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Rapid cell death is preceded by amyloid plaque-mediated oxidative stress
Open accessAbstract
Neuronal loss is the ultimate outcome in a variety of neurodegenerative diseases and central nerve system disorders. Understanding the sequelae of events that leads to cell death would provide insight into neuroprotective approaches. We imaged neurons in the living brain of a mouse model of Alzheimer's disease that overexpresses mutant human amyloid precursor protein and presenilin 1 and followed the death of individual neurons in real time. This mouse model exhibited limited neurodegeneration and atrophy, but we were able to identify a small fraction of vulnerable cells that would not have been detectable by using standard approaches. By exploiting a genetically encoded reporter of oxidative stress, we identified susceptible neurons by their increased redox potential. The oxidative stress was most dramatic in neurites near plaques, propagated to cell bodies, and preceded activation of caspases that led to cell death within 24 h. Thus, local oxidative stress surrounding plaques contributes to long-range toxicity and selective neuronal death in Alzheimer's disease.
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“and local oxidative stress surrounding plaques has been proposed as a potential mechanism contributing to selective neuronal death [37].”
From Neuron Loss in Alzheimer’s Disease: Translation in Transgenic Mouse Models (2020) · cites this paper as [37]
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Cites
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614
Oxidative stress hypothesis in Alzheimer’s disease
Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012
Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296
Oxidative damage to mitochondrial DNA is increased in Alzheimer’s disease
Mecocci, P., MacGarvey, U., & Beal, M. F. (1994) · Annals of Neurology · doi:10.1002/ana.410360510 · Cited by 1,037
Sayre, L., Zelasko, D. A., Harris, P. L. R., Perry, G., Salomon, R. G., & Smith, M. A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68052092.x · Cited by 1,032
Borchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., Copeland, N. G., Price, D. L., & Sisodia, S. S. (1997) · Neuron · doi:10.1016/s0896-6273(00)80974-5 · Cited by 1,023
Rapid appearance and local toxicity of amyloid-β plaques in a mouse model of Alzheimer’s disease
Meyer-Luehmann, M., Spires-Jones, T. L., Prada, C., Garcia-Alloza, M., de Calignon, A., Rozkalne, A., Koenigsknecht-Talboo, J., Holtzman, D. M., Bacskai, B. J., & Hyman, B. T. (2008) · Nature · doi:10.1038/nature06616 · Cited by 987
Self-citationKoffie, R. M., Meyer-Luehmann, M., Hashimoto, T., Adams, K. W., Mielke, M. L., Garcia-Alloza, M., Micheva, K. D., Smith, S. J., Kim, M. L., Lee, V. M., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811698106 · Cited by 850
Research works printed but not linked: 1
- 10.1523/JNEUROSCI.1879-05.2005 · DOI · Paper page
Cited by
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Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357
Grubman, A., Chew, G., Ouyang, J. F., Sun, G., Choo, X. Y., McLean, C., Simmons, R. K., Buckberry, S., Vargas-Landin, D. B., Poppe, D., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0539-4 · Cited by 956
Glial Lipid Droplets and ROS Induced by Mitochondrial Defects Promote Neurodegeneration
Liu, L., Zhang, K., Sandoval, H., Yamamoto, S., Jaiswal, M., Sanz, E., Li, Z., Hui, J., Graham, B. H., Quintana, A., et al. (2015) · Cell · doi:10.1016/j.cell.2014.12.019 · Cited by 876
Understanding mechanisms of antioxidant action in health and disease
Halliwell, B. B. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00645-4 · Cited by 709
Jiang, T., Sun, Q., & Chen, S. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.07.005 · Cited by 605
Calvo-Rodríguez, M., Hou, S. S., Snyder, A. C., Kharitonova, E. K., Russ, A., Das, S., Fan, Z., Muzikansky, A., Garcı́a-Alloza, M., Serrano‐Pozo, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16074-2 · Cited by 432
Lactate and pyruvate promote oxidative stress resistance through hormetic ROS signaling
Tauffenberger, A., Fiumelli, H., Almustafa, S., & Magistretti, P. J. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1877-6 · Cited by 352
Sadleir, K. R., Kandalepas, P. C., Buggia-Prévot, V., Nicholson, D. A., Thinakaran, G., & Vassar, R. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1558-9 · Cited by 294
Dissecting Redox Biology Using Fluorescent Protein Sensors
Schwarzländer, M., Dick, T. P., Meyer, A. J., & Morgan, B. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6266 · Cited by 310
Mitochondria and Calcium in Alzheimer’s Disease: From Cell Signaling to Neuronal Cell Death
Calvo-Rodriguez, M., & Bacskai, B. J. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2020.10.004 · Cited by 254
Role of Copper in the Onset of Alzheimer’s Disease Compared to Other Metals
Bagheri, S., Squitti, R., Haertlé, T., Siotto, M., & Saboury, A. A. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00446 · Cited by 235
The role of different SIRT1-mediated signaling pathways in toxic injury
Ren, Z., He, H., Zuo, Z., Xu, Z., Wei, Z., & Deng, J. (2019) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-019-0158-9 · Cited by 197
Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model
Xie, H., Guan, J., Borrelli, L. A., Xu, J., Serrano-Pozo, A., & Bacskai, B. J. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1836-13.2013 · Cited by 185
“roGFP was introduced into the construct pAAV-CBA-roGFP1-WPRE and the ratio of the emission fluorescence excited at 800 and 900 nm was used as an index of the redox status of roGFP (Xie et al., 2013).”
BackgroundMethodInfluentialBuccellato, F. R., D’Anca, M., Fenoglio, C., Scarpini, E., & Galimberti, D. (2021) · Antioxidants · doi:10.3390/antiox10091353 · Cited by 179
Antioxidant gene therapy against neuronal cell death
Navarro-Yepes, J., Zavala-Flores, L. M., Anandhan, A., Wang, F., Skotak, M., Chandra, N., Li, M., Pappa, A., Martínez‐Fong, D., Razo, L. M. D., et al. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.007 · Cited by 182
Lü, Y., Guo, Z., Zhang, Y., Li, C., Zhang, Y., Guo, Q., Chen, Q., Chen, X., He, X., Liu, L., et al. (2018) · Advanced Science · doi:10.1002/advs.201801586 · Cited by 164
Oxidative stress and lipid peroxidation are upstream of amyloid pathology
Arimon, M., Takeda, S., Post, K. E., Svirsky, S. E., Hyman, B. T., & Berezovska, O. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.06.013 · Cited by 157
Ullah, R., Khan, M., Shah, S. A., Saeed, K. M., & Kim, M. O. (2019) · Nutrients · doi:10.3390/nu11061195 · Cited by 158
Copper Toxicity Links to Pathogenesis of Alzheimer’s Disease and Therapeutics Approaches
Ijaz, H. W., Wang, W., & Lang, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207660 · Cited by 146
Konno, T., Melo, E. P., Chambers, J. E., & Avezov, E. (2021) · Cells · doi:10.3390/cells10020233 · Cited by 143
Mitochondrial Dysfunction in Alzheimer’s Disease: A Biomarker of the Future?
Bell, S., Barnes, K., Marco, M. D., Shaw, P. J., Ferraiuolo, L., Blackburn, D. J., Venneri, A., & Mortiboys, H. (2021) · Biomedicines · doi:10.3390/biomedicines9010063 · Cited by 138
Liu, P., Zhang, T., Chen, Q., Li, C., Chu, Y., Guo, Q., Zhang, Y., Zhou, W., Chen, H., Zhou, Z., et al. (2021) · Advanced Materials · doi:10.1002/adma.202100746 · Cited by 140
Yang, J., Zhang, X., Yuan, P., Yang, J., Xu, Y., Grutzendler, J., Shao, Y., Moore, A. V., & Ran, C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706248114 · Cited by 133
Villavicencio-Tejo, F., & Quintanilla, R. A. (2021) · Antioxidants · doi:10.3390/antiox10071069 · Cited by 143
Zhang, J., Cao, Q., Li, S., Lu, X., Zhao, Y., Guan, J., Chen, J., Wu, Q., & Chen, G. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.06.043 · Cited by 130
Astroglial connexin43 contributes to neuronal suffering in a mouse model of Alzheimer’s disease
Yi, C., Mei, X., Ezan, P., Mato, S., Matias, I., Giaume, C., & Koulakoff, A. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.63 · Cited by 133
Rahman, S. O., Panda, B. P., Parvez, S., Kaundal, M., Hussain, S., Akhtar, M., & Najmi, A. K. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.11.043 · Cited by 131
Benseny‐Cases, N., Klementieva, O. L., Cotte, M., Ferrer, I., & Cladera, J. (2014) · Analytical Chemistry · doi:10.1021/ac502667b · Cited by 122
Zhang, J., Shi, R., Li, H., Xiang, Y., Xiao, L., Hu, M., Ma, F., Ma, C. W., & Huang, Z. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.09.031 · Cited by 112
Molecular crosstalk between cancer and neurodegenerative diseases
Seo, J., & Park, M. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03428-3 · Cited by 109
Yi, C., Ezan, P., Fernández, P., Schmitt, J., Sáez, J. C., Giaume, C., & Koulakoff, A. (2017) · Glia · doi:10.1002/glia.23182 · Cited by 107
The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer’s Disease
Sulistio, Y. A., & Heese, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9063-4 · Cited by 93
Park, J., Choi, H., Min, J., Kim, B., Lee, S., Yun, J. W., Choi, M., Chang, K., & Lee, D. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.12984 · Cited by 93
Calvo-Rodríguez, M., Kharitonova, E. K., Snyder, A. C., Hou, S. S., Sanchez-Mico, M. V., Das, S., Fan, Z., Shirani, H., Nilsson, K. P. R., Serrano‐Pozo, A., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00702-2 · Cited by 100
Karvandi, M. S., Hesari, F. S., Aref, A. R., & Mahdavi, M. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1105247 · Cited by 97
Kapila, A. K., Watts, H. R., Wang, T., & Ma, D. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132258 · Cited by 88
Kim, B., Park, J., Chang, K., & Lee, D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.015 · Cited by 86
Prasad, K. N. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.01.002 · Cited by 83
Sancataldo, G., Vetri, V., Foderà, V., Cara, G. D., Militello, V., & Leone, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084552 · Cited by 79
Xie, H. B., Liu, Y., Zhu, Y., Ding, X., Yang, Y., & Guan, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316808111 · Cited by 82
Neuron Loss in Alzheimer’s Disease: Translation in Transgenic Mouse Models
Wirths, O., & Zampar, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218144 · Cited by 75
“Nonetheless, thioflavin S-positive fibrillary Aβ deposits contribute to focal neuronal toxicity, at least in their immediate environment, as shown in both AD cases and AD transgenic mice [36] and local oxidative stress surrounding plaques has been proposed as a potential mechanism contributing to selective neuronal de…”
BackgroundThe Bewildering Effect of AMPK Activators in Alzheimer’s Disease: Review of the Current Evidence
Assefa, B. T., Tafere, G. G., Wondafrash, D. Z., & Gidey, M. T. (2020) · BioMed Research International · doi:10.1155/2020/9895121 · Cited by 76
van Creveld, S. G., Rosenwasser, S., Schatz, D., Koren, I., & Vardi, A. (2014) · The ISME Journal · doi:10.1038/ismej.2014.136 · Cited by 75
eEF2K inhibition blocks Aβ42 neurotoxicity by promoting an NRF2 antioxidant response
Jan, A., Jansonius, B., Delaidelli, A., Somasekharan, S. P., Bhanshali, F., Vandal, M., Negri, G. L., Moerman, D. G., Mackenzie, I. R., Calon, F., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1634-1 · Cited by 74
Röhr, D., Boon, B. D. C., Schuler, M., Kremer, K., Hoozemans, J. J. M., Bouwman, F. H., El-Mashtoly, S. F., Nabers, A., Großerueschkamp, F., Rozemuller, A. J. M., et al. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01091-5 · Cited by 77
New tools for redox biology: From imaging to manipulation
Bilan, D. S., & Belousov, V. V. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.004 · Cited by 73
Dietary natural products as epigenetic modifiers in aging-associated inflammation and disease
Evans, L. W., Stratton, M. S., & Ferguson, B. S. (2020) · Natural Product Reports · doi:10.1039/c9np00057g · Cited by 71
Moulin, M., & Ferreiro, A. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.08.003 · Cited by 68
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Raut, S., Bhalerao, A., Powers, M., Gonzalez, M., Mancuso, S., & Cucullo, L. (2023) · Cells · doi:10.3390/cells12162019 · Cited by 65
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Kostyuk, A. I., Panova, A. S., Kokova, A. D., Kotova, D. A., Maltsev, D. I., Podgorny, O. V., Belousov, V. V., & Bilan, D. S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218164 · Cited by 66
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
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Reissaus, C. A., Piñeros, A. R., Twigg, A. N., Orr, K. S., Conteh, A. M., Irizarry, M. M. M., Kamocka, M. M., Day, R. N., Tersey, S. A., Mirmira, R. G., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-44777-0 · Cited by 53
Bi, R., Zhang, W., Zhang, D., Xu, M., Fan, Y., Hu, Q.-X., Jiang, H., Tan, L., Li, T., Fang, Y., et al. (2018) · Neuropsychopharmacology · doi:10.1038/s41386-018-0144-3 · Cited by 54
Activators of Nrf2 to Counteract Neurodegenerative Diseases
Amoroso, R., Maccallini, C., & Bellezza, I. (2023) · Antioxidants · doi:10.3390/antiox12030778 · Cited by 49
CART treatment improves memory and synaptic structure in APP/PS1 mice
Jin, J., Liou, A. K. F., Shi, Y., Yin, K., Chen, L., Li, L., Zhu, X., Qian, L., Yang, R., Chen, J., et al. (2015) · Scientific Reports · doi:10.1038/srep10224 · Cited by 48
Curcumin Scaffold as a Multifunctional Tool for Alzheimer’s Disease Research
Yang, H., Zeng, F., Luo, Y., Zheng, C., Ran, C., & Yang, J. (2022) · Molecules · doi:10.3390/molecules27123879 · Cited by 52
In Vivo Imaging of Microglia With Multiphoton Microscopy
Hierro‐Bujalance, C., Bacskai, B. J., & García-Alloza, M. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00218 · Cited by 50
Pulse Pressure: An Emerging Therapeutic Target for Dementia
Levin, R., Carnegie, M. H., & Celermajer, D. S. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00669 · Cited by 48
An insight into the in vivo imaging potential of curcumin analogues as fluorescence probes
Liu, Y., Zhang, C., Pan, H., Li, L., Yu, Y., & Liu, B. (2020) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2020.11.003 · Cited by 47
Sullivan, S. E., Dillon, G. M., Sullivan, J. M., & Ho, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.541003 · Cited by 44
β-amyloid and Oxidative Stress: Perspectives in Drug Development
Caruso, G., Spampinato, S. F., Cardaci, V., Caraci, F., Sortino, M. A., & Merlo, S. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666191209115431 · Cited by 45
Trujillo‐Estrada, L., Jiménez, S., Castro, V. D., Torres, M., Baglietto‐Vargas, D., Moreno‐González, I., Navarro, V., Sanchez-Varo, R. M., Sánchez‐Mejías, E., Dávila, J. C., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-73 · Cited by 44
Bioorthogonal chemical labeling of endogenous neurotransmitter receptors in living mouse brains
Nonaka, H., Sakamoto, S., Shiraiwa, K., Ishikawa, M., Tamura, T., Okuno, K., Kondo, T., Kiyonaka, S., Susaki, E. A., Shimizu, C., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313887121 · Cited by 41
Cyclin dependent kinase 5: A novel avenue for Alzheimer’s disease
Bhounsule, A. S., Bhatt, L. K., Prabhavalkar, K. S., & Oza, M. J. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.05.006 · Cited by 43
Boonruamkaew, P., Chonpathompikunlert, P., Vong, L. B., Sakaue, S., Tomidokoro, Y., Ishii, K., Tamaoka, A., & Nagasaki, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-03411-7 · Cited by 43
Hafez, H. A., Kamel, M. A. E.-N., Osman, M. Y. H., Osman, H., Elblehi, S. S., & Mahmoud, S. A. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04079-4 · Cited by 42
O'Farrell, K., Fagan, E., Connor, T., & Harkin, A. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.07.008 · Cited by 38
Alsharif, I., Boukhzar, L., Lefranc, B., Godefroy, D., Aury‐Landas, J., do Rego, J. L., do-Rego, J.-C., Naudet, F., Arabo, A., Chagraoui, A., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101839 · Cited by 42
Kruk-Słomka, M., Boguszewska‐Czubara, A., Słomka, T., Budzyńska, B., & Biała, G. (2015) · Neural Plasticity · doi:10.1155/2016/9815092 · Cited by 37
Ouyang, Y., Chen, Z., Tan, M., Liu, A., Chen, M., Liu, J., Pi, R., & Fang, J. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.10.160 · Cited by 36
Lentivirus-Mediated HDAC3 Inhibition Attenuates Oxidative Stress in APPswe/PS1dE9 Mice
Yu, L., Liu, Y., Jin, Y., Cao, X., Chen, J., Jin, J., Gu, Y., Bao, X., Ren, Z., Xu, Y., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170844 · Cited by 37
Lv, G., Shen, Y., Zheng, W., Yang, J., Li, C., & Lin, J. (2019) · Advanced Therapeutics · doi:10.1002/adtp.201900054 · Cited by 34
Sabaani, N. A. A. (2020) · Journal of Ocular Pharmacology and Therapeutics · doi:10.1089/jop.2019.0151 · Cited by 34
Wan, T., Fu, M., Jiang, Y., Jiang, W., Li, P., & Zhou, S. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03448-1 · Cited by 38
Organic silicon protects human neuroblastoma SH-SY5Y cells against hydrogen peroxide effects
Garcimartín, A., Merino, J. J., González, M. P., Sánchez-Reus, M. I., Sánchez-Muniz, F. J., Bastida, S., & Benedı́, J. (2014) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-14-384 · Cited by 34
Free Heme and Amyloid-β: A Fatal Liaison in Alzheimer’s Disease
Chiziane, E., Telemann, H., Krueger, M. C., Adler, J., Arnhold, J., Alia, A., & Flemmig, J. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170711 · Cited by 33
Neuronal glutathione loss leads to neurodegeneration involving gasdermin activation
Hashimoto, S., Matsuba, Y., Takahashi, M., Kamano, N., Watamura, N., Sasaguri, H., Takado, Y., Yoshihara, Y., Saito, T., & Saido, T. C. (2023) · Scientific Reports · doi:10.1038/s41598-023-27653-w · Cited by 36
Perrotte, M., Page, A. Y. L., Fournet, M., Sayec, M. L., Rassart, É., Fülöp, T., & Ramassamy, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.452 · Cited by 33
Nopparat, C., Chantadul, V., Permpoonputtana, K., & Govitrapong, P. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.04.001 · Cited by 35
Lactate: elucidating its indispensable role in human health
Zhang, S., Wang, J., Xu, Z., Cheng, Z., Shao, B., & Yu, J. (2026) · Molecular Cancer · doi:10.1186/s12943-025-02519-z · Cited by 35
Byun, J., Son, S. M., Cha, M.-Y., Shong, M., Hwang, Y. J., Kim, Y. S., Ryu, H., Moon, M., Kim, K.-S., & Mook‐Jung, I. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.184 · Cited by 31
Lee, Y. F., Russ, A., Zhao, Q., Perle, S. J., Maci, M., Miller, M. R., Hou, S. S., Algamal, M., Zhao, Z., Li, H., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-40402-3 · Cited by 30
Park, J., Kim, B., Chae, U., Lee, D. G., Kam, M. K., Lee, S., Lee, S., Lee, H., Park, J., & Lee, D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6810 · Cited by 28
Rodríguez‐Chávez, J. L., Coballase-Urrutía, E., Nieto‐Camacho, A., & Delgado, G. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/843237 · Cited by 28
The Role of Reactive Oxygen Species in Alzheimer's Disease: From Mechanism to Biomaterials Therapy
Yu, Z., & Luo, F. H. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202304373 · Cited by 30
Mitochondria and the Repurposing of Diabetes Drugs for Off-Label Health Benefits
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Metadata
- Authors
- Xie, H., Hou, S., Jiang, J., Sekutowicz, M., Kelly, J., & Bacskai, B. J.
- Affiliations
- Massachusetts General Hospital (US)
- Tsinghua University (CN)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2013-04-22
- Volume
- 110
- Issue
- 19
- Pages
- 7904-7909
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3651444
- OpenAlex
- W2086831255
- Cited by
- 172
- References
- 29
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 15 · 2023: 11 · 2022: 12 · 2021: 14 · 2020: 16 · 2019: 17 · 2018: 11 · 2017: 8 · 2016: 11 · 2015: 13 · 2014: 14 · 2013: 8
- FWCI
- 10.65
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG024688, R01AG024688)
- National Institute of Biomedical Imaging and Bioengineering (EB 000768, R01EB000768)
- National Center for Research Resources (S10RR025645)
- 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
- Alzheimer's disease, amyloid plaques, oxidative stress, neuronal cell death, presenilin 1, amyloid precursor protein, caspase activation, neurodegeneration, neuroprotection
- MeSH terms
- Alzheimer Disease, Animals, Atrophy, Gene Expression Regulation, Image Processing, Computer-Assisted, Mice, Transgenic, Neurons, Oxidation-Reduction, Time Factors, Cell Death, Oxidative Stress, Caspases, Green Fluorescent Proteins, Mice, Plaque, Amyloid
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