The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
Cellular response to oxidative stress: Signaling for suicide and survival*
Martindale, J. L., & Holbrook, N. J. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10119 · Cited by 2,314
Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869
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
Orr, W. C., & Sohal, R. S. (1994) · Science · doi:10.1126/science.8108730 · Cited by 1,461
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
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
Cummings, J. L. (2004) · New England Journal of Medicine · doi:10.1056/nejmra040223 · Cited by 1,152
Tauopathy in Drosophila : 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
Self-citation
Cited by
Sorted by citations
Items 201–300 of 320
UsingDrosophilamodels of neurodegenerative diseases for drug discovery
Newman, T. A., Sinadinos, C., Johnston, A. H., Sealey, M. A., & Mudher, A. K. (2011) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2011.549124 · Cited by 14
Bahadorani, S., & Hilliker, A. J. (2008) · Genome · doi:10.1139/g08-012 · Cited by 14
Zhu, Y., Tian, M., Lu, S., Qin, Y., Zhao, T. S., Shi, H., Li, Z., & Qin, D. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111253 · Cited by 13
Comparative approaches to the study of physiology:Drosophilaas a physiological tool
Neckameyer, W. S., & Argue, K. J. (2012) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00084.2012 · Cited by 13
NORMA: The Network Makeup Artist — A Web Tool for Network Annotation Visualization
Koutrouli, M., Karatzas, E., Papanikolopoulou, K., & Pavlopoulos, G. A. (2021) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2021.02.005 · Cited by 13
Jiyah, A., Muhammad, S. A., Ibrahim, A., Bulama, I., Ibrahim, A., Abbas, A. Y., Imam, M. U., Saidu, Y., & Bilbis, L. S. (2024) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2024.105618 · Cited by 13
Oxidative Stress in Elderly with Different Cognitive Status: My Mind Project
Fattoretti, P., Malavolta, M., Fabbietti, P., Papa, R., Giacconi, R., Costarelli, L., Galeazzi, R., Paoloni, C., Postacchini, D., Lattanzio, F., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171117 · Cited by 12
Toxicities of amyloid-beta and tau protein are reciprocally enhanced in the Drosophila model
Sun, Z.-D., Hu, J.-X., Wu, J.-R., Zhou, B., & Hu, J. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.336872 · Cited by 14
Vourkou, E., Paspaliaris, V., Bourouliti, A., Zerva, M.-C., Prifti, E., Papanikolopoulou, K., & Skoulakis, E. M. C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112985 · Cited by 12
Tau 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
Therapeutic 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
Cellular Uptake of Tau Aggregates Triggers Disulfide Bond Formation in Four-Repeat Tau Monomers
Krzesinski, B. J., Holub, T. J., Gabani, Z. Y., & Margittai, M. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00607 · Cited by 11
Zhang, M. Y., Lear, B. C., & Allada, R. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab303 · Cited by 11
Jin, Y., Li, X., Wei, C., & Yuan, Q. (2023) · Experimental Brain Research · doi:10.1007/s00221-023-06749-9 · Cited by 11
Adaptive responses to alloxan‐induced mild oxidative stress ameliorate certain tauopathy phenotypes
Yoshiike, Y., Yamashita, S., Mizoroki, T., Maeda, S., Murayama, M., Kimura, T., Sahara, N., Soeda, Y., & Takashima, A. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00756.x · Cited by 11
Keramidis, I., Vourkou, E., Papanikolopoulou, K., & Skoulakis, E. M. C. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.569520 · Cited by 11
Pieńkowska, N., Fahnestock, M. L., Mahadeo, C., Zaborniak, I., Chmielarz, P., Bartosz, G., & Sadowska‐Bartosz, I. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010359 · Cited by 10
Bergkvist, L., Sandin, L., Kågedal, K., & Brorsson, A. (2016) · Biology Open · doi:10.1242/bio.017194 · Cited by 10
Arnés, M., Kim, Y. A., Lannes, J., Alaniz, M. E., Cho, J. D., McCabe, B. D., & Santa‐María, I. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/607176 · Cited by 11
Chauhan, P., Wadhwa, K., & Singh, G. (2025) · Pathology - Research and Practice · doi:10.1016/j.prp.2025.156109 · Cited by 12
Biochemical and Behavioral Evaluation of Human MAPT Mutations in Transgenic Drosophila melanogaster
Haddadi, M., Nongthomba, U., & Ramesh, S. R. (2015) · Biochemical Genetics · doi:10.1007/s10528-015-9701-1 · Cited by 9
dos Santos, A., Teixeira, F. C., da Silva, D. S., Veleda, T. A., de Mello, J. E., Luduvico, K. P., Tavares, R. G., Stefanello, F. M., Cunico, W. J., & Spanevello, R. M. (2022) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2022.11.015 · Cited by 11
Early Chronic Stress Induced Changes within the Locus Coeruleus in Sporadic Alzheimer’s Disease
Minné, D., Marnewick, J. L., & Engel-Hills, P. C. (2023) · Current Alzheimer Research · doi:10.2174/1567205020666230811092956 · Cited by 10
Network analysis of S-nitrosylated synaptic proteins demonstrates unique roles in health and disease
Stykel, M. G., & Ryan, S. D. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119720 · Cited by 9
Loewen, C. A., Boekhoff‐Falk, G., Ganetzky, B., & Chtarbanova, S. (2018) · G3 Genes Genomes Genetics · doi:10.1534/g3.118.200627 · Cited by 9
Altered Gut Microbial Load and Immune Activation in a Drosophila Model of Human Tauopathy
Rydbom, J., Kohl, H., Hyde, V. R., & Lohr, K. M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.731602 · Cited by 9
Bukhari, H., Nithianandam, V., Battaglia, R. A., Cicalo, A., Sarkar, S., Comjean, A., Hu, Y., Leventhal, M. J., Dong, X., & Feany, M. Β. (2024) · Genome Research · doi:10.1101/gr.278576.123 · Cited by 11
Self-citationMurray-Cors, S., Owens, M., Liew, Y.-T., Day, M., Cairns, W., & Prokop, A. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1631752 · Cited by 9
Endogenous and Exogenous Factors in Hyperphosphorylation of Tau in Alzheimer′s Disease*
Wei, Y., Jun-Ye, M. I. A. O., & Liu, Y. M. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2012.00365 · Cited by 8
PIWIL1 protein power targets tau therapy
Soukup, S., & Verstreken, P. (2014) · Nature Neuroscience · doi:10.1038/nn.3659 · Cited by 8
P., N. N. V., Sundararajan, V., Dan, P., Venkatasubbu, G. D., & Mohideen, S. S. (2021) · Biocell · doi:10.32604/biocell.2021.015090 · Cited by 7
Drosophila as a Model for Human Viral Neuroinfections
Benoit, I., Curzio, D. L. D., Civetta, A., & Douville, R. N. (2022) · Cells · doi:10.3390/cells11172685 · Cited by 8
The Cascade of Oxidative Stress and Tau Protein Autophagic Dysfunction in Alzheimer’s Disease
Liu, Z., Li, P., Wu, J., Wang, Y., Li, P., Hou, X., Zhang, Q., Wei, N., Zhao, Z., Liang, H., et al. (2015) · InTech eBooks · doi:10.5772/59980 · Cited by 9
Advanced intranasal peptide delivery systems for improved management of Alzheimer's disease
Majie, A., Karmakar, V., Ghosh, A., Chakraborty, S., Apurva, A., Layek, B., & Gorain, B. (2025) · Biomaterials Advances · doi:10.1016/j.bioadv.2025.214474 · Cited by 8
Effects of Syzygium cumini Seed Extract on the Memory Loss of Alzheimer’s Disease Model Rats
Hossain, S., Islam, J., Bhowmick, S., Haque, M., & Rahaman, K. A. (2017) · Advances in Alzheimer s Disease · doi:10.4236/aad.2017.63005 · Cited by 7
Nikookar, H., Haddadi, M., Haghi, M., & Masoudi, R. (2021) · Archives of Gerontology and Geriatrics · doi:10.1016/j.archger.2021.104355 · Cited by 7
Autophagy as a Promising Therapeutic Target in Age-Associated Neurodegenerative Disorders
Bhaduri, I., Trisal, A., & Singh, A. K. (2023) · Springer eBooks · doi:10.1007/978-981-19-7443-4_3 · Cited by 7
hSOD1 Promotes Tau Phosphorylation and Toxicity in the Drosophila Model
Huang, Y., Wu, Z., & Zhou, B. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-141608 · Cited by 7
m6A-dependent circular RNA formation mediates tau-induced neurotoxicity
Atrian, F., Ramirez, P., De Mange, J., Marquez, M., Gonzalez, E. M., Minaya, M., Karch, C. M., & Frost, B. (2024) · doi:10.1101/2024.01.25.577211 · Cited by 7
Oxidative stress induces tau hyperphosphorylation via MARK activation in neuroblastoma N1E-115 cells
Liu, Y., Chen, Y., & Fukui, K. (2023) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.22-39 · Cited by 7
Wang, R., Li, J., Li, X., Guo, Y., Chen, P., & Tian, P. (2025) · Reviews in the Neurosciences · doi:10.1515/revneuro-2025-0013 · Cited by 7
Air pollution as a key risk factor for alzheimer’s disease: A comprehensive review
Zhu, X., Guo, C., Zhang, Y., & Wei, Y. (2025) · Environmental Technology & Innovation · doi:10.1016/j.eti.2025.104555 · Cited by 6
Selective neuronal vulnerability to deficits in RNA processing
Zuniga, G., & Frost, B. E. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102500 · Cited by 8
Xu, Y., Yu, L., Xu, R., Zhang, Y., Zhang, C., Yin, J., Bao, H., & Wang, X. (2023) · Brain Research · doi:10.1016/j.brainres.2023.148607 · Cited by 6
Molecular Modeling of Tau Proline-Directed Protein Kinase (PDPK) Inhibitors
Navarro‐Retamal, C., & Caballero, J. (2017) · Neuromethods · doi:10.1007/978-1-4939-7404-7_13 · Cited by 6
Parishin A ameliorates cognitive decline by promoting PS1 autophagy in Alzheimer’s disease
Guo, S., Yi, L., Luo, M., Dong, Z., & Du, Y. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1516190 · Cited by 5
A Drosophila model relevant to chemotherapy-related cognitive impairment
Torre, M., Bukhari, H., Nithianandam, V., Zanella, C. A., Mata, D. A., & Feany, M. Β. (2023) · Scientific Reports · doi:10.1038/s41598-023-46616-9 · Cited by 5
Self-citationKang, J., Zhang, C., Wang, Y., Peng, J., Berger, B., Perrimon, N., & Shen, J. (2023) · Genetics · doi:10.1093/genetics/iyad202 · Cited by 5
Pathways controlling neurotoxicity and proteostasis in mitochondrial complex I deficiency
Nithianandam, V., Sarkar, S., & Feany, M. Β. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae018 · Cited by 6
Self-citationHippocampal mitophagy alterations in MAPT-associated frontotemporal dementia with parkinsonism
Richardson, T., Hou, X., Fiesel, F. C., Wszolek, Z., Dickson, D. W., & Springer, W. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-01955-8 · Cited by 5
Guidelines for Studying the Oxidative Stress Damage Model on Drosophila melanogaster
Wu, Q. (2025) · Future Postharvest and Food · doi:10.1002/fpf2.70003 · Cited by 7
Bulgart, H. R., Perez, M. A. L., Tucker, A., Giarrano, G. N., Banford, K. K., Miller, O., Bonser, S. W. G., Wold, L. E., Scharre, D. W., & Weisleder, N. L. (2024) · The FASEB Journal · doi:10.1096/fj.202401731rr · Cited by 4
Zhang, L., Zhen, R.-R., Gu, C., Zhang, T.-L., Li, Y., Jin, M., Hu, B., & An, H. (2020) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-020-2834-8 · Cited by 5
RetractedAnimal models in Alzheimer's disease: Biological plausibility and mood disorders
Castillo-Rangel, C., Marín, G., Díaz-Chiguer, D. L., Zarate-Calderon, C., Viveros-Martínez, I., Salazar, F., Torres-Pasillas, J. G., Hernández-Contreras, K. A., Vega-Quesada, L. A., Cano-Ortega, Y., et al. (2023) · Neurology Perspectives · doi:10.1016/j.neurop.2023.100110 · Cited by 5
Zarini-Gakiye, E., Sanadgol, N., Parivar, K., & Vaezi, G. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00679-7 · Cited by 7
Singh, H., Mohanto, S., Bhunia, A., Singh, B. K., Chauhan, K., Kumar, A., Mishra, A., Mishra, A. K., & Shrivastav, A. (2024) · Antioxidants · doi:10.1002/9781394270576.ch8 · Cited by 5
Kumari, A., & Zeng, X.-A. (2026) · Nutrients · doi:10.3390/nu18060907 · Cited by 4
Liu, Y., Chen, Y., & Fukui, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158428 · Cited by 5
Neuronal Models for Studying Tau Pathology
Koechling, T., Lim, F., Hernández, F., & Ávila, J. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2010/528474 · Cited by 6
Kelliny, S., Xiong, J., Bobrovskaya, L., & Zhou, X. (2021) · Neurotoxicity Research · doi:10.1007/s12640-021-00405-2 · Cited by 4
Hu, R., Li, M., Chen, S., Wang, M., Tao, X., Zhu, Y., Yan, H., & Liu, Y. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012797 · Cited by 3
NEURONAL FUNCTIONS OF PROTEIN PHOSPHATASE 2A
Leung, H. (2013) · Neuroscience International · doi:10.3844/amjnsp.2013.46.55 · Cited by 3
Neurochemical Aspects of Alzheimer’s Type of Dementia
Farooqui, A. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816347-4.00003-9 · Cited by 4
Leveraging Plasma Membrane Repair Therapeutics for Treating Neurodegenerative Diseases
Bulgart, H. R., Goncalves, I., & Weisleder, N. L. (2023) · Cells · doi:10.3390/cells12121660 · Cited by 3
Plant-Derived Antioxidants as a Protective Strategy against Oxidative Stress
Kalson, P., Pathak, G. C., -, B. M., & Bhan, V. (2023) · International Journal For Multidisciplinary Research · doi:10.36948/ijfmr.2023.v05i04.4336 · Cited by 3
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
Elzayat, E. M., Husein, A., Elbeltagy, Y., Mohamed, F., & Hosney, M. (2021) · Egyptian Academic Journal of Biological Sciences. D, Histology and Histochemistry · doi:10.21608/eajbsd.2021.200376 · Cited by 3
Heat Stress Modulates the GSK-3β Levels and Tau PhosphorylationPreprint
Dubey, T., & Chinnathambi, S. (2020) · Preprints.org · doi:10.20944/preprints202007.0645.v1 · Cited by 2
Atractylenolide III alleviates amyloid-β-induced cognitive impairments in mice
Yuan, H., Xia, L., Li, J., Dai, C., Li, X., Xu, B., Xue, M., Shi, X., Wu, B., Dong, Z., et al. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-10893-6 · Cited by 2
Moreno, M. R., Cooper, A. S., Lian, T., Liu, J., Abtahi, S., Skoulakis, E. M. C., Sivanantharajah, L., Allan, D. W., & Mudher, A. K. (2026) · Disease Models & Mechanisms · doi:10.1242/dmm.052492 · Cited by 2
Drosophila Models of Tauopathy
Ali, Y., Ruan, K., & Zhai, R. G. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00054-8 · Cited by 2
Baseline Neurodegeneration Influences the Longitudinal Effects of Tau on Cognition
Ng, K. P., Initiative, A. D. N., Cheng, G. H. ‐., Yatawara, C., Rosa‐Neto, P., Gauthier, S. G., & Kandiah, N. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201425 · Cited by 2
A review on neurodegenerative diseases associated with oxidative stress and mitochondria
Almalki, W. H., Alshamrani, S. A., Fagieha, R. E., Hallabi, N. H. B., Almatrafi, L. A., & Alahmadi, T. A. (2022) · International Journal of Health Sciences · doi:10.53730/ijhs.v6ns1.6130 · Cited by 2
Cao, Y., Yang, C., Liu, C., Fan, Z., Yang, S., Song, H., & Hao, R. (2024) · Environmental Technology & Innovation · doi:10.1016/j.eti.2024.103965 · Cited by 2
Chen, Q. B., Chakraborty, S. D., Visic, P., Buford, K. D., Zong, Y., Buti, W., Odom, K. R., Lee, H., & Leal, S. M. (2015) · Mechanisms of Development · doi:10.1016/j.mod.2015.02.005 · Cited by 2
Endoplasmic Reticulum Stress and Oxidative Stress: Mechanisms and Link to Disease
Malhotra, J. D., & Kaufman, R. J. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch2 · Cited by 2
McConnell, G. C. (2008) · SMARTech Repository (Georgia Institute of Technology) · Cited by 2
Alizarin Red perturbs skeletal patterning and biomineralization via catalase inhibition
Descoteaux, A. E., Radulovic, M., Mahoney, E., Ghogale, M., Chandragiri, S., Abayawardena, D., Shrestha, B. D., Wikramanayake, A. H., Prakash, V. N., & Bradham, C. A. (2026) · Development · doi:10.1242/dev.205079 · Cited by 1
Zhu, X., Diep, Y. N., Tran, V. T. A., Kang, Y. J., Lee, L. P., & Cho, H. (2025) · BioChip Journal · doi:10.1007/s13206-025-00228-9 · Cited by 1
Multifunctional molecular agent for tau-targeted combinational therapy of Alzheimer’s disease
Wu, J., Chai, K., Tu, Y., Fang, K., Shi, S., Hu, X., Liu, J., & Yao, T. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110583 · Cited by 1
Muhammad, S. A., Aliyu, A. D., Abolaji, A. O., Jiyah, A., Bulama, I., Ibrahim, A., Abbas, A. Y., Imam, M. U., & Bilbis, L. S. (2025) · Journal of Cellular Neuroscience and Oxidative Stress · doi:10.37212/jcnos.1741523 · Cited by 1
Exploring the potential of cinnamic acid analogues in alzheimer’s disease
Patil, P., Jaiswal, S., & Prabhu, A. (2026) · DARU Journal of Pharmaceutical Sciences · doi:10.1007/s40199-026-00593-2 · Cited by 2
Oxidative stress and inflammation in neurodegenerative disorders
Jomová, K., Alomar, S. Y., Valko, R., Nepovimová, E., Kuča, K., & Valko, M. (2026) · Archives of Toxicology · doi:10.1007/s00204-026-04518-5 · Cited by 1
Chen, M., Kretzschmar, D., Verdile, G., & Lardelli, M. T. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415894-8.00025-7 · Cited by 2
Neurodegeneration models in Drosophila
Roy, B., & Jackson, G. R. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511920585.012 · Cited by 1
Neuroimmunological phenomena involved in chronic traumatic brain injury
Velasco‐González, R., Vargas‐Castro, N., Mendoza-Negrete, K., Acacio‐Martínez, D., Luna‐Mendoza, J., Méndez-Cuesta, L. A., Sotomayor-Sobrino, M. A., Ochoa-Aguilar, A., & Acevedo, C. G. (2019) · Clinical and Experimental Neuroimmunology · doi:10.1111/cen3.12492 · Cited by 1
Oxidative Stress in the Airway System of the Fruit FlyDrosophila melanogaster
Roeder, T. (2011) · doi:10.1002/9781118148143.ch19 · Cited by 1
Joshi, M., van Falier, S. J. A., & Sinnige, T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.01.668095 · Cited by 1
Mecanismos de daño celular en enfermedades neurodegenerativas
Enríquez, S. S., Mora, A. E. R., López, L. D. S. V., Becerra, B. I. C., Hernández, M. A. D., & Hita, M. E. G. (2007) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Role of C-terminus of HSC70 interacting protein in determining neuronal fate in acute injury
Stankowski, J. N. (2011)
Mitochondrial Abnormalities and Oxidative Stress in Alzheimer’s Disease
Moreira, P. I., & Oliveira, C. R. (2012) · Oxidative stress and disease · doi:10.1201/b12308-22
Animal Models of Frontotemporal Dementia
Dawson, H. N., & Laskowitz, D. T. (2010) · Neuromethods · doi:10.1007/978-1-60761-898-0_28
Drosophila model of cognitive disorders: Focus on memory abnormality
Shao, L., & Zhong, Y. (2014) · Cambridge University Press eBooks · doi:10.1017/cbo9780511920585.013
The Roles of Presenilin and FKBP14 in Drosophila Development and Notch Signalling
van de Hoef, D. L. (2009) · TSpace (University of Toronto)
ROS regulation of axonal mitochondrial transport
Liao, P. (2016) · Purdue e-Pubs (Purdue University System)
Malhotra, J. D., & Kaufman, R. J. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00276-x
Animal Models of Pathological Aging
Emmons, E. B., Kim, Y.-C., & Narayanan, N. S. (2018) · Wiley eBooks · doi:10.1002/9781118772034.ch4
Kelliny, S., Xiong, J., Bobrovskaya, L., & Zhou, X. (2021) · Research Square · doi:10.21203/rs.3.rs-306628/v1
Mitochondrial perturbation drives tau oligomers pathology in Alzheimer’s diseasePreprint
Du, F., Yu, Q., Chen, D., Yan, S. F., & Yan, S. S. (2020) · doi:10.21203/rs.3.rs-40746/v1
Ryoo, H. D. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733685711.793549102
Metadata
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review