrotic cell death have been recently identified in neurons from transgenic mice expressing nonmutant forms of human tau (53).”
BackgroundJackson, G. R., Wiedau-Pazos, M., Sang, T.-K., Wagle, N., Brown, C. A., Massachi, S., & Geschwind, D. H. (2002) · Neuron · doi:10.1016/s0896-6273(02)00706-7 · Cited by 488 · see citing works
Mattson, M. P. (2003) · NeuroMolecular Medicine · doi:10.1385/nmm:3:2:65 · Cited by 475 · see citing works
Zhu, X.-W., Raina, A., Rottkamp, C., Aliev, G., Perry, G., Boux, H., & Smith, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00046.x · Cited by 440 · see citing works
Tau phosphorylation: physiological and pathological consequences
Stoothoff, W. H., & Johnson, G. V. W. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.017 · Cited by 439 · see citing works
Oxidative stress signalling in Alzheimer's disease
Zhu, X., Raina, A. K., Lee, H., Casadesús, G., Smith, M. A., & Perry, G. L. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.012 · Cited by 390 · see citing works
Phillips, J. P., Campbell, S. D., Michaud, D., Charbonneau, M., & Hilliker, A. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.8.2761 · Cited by 389 · see citing works
Sun, J., Folk, D. G., Bradley, T. J., & Tower, J. (2002) · Genetics · doi:10.1093/genetics/161.2.661 · Cited by 381 · see citing works
Cell Cycle Activation Linked to Neuronal Cell Death Initiated by DNA Damage
Kruman, I. I., Wersto, R. P., Cardozo‐Pelaez, F., Smilenov, L. B., Chan, S. L., Chrest, F. J., Emokpae, R., Gorospe, M., & Mattson, M. P. (2004) · Neuron · doi:10.1016/s0896-6273(04)00017-0 · Cited by 365 · see citing works
Nishimura, I., Yang, Y., & Lu, B. (2004) · Cell · doi:10.1016/s0092-8674(04)00170-9 · Cited by 324 · see citing works
Sung, S., Yao, Y., Uryu, K., Yang, H., Lee, V. M. ‐., Trojanowski, J. Q., & Praticò, D. (2003) · The FASEB Journal · doi:10.1096/fj.03-0961fje · Cited by 298 · see citing works
Divide and Die: Cell Cycle Events as Triggers of Nerve Cell Death
Herrup, K., Neve, R. L., Ackerman, S. L., & Copani, A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3347-04.2004 · Cited by 285 · see citing works
Alpha-tocopherol: roles in prevention and therapy of human disease
Tucker, J. M., & Townsend, D. M. (2005) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2005.06.005 · Cited by 285 · see citing works
Stress-Responsive Protein Kinases in Redox-Regulated Apoptosis Signaling
Matsuzawa, A., & Ichijo, H. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.472 · Cited by 283 · see citing works
TOR-Mediated Cell-Cycle Activation Causes Neurodegeneration in a Drosophila Tauopathy Model
Khurana, V., Lu, Y., Steinhilb, M. L., Oldham, S., Shulman, J. M., & Feany, M. B. (2006) · Current Biology · doi:10.1016/j.cub.2005.12.042 · Cited by 266 · see citing works
Self-citationGenetic modifiers of tauopathy in Drosophila
Shulman, J. M., & Feany, M. B. (2003) · Genetics · doi:10.1093/genetics/165.3.1233 · Cited by 256 · see citing works
Self-citationNathan, C., Calingasan, N., Nezezon, J., Ding, A., Lucia, M. S., La Perle, K., Fuortes, M., Lin, M., Ehrt, S., Kwon, N. S., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051529 · Cited by 214 · see citing works
Kirby, K., Hu, J., Hilliker, A. J., & Phillips, J. P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252342899 · Cited by 208 · see citing works
Mitotic activation: a convergent mechanism for a cohort of neurodegenerative diseases
Husseman, J. W. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00221-9 · Cited by 187 · see citing works
Ectopic localization of phosphorylated histone H3 in Alzheimer's disease: a mitotic catastrophe?
Ogawa, O., Zhu, X., Lee, H., Raina, A. K., Obrenovich, M. E., Bowser, R. P., Ghanbari, H. A., Castellani, R. J., Perry, G. L., & Smith, M. A. (2003) · Acta Neuropathologica · doi:10.1007/s00401-003-0684-3 · Cited by 175 · see citing works
Vitamin C and Vitamin E for Alzheimer's Disease
Boothby, L. A., & Doering, P. L. (2005) · Annals of Pharmacotherapy · doi:10.1345/aph.1e495 · Cited by 175 · see citing works
Yang, Y., Varvel, N. H., Lamb, B. T., & Herrup, K. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3707-05.2006 · Cited by 174 · see citing works
JNK activation is associated with intracellular β-amyloid accumulation
Shoji, M., Iwakami, N., Takeuchi, S., Waragai, M., Suzuki, M., Kanazawa, I., Lippa, C. F., Ono, S., & Okazawa, H. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00245-x · Cited by 166 · see citing works
Conte, V., Uryu, K., Fujimoto, S., Yao, Y., Rokach, J., Longhi, L., Trojanowski, J. Q., Lee, V. M., McIntosh, T. K., & Praticò, D. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02560.x · Cited by 164 · see citing works
A Sod2 Null Mutation Confers Severely Reduced Adult Life Span in Drosophila
Duttaroy, A., Paul, A., Kundu, M., & Belton, A. (2003) · Genetics · doi:10.1093/genetics/165.4.2295 · Cited by 153 · see citing works
Self-citationApoptosis and protein expression after focal cerebral ischemia in rat
Li, Y., Chopp, M., Powers, C., & Jiang, N. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00524-6 · Cited by 150 · see citing works
Arking, R., Buck, S. A., Berrios, A., Dwyer, S. B., & Baker, G. T. (1991) · Developmental Genetics · doi:10.1002/dvg.1020120505 · Cited by 139 · see citing works
Vitamin E in Neurodegenerative Disorders: Alzheimer's Disease
Kontush, A., & Schekatolina, S. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1331.025 · Cited by 131 · see citing works
Colton, C. A., Vitek, M. P., Wink, D. A., Xu, Q., Cantillana, V., Previti, M. L., Van Nostrand, W. E., Weinberg, J. B., & Dawson, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601075103 · Cited by 128 · see citing works
Cooperative action of antioxidant defense systems in Drosophila
Missirlis, F., Phillips, J. P., & Jäckle, H. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00393-1 · Cited by 113 · see citing works
Sohal, R. S. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00885-7 · Cited by 113 · see citing works
Neuronal RNA Oxidation in Alzheimer's Disease and Down's Syndrome
Nunomura, A., Perry, G. L., Hirai, K., Aliev, G. M., Takeda, A., Chiba, S., & Smith, M. A. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07855.x · Cited by 111 · see citing works
Compartment-specific Protection of Iron-Sulfur Proteins by Superoxide Dismutase
Missirlis, F., Hu, J., Kirby, K., Hilliker, A. J., Rouault, T. A., & Phillips, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307700200 · Cited by 111 · see citing works
Molecular characterization and rescue of acatalasemic mutants of Drosophila melanogaster.
Griswold, C. M., Matthews, A. L., Bewley, K. R., & Mahaffey, J. W. (1993) · Genetics · doi:10.1093/genetics/134.3.781 · Cited by 100 · see citing works
Effects of α-tocopherol on an animal model of tauopathies
Nakashima, H., Ishihara, T., Yokota, O., Terada, S., Trojanowski, J. Q., Lee, V. M. ‐., & Kuroda, S. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.037 · Cited by 99 · see citing works
Molecular Genetics of Chromosome 17 Tauopathies
HUTTON, M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06906.x · Cited by 92 · see citing works
Missirlis, F., Hirosawa, M., Grönke, S., Schäfer, U., Jäckle, H., Ulschmid, J. K., Becker, K., & Phillips, J. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111692200 · Cited by 86 · see citing works
Missirlis, F., Rahlfs, S., Dimopoulos, N., Bauer, H., Becker, K., Hilliker, A. J., Phillips, J. P., & Jäckle, H. (2003) · Biological Chemistry · doi:10.1515/bc.2003.052 · Cited by 85 · see citing works
Calorie restriction delays lipid oxidative damage in Drosophila melanogaster
Zheng, J., Mutcherson, R. J., & Helfand, S. L. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00159.x · Cited by 83 · see citing works
Oxidative stress‐induced death in the nervous system: Cell cycle dependent or independent?
Langley, B. C., & Ratan, R. R. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20210 · Cited by 68 · see citing works
Oxidative Stress and Neuronal Adaptation in Alzheimer Disease: The Role of SAPK Pathways
Zhu, X., Raina, A. K., Lee, H., Chao, M. P., Nunomura, A., Tabaton, M., Petersen, R. B., Perry, G. L., & Smith, M. A. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770310220 · Cited by 67 · see citing works
c-Jun and cyclin D1 proteins as mediators of neuronal death after a focal ischaemic insult
Guégan, C., Lévy, V., David, J.-P., Cymbalista, F., & Sola, B. (1997) · Neuroreport · doi:10.1097/00001756-199703030-00037 · Cited by 56 · see citing works
Alzheimer neurofibrillary lesions: Molecular nature and potential roles of different components
Yen, S.-H. C., Liu, W.-K., Hall, F. L., Yan, S., Stern, D. M., & Dickson, D. W. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00022-7 · Cited by 53 · see citing works
Krishnamurthy, P., & Johnson, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311203200 · Cited by 52 · see citing works
Pro-apoptotic effects of tau mutations in chromosome 17 frontotemporal dementia and parkinsonism
Furukawa, K., D’Souza, I., Crudder, C. H., Onodera, H., Itoyama, Y., Poorkaj, P., Bird, T. D., & Schellenberg, G. D. (2000) · Neuroreport · doi:10.1097/00001756-200001170-00011 · Cited by 28 · see citing works
Hashimoto, Y., Tsukamoto, E., Niikura, T., Yamagishi, Y., Ishizaka, M., Aiso, S., Takashima, A., & Nishimoto, I. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10861 · Cited by 23 · see citing works
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Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword?
Malhotra, J. D., & Kaufman, R. J. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1782 · Cited by 1,556 · see citing works
The endoplasmic reticulum and the unfolded protein response
Malhotra, J. D., & Kaufman, R. J. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.09.003 · Cited by 984 · see citing works
Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future
Zhang, Y., Chen, H., Li, R., Sterling, K., & Song, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01484-7 · Cited by 988 · see citing works
Oxidative Stress and the Pathogenesis of Alzheimer's Disease
Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855 · see citing works
Oxidative stress in Alzheimer’s disease
Chen, Z., & Zhong, C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1423-y · Cited by 797 · see citing works
Oxidative stress: The core pathogenesis and mechanism of Alzheimer’s disease
Bai, R., Guo, J., Ye, X.-Y., Xie, Y., & Xie, T. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101619 · Cited by 813 · see citing works
Animal models of Alzheimer's disease and frontotemporal dementia
Götz, J., & Ittner, L. M. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2420 · Cited by 676 · see citing works
Tau promotes neurodegeneration through global chromatin relaxation
Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works
Self-citationKamat, P. K., Kalani, A., Rai, S., Swarnkar, S., Tota, S., Nath, C., & Tyagi, N. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-9053-6 · Cited by 504 · see citing works
McConnell, G. C., Rees, H. D., Levey, A. I., Gutekunst, C.-A., Gross, R. E., & Bellamkonda, R. V. (2009) · Journal of Neural Engineering · doi:10.1088/1741-2560/6/5/056003 · Cited by 480 · see citing works
Rutin as a Potent Antioxidant: Implications for Neurodegenerative Disorders
Enogieru, A. B., Haylett, W. L., Hiss, D. C., Bardien, S., & Ekpo, O. E. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6241017 · Cited by 483 · see citing works
Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
Fulga, T. A., Elson-Schwab, I., Khurana, V., Steinhilb, M. L., Spires, T. L., Hyman, B. T., & Feany, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1528 · Cited by 452 · see citing works
Self-citationTau association with synaptic vesicles causes presynaptic dysfunction
Zhou, L., McInnes, J., Wierda, K., Holt, M., Herrmann, A. G., Jackson, R. J., Wang, Y.-C., Swerts, J., Beyens, J., Miskiewicz, K., et al. (2017) · Nature Communications · doi:10.1038/ncomms15295 · Cited by 434 · see citing works
Antioxidant Therapies for Alzheimer's Disease
Feng, Y., & Wang, X. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/472932 · Cited by 382 · see citing works
Tau Promotes Neurodegeneration via DRP1 Mislocalization In Vivo
DuBoff, B., Götz, J., & Feany, M. B. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.026 · Cited by 377 · see citing works
Self-citationFerreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373 · see citing works
Mitochondrial Oxidative Stress Causes Hyperphosphorylation of Tau
Melov, S., Adlard, P. A., Morten, K., Johnson, F., Golden, T. R., Hinerfeld, D., Schilling, B., Mavros, C., Masters, C. L., Volitakis, I., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000536 · Cited by 363 · see citing works
Diabetes mellitus and Alzheimer's disease: shared pathology and treatment?
Akter, K., Lanza, E. A., Martin, S. A., Myronyuk, N., Rua, M., & Raffa, R. B. (2011) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2010.03830.x · Cited by 352 · see citing works
Naini, S. M. A., & Soussi‐Yanicostas, N. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/151979 · Cited by 318 · see citing works
Sun, W., Samimi, H., Gamez, M., Zare, H., & Frost, B. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0194-1 · Cited by 315 · see citing works
Buckingham, S. D., Jones, A. K., Brown, L. A., & Sattelle, D. B. (2009) · Pharmacological Reviews · doi:10.1124/pr.108.000562 · Cited by 307 · see citing works
Stress-Responsive Protein Kinases in Redox-Regulated Apoptosis Signaling
Matsuzawa, A., & Ichijo, H. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.472 · Cited by 283 · see citing works
DNA replication stress, genome instability and aging
Burhans, W. C., & Weinberger, M. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1059 · Cited by 279 · see citing works
Cellular and pathological functions of tau
Bravo, C. P., Naguib, S. A., & Gan, L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00753-9 · Cited by 245 · see citing works
Drosophila melanogaster in the Study of Human Neurodegeneration
Hirth, F. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791556104 · Cited by 236 · see citing works
A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies
Orr, M. E., Sullivan, A. C., & Frost, B. E. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.011 · Cited by 232 · see citing works
Dysfunctional Mitochondria and Mitophagy as Drivers of Alzheimer’s Disease Pathogenesis
Chakravorty, A., Jetto, C. T., & Manjithaya, R. R. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00311 · Cited by 219 · see citing works
Liu, Z., Li, T., Li, P., Wei, N., Zhao, Z., Liang, H., Ji, X., Chen, W., Xue, M., & Wei, J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/352723 · Cited by 208 · see citing works
OxInflammation: From Subclinical Condition to Pathological Biomarker
Valacchi, G., Virgili, F., Cervellati, C., & Pecorelli, A. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00858 · Cited by 206 · see citing works
Spermidine and spermine delay brain aging by inducing autophagy in SAMP8 mice
Xu, T., Li, H., Dai, Z., Lau, G. K., Li, B., Zhu, W., Liu, X.-Q., Liu, H.-F., Cai, W.-W., Huang, S., et al. (2020) · Aging · doi:10.18632/aging.103035 · Cited by 204 · see citing works
Zhao, F.-P., Xu, Y., Gao, S.-C., Qin, L., Austria, Q. M., Siedlak, S., Pajdzik, K., Dai, Q., He, C., Wang, W.-Z., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00484-x · Cited by 182 · see citing works
Interplay between MicroRNAs and Oxidative Stress in Neurodegenerative Diseases
Konovalova, J., Gerasymchuk, D., Parkkinen, I., Chmielarz, P., & Domanskyi, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20236055 · Cited by 199 · see citing works
Hsieh, Y.-C., Guo, C., Yalamanchili, H. K., Abreha, M., Al-Ouran, R., Li, Y., Dammer, E. B., Lah, J. J., Levey, A. I., Bennett, D. A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.104 · Cited by 196 · see citing works
Roy, R. G., Mandal, P. K., & Maroon, J. C. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00486 · Cited by 194 · see citing works
Mitochondrial Dysfunction in Alzheimers Disease: Opportunities forDrug Development
Bhatia, S., Rawal, R., Sharma, P., Singh, T., Singh, M., & Singh, V. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666210517114016 · Cited by 197 · see citing works
Tau Phosphorylation Sites Work in Concert to Promote Neurotoxicity In Vivo
Steinhilb, M. L., Dias-Santagata, D., Fulga, T. A., Felch, D. L., & Feany, M. B. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0327 · Cited by 187 · see citing works
Self-citationMehan, S., Meena, H., Sharma, D., & Sankhla, R. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9454-6 · Cited by 185 · see citing works
Chatterjee, S., Sang, T.-K., Lawless, G. M., & Jackson, G. R. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddn326 · Cited by 178 · see citing works
Pervasive Axonal Transport Deficits in Multiple Sclerosis Models
Sorbara, C. D., Wagner, N. E., Ladwig, A., Nikić, I., Merkler, D., Kleele, T., Marinković, P., Naumann, R., Godinho, L., Bareyre, F. M., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.11.006 · Cited by 168 · see citing works
Rad, S. K., Arya, A., Karimian, H., Madhavan, P., Rizwan, F., Koshy, S., & Prabhu, G. (2018) · Drug Design Development and Therapy · doi:10.2147/dddt.s173970 · Cited by 155 · see citing works
Curcumin Promotes A-beta Fibrillation and Reduces Neurotoxicity in Transgenic Drosophila
Caesar, I., Jonson, M., Nilsson, K. P. R., Thor, S., & Hammarström, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031424 · Cited by 152 · see citing works
Linking Alzheimer's disease to insulin resistance: the FoxO response to oxidative stress
Manolopoulos, K. N., Klotz, L.-O., Korsten, P., Bornstein, S. R., & Barthel, A. (2010) · Molecular Psychiatry · doi:10.1038/mp.2010.17 · Cited by 150 · see citing works
Lysosomal Dysfunction Promotes Cleavage and Neurotoxicity of Tau In Vivo
Khurana, V., Elson‐Schwab, I., Fulga, T. A., Sharp, K. A., Loewen, C. A., Mulkearns-Hubert, E. E., Tyynelä, J., Scherzer, C. R., & Feany, M. Β. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001026 · Cited by 148 · see citing works
Self-citationDumont, M., Stack, C., Elipenahli, C., Jainuddin, S., Gerges, M., Starkova, N. N., Yang, L., Starkov, A. A., & Beal, F. M. (2011) · The FASEB Journal · doi:10.1096/fj.11-186650 · Cited by 139 · see citing works
Oxidant/antioxidant imbalance and the risk of Alzheimer's disease
Moneim, A. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150325182702 · Cited by 136 · see citing works
Tauopathy: A common mechanism for neurodegeneration and brain aging
Saha, P., & Sen, N. (2019) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2019.01.007 · Cited by 128 · see citing works
Natural Antioxidant Compounds as Potential Pharmaceutical Tools against Neurodegenerative Diseases
Marino, A., Battaglini, M., Moles, N., & Ciofani, G. (2022) · ACS Omega · doi:10.1021/acsomega.2c03291 · Cited by 132 · see citing works
Soeda, Y., Yoshikawa, M., Almeida, O. F. X., Sumioka, A., Maeda, S., Osada, H., Kondoh, Y., Saito, A., Miyasaka, T., Kimura, T., et al. (2015) · Nature Communications · doi:10.1038/ncomms10216 · Cited by 126 · see citing works
Connecting the dots between tau dysfunction and neurodegeneration
Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124 · see citing works
Self-citationMetal ions influx is a double edged sword for the pathogenesis of Alzheimer’s disease
Wang, P., & Wang, Z. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.10.003 · Cited by 122 · see citing works
Zuo, L., Hemmelgarn, B. T., Chuang, C., & Best, T. M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/604658 · Cited by 118 · see citing works
Novel therapeutic strategies for the treatment of protein-misfolding diseases
Rochet, J. (2007) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399407000385 · Cited by 118 · see citing works
Zinc Binding Directly Regulates Tau Toxicity Independent of Tau Hyperphosphorylation
Huang, Y., Wu, Z., Cao, Y., Lang, M., Lu, B., & Zhou, B. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.047 · Cited by 114 · see citing works
Inaba, S., Iwai, M., Furuno, M., Tomono, Y., Kan‐no, H., Senba, I., Okayama, H., Mogi, M., Higaki, J., & Horiuchi, M. (2008) · Hypertension · doi:10.1161/hypertensionaha.108.123612 · Cited by 114 · see citing works
Genetic control of necrosis—another type of programmed cell death
McCall, K. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.09.002 · Cited by 110 · see citing works
Transgenic Drosophila models of Alzheimer’s disease and tauopathies
Iijima‐Ando, K., & Iijima, K. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0234-4 · Cited by 110 · see citing works
The Impact of Vitamin E and Other Fat-Soluble Vitamins on Alzheimer´s Disease
Grimm, M. O. W., Mett, J., & Hartmann, T. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111785 · Cited by 108 · see citing works
Protein aggregation as a paradigm of aging
Lindner, A. B., & Démarez, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.005 · Cited by 106 · see citing works
Reduced mitochondrial SOD displays mortality characteristics reminiscent of natural aging
Paul, A., Belton, A., Nag, S., Martin, I., Grotewiel, M. S., & Duttaroy, A. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.10.013 · Cited by 105 · see citing works
Self-citationJiang, W., Luo, T., Li, S., Zhou, Y., Shen, X., He, F., Xu, J., & Wang, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152371 · Cited by 104 · see citing works
Kosmidis, S., Grammenoudi, S., Papanikolopoulou, K., & Skoulakis, E. M. C. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1490-09.2010 · Cited by 105 · see citing works
Mechanistic Link between Vitamin B12 and Alzheimer’s Disease
Lauer, A. A., Grimm, H. S., Apel, B., Golobrodska, N., Kruse, L., Ratanski, E., Schulten, N., Schwarze, L., Slawik, T., Sperlich, S., et al. (2022) · Biomolecules · doi:10.3390/biom12010129 · Cited by 109 · see citing works
Protein folding diseases and neurodegeneration: Lessons learned from yeast
Winderickx, J., Delay, C., Vos, A. D., Klinger, H., Pellens, K., Vanhelmont, T., LEUVEN, F. V., & Zabrocki, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.01.020 · Cited by 102 · see citing works
Cao, W., Song, H., Gangi, T., Kelkar, A., Antani, I., Garza, D., & Konsolaki, M. (2008) · Genetics · doi:10.1534/genetics.107.078394 · Cited by 97 · see citing works
Probing Mechanisms That Underlie Human Neurodegenerative Diseases in Drosophila
Jaiswal, M., Sandoval, H., Zhang, K., Bayat, V., & Bellen, H. J. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155456 · Cited by 95 · see citing works
Du, F., Yu, Q., Kanaan, N. M., & Yan, S. S. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddab363 · Cited by 93 · see citing works
Specific activities of individual c-Jun N-terminal kinases in the brain
Haeusgen, W., Boehm, R., Zhao, Y., Herdegen, T., & Waetzig, V. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.04.014 · Cited by 93 · see citing works
Atlante, A., Amadoro, G., Bobba, A., Lidia de, B. A. R. I., Corsetti, V., Pappalardo, G., Marra, E., Calissano, P., & Passarella, S. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.07.004 · Cited by 93 · see citing works
Bahadorani, S., Bahadorani, P., Phillips, J. P., & Hilliker, A. J. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.1.35 · Cited by 91 · see citing works
The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics
Pritchard, S. M., Dolan, P. J., Vitkus, A., & Johnson, G. V. W. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01273.x · Cited by 89 · see citing works
Crosstalk between Oxidative Stress and Tauopathy
Haque, M. M., Murale, D. P., Kim, Y. K., & Lee, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081959 · Cited by 86 · see citing works
Mechanistic Link between Vitamin B12 and Alzheimer’s Disease
Lauer, A. A., Grimm, H. S., Apel, B., Golobrodska, N., Kruse, L., Ratanski, E., Schulten, N., Schwarze, L., Slawik, T., Sperlich, S., et al. (2022) · Publications of the UdS (Saarland University) · doi:10.22028/d291-35299 · Cited by 90 · see citing works
The Unfolded Protein Response Protects from Tau Neurotoxicity In Vivo
Loewen, C. A., & Feany, M. Β. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013084 · Cited by 88 · see citing works
Self-citationAD-linked, toxic NH2 human tau affects the quality control of mitochondria in neurons
Amadoro, G., Corsetti, V., Florenzano, F., Atlante, A., Ciotti, M. T., Mongiardi, M. P., Bussani, R., Nicolin, V., Nori, S. L., Campanella, M., et al. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.10.018 · Cited by 85 · see citing works
Lead (Pb) induced Oxidative Stress as a Mechanism to Cause Neurotoxicity in Drosophila melanogaster
Olakkaran, S., Anupama, K. P., Antony, A., & Gurushankara, H. P. (2021) · Toxicology · doi:10.1016/j.tox.2021.152959 · Cited by 77 · see citing works
Functional Screening of Alzheimer Pathology Genome-wide Association Signals in Drosophila
Shulman, J. M., Chipendo, P. I., Chibnik, L. B., Aubin, C., Tran, D., Keenan, B. T., Kramer, P. L., Schneider, J. A., Bennett, D., Feany, M. Β., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.01.006 · Cited by 77 · see citing works
Self-citationYu, L., Wang, W., Pang, W., Xiao, Z.-H., Jiang, Y., & Hong, Y. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161216 · Cited by 77 · see citing works
p53 prevents neurodegeneration by regulating synaptic genes
Merlo, P., Frost, B. E., Peng, S., Yang, Y. J., Park, P. J., & Feany, M. Β. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419083111 · Cited by 75 · see citing works
Self-citationOxidative challenge in Alzheimer's disease: state of knowledge and future needs
Cervellati, C., Wood, P. L., Romani, A., Valacchi, G., Squerzanti, M., Sanz, J. M., Ortolani, B., & Zuliani, G. (2016) · Journal of Investigative Medicine · doi:10.1136/jim-2015-000017 · Cited by 75 · see citing works
Synaptic Mitochondria: An Early Target of Amyloid-β and Tau in Alzheimer’s Disease
Torres, A. K., Jara, C., Park-Kang, H. S., Polanco, C. M., Tapia, D., Alarcón, F., de la Peña, A., Llanquinao, J., Vargas-Mardones, G., Álvarez‐Indo, J., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215139 · Cited by 79 · see citing works
Distinct phenotypes of three-repeat and four-repeat human tau in a transgenic model of tauopathy
Sealey, M. A., Vourkou, E., Cowan, C. M., Bossing, T., Quraishe, S., Grammenoudi, S., Skoulakis, E. M. C., & Mudher, A. K. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.05.003 · Cited by 73 · see citing works
Iijima-Ando, K., Zhao, L., Gatt, A., Shenton, C., & Iijima, K. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq068 · Cited by 72 · see citing works
Modeling the complex pathology of Alzheimer's disease in Drosophila
Fernandez-Funez, P., de Mena, L., & Rincon-Limas, D. E. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.05.013 · Cited by 69 · see citing works
Drosophila Models of Alzheimer's Disease: Advances, Limits, and Perspectives
Bouleau, S., & Tricoire, H. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142802 · Cited by 69 · see citing works
Colodner, K. J., & Feany, M. Β. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2491-10.2010 · Cited by 67 · see citing works
Self-citationTan, X. L., Wright, D. K., Liu, S., Hovens, C. M., O'Brien, T. J., & Shultz, S. R. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.05.001 · Cited by 68 · see citing works
Oxidative Stress in Invertebrate Systems
Chaitanya, R. K., Shashank, K., & Sridevi, P. (2016) · InTech eBooks · doi:10.5772/64573 · Cited by 68 · see citing works
Role of angiotensin II receptor subtype activation in cognitive function and ischaemic brain damage
Horiuchi, M., & Mogi, M. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.01167.x · Cited by 66 · see citing works
Lalouette, L., Pottier, M.-A., Wycke, M.-A., Boitard, C., Bozzolan, F., Maria, A., Demondion, E., Chertemps, T., Lucas, P., Renault, D., et al. (2015) · Environmental Science and Pollution Research · doi:10.1007/s11356-015-5923-3 · Cited by 66 · see citing works
Zhang, Z., Sheng, H., Liao, L., Chen, X., Zhang, A., Yang, Y., Zhao, L., Duan, L., Hu, C., & Zhang, B. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200686 · Cited by 67 · see citing works
Tau is required for glial lipid droplet formation and resistance to neuronal oxidative stress
Goodman, L. D., Ralhan, I., Li, X., Lu, S., Moulton, M. J., Park, Y.-J., Zhao, P., Kanca, O., Taleghani, Z. S. G., Jacquemyn, J., et al. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01740-1 · Cited by 67 · see citing works
Quintanilla, R. A., Orellana, J. A., & Rommy von Bernhardi, M. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.016 · Cited by 64 · see citing works
Brennan, L., Haukedal, J. A., Earle, J. C., Keddie, B. A., & Harris, H. L. (2012) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2012.01155.x · Cited by 64 · see citing works
Review on anti-alzheimer drug development: approaches, challenges and perspectives
Abdallah, A. E. (2024) · RSC Advances · doi:10.1039/d3ra08333k · Cited by 63 · see citing works
Prevention and Treatment of Alzheimer’s Disease: Biological Mechanisms of Exercise
McGurran, H., Glenn, J. M., Madero, E. N., & Bott, N. T. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180958 · Cited by 63 · see citing works
Apelin/APJ system: A novel promising target for neurodegenerative diseases
Luo, H., Han, L., & Xu, J. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29001 · Cited by 61 · see citing works
Reduced life span with heart and muscle dysfunction in Drosophila sarcoglycan mutants
Allikian, M. J., Bhabha, G., Dospoy, P. D., Heydemann, A., Ryder, P. V., Earley, J. U., Wolf, M. J., Rockman, H. A., & McNally, E. M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm254 · Cited by 61 · see citing works
van Leeuwen, L. A. G., & Hoozemans, J. J. M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1382-7 · Cited by 60 · see citing works
Drosophila Models of Tauopathies: What Have We Learned?
Gistelinck, M., Lambert, J., Callaerts, P., Dermaut, B., & Dourlen, P. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/970980 · Cited by 58 · see citing works
Health Benefits of Anti-aging Drugs
Piskovatska, V., Strilbytska, O. M., Koliada, A. K., Vaiserman, A. M., & Lushchak, O. V. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-3681-2_13 · Cited by 62 · see citing works
- Authors
- Dias-Santagata, D., Fulga, T. A., Duttaroy, A., & Feany, M. B.
- Affiliations
- Brigham and Women's Hospital (US)
- Howard University (US)
- Venue
- Journal of Clinical Investigation
- Published
- 2007-01-02
- Volume
- 117
- Issue
- 1
- Pages
- 236-245
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC1697799
- OpenAlex
- W1997198091
- Cited by
- 318
- References
- 61
- Citations by year
- 2026: 6 · 2025: 22 · 2024: 20 · 2023: 21 · 2022: 21 · 2021: 24 · 2020: 15 · 2019: 16 · 2018: 14 · 2017: 15 · 2016: 15 · 2015: 21 · 2014: 14 · 2013: 7 · 2012: 13
- FWCI
- 7.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Brigham and Women's Hospital
- National Institutes of Health (AG005134)
- Fundação para a Ciência e a Tecnologia (SFRH/BPD/20685/2004)
- National Institute on Aging (AG005134, AG-19790, P50AG005134, R01AG019790)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurobiology and Insect Physiology Research
- Keywords
- oxidative stress, tau protein, tauopathy, neurodegeneration, Alzheimer's disease, JNK signaling, antioxidant defense, cell cycle activation, Drosophila model, tau phosphorylation
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Drosophila, Humans, Nerve Degeneration, Paraquat, Vitamin E, tau Proteins, Oxidative Stress, Tauopathies
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