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Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Open accessAbstract
Reactive oxygen and nitrogen species change cellular responses through diverse mechanisms that are now being defined. At low levels, they are signalling molecules, and at high levels, they damage organelles, particularly the mitochondria. Oxidative damage and the associated mitochondrial dysfunction may result in energy depletion, accumulation of cytotoxic mediators and cell death. Understanding the interface between stress adaptation and cell death then is important for understanding redox biology and disease pathogenesis. Recent studies have found that one major sensor of redox signalling at this switch in cellular responses is autophagy. Autophagic activities are mediated by a complex molecular machinery including more than 30 Atg (AuTophaGy-related) proteins and 50 lysosomal hydrolases. Autophagosomes form membrane structures, sequester damaged, oxidized or dysfunctional intracellular components and organelles, and direct them to the lysosomes for degradation. This autophagic process is the sole known mechanism for mitochondrial turnover. It has been speculated that dysfunction of autophagy may result in abnormal mitochondrial function and oxidative or nitrative stress. Emerging investigations have provided new understanding of how autophagy of mitochondria (also known as mitophagy) is controlled, and the impact of autophagic dysfunction on cellular oxidative stress. The present review highlights recent studies on redox signalling in the regulation of autophagy, in the context of the basic mechanisms of mitophagy. Furthermore, we discuss the impact of autophagy on mitochondrial function and accumulation of reactive species. This is particularly relevant to degenerative diseases in which oxidative stress occurs over time, and dysfunction in both the mitochondrial and autophagic pathways play a role.
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“Oxidative stress has been shown to be an initiator and major contributor to both endoplasmic reticulum (ER) stress (Hotamisligil 2010; Kaneto et al. 2005) and lysosome-mediated autophagy (Lee et al. 2012)”
From Particulate matter 2.5 damages skin cells by inducing oxidative stress, subcellular organelle dysfunction, and apoptosis (2018) · cites this paper as Lee et al. 2012
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“In response to oxidative stress, autophagy increases in an attempt to remove oxidatively damaged organelles (Lee et al., 2012; Seo et al., 2012).”
From Microtubule-associated protein 1 light chain 3B, (LC3B) is necessary to maintain lipid-mediated homeostasis in the retinal pigment epithelium (2018) · cites this paper as Lee et al., 2012
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2 retracted
Mariño, G., Salvador-Montoliu, N., Fueyo, A., Knecht, E., Mizushima, N., & López-Otı́n, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701194200 · Cited by 427
RetractedChen, W., Li, N., Chen, T., Han, Y., Li, C., Wang, Y., He, W., Zhang, L., Wan, T. Y., & Cao, X. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502190200 · Cited by 82
RetractedHow mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026
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Items 101–200 of 999
Chang, K., Liu, P., Chang, C., Lin, Y., Chen, Y., & Shu, C. (2022) · Cell & Bioscience · doi:10.1186/s13578-021-00736-9 · Cited by 174
Autophagy Modulated by Inorganic Nanomaterials
Guo, L., He, N., Zhao, Y., Liu, T., & Deng, Y. (2020) · Theranostics · doi:10.7150/thno.40414 · Cited by 166
Reactive oxygen species and colorectal cancer
Lin, S., Li, Y., Zamyatnin, A. A., Werner, J., & Bazhin, A. V. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26356 · Cited by 164
Unravelling the mechanisms regulating muscle mitochondrial biogenesis
Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159
Melatonin and Autophagy in Aging-Related Neurodegenerative Diseases
Luo, F., Sandhu, A. F., Rungratanawanich, W., Williams, G. E., Akbar, M. D., Zhou, S., Song, B., & Wang, X. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197174 · Cited by 162
Zuo, W., Zhang, S., Xia, C., Guo, X., He, W., & Chen, N. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.07.002 · Cited by 158
Wu, S., Wu, Y., Wu, T.-P., & Wei, Y. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.10.034 · Cited by 164
Antioxidants Targeting Mitochondrial Oxidative Stress: Promising Neuroprotectants for Epilepsy
Yang, N., Guan, Q.-W., Chen, F., Xia, Q., Yin, X., Zhou, H.-H., & Mao, X. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6687185 · Cited by 161
Rutin as Neuroprotective Agent: From Bench to Bedside
Budzyńska, B., Faggio, C., Kruk-Słomka, M., Šamec, D., Nabavi, S. F., Sureda, A., Devi, K. P., & Nabavi, S. M. (2017) · Current Medicinal Chemistry · doi:10.2174/0929867324666171003114154 · Cited by 157
Zhu, T., Zou, L., Li, Y., Yao, X., Xu, F., Deng, X., Zhang, D., & Lin, H. (2018) · Plant Biotechnology Journal · doi:10.1111/pbi.12939 · Cited by 160
Jia, S., Xu, X., Zhou, S., Chen, Y., Ding, G., & Cao, L. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1366-y · Cited by 158
Regulation of autophagy by protein post-translational modification
Wani, W. Y., Boyer‐Guittaut, M., Dodson, M. B., Chatham, J. C., Darley-Usmar, V. M., & Zhang, J. (2014) · Laboratory Investigation · doi:10.1038/labinvest.2014.131 · Cited by 160
Self-citationOxidative Stress and Vascular Dysfunction in the Retina: Therapeutic Strategies
Ruan, Y., Jiang, S., Musayeva, A., & Gericke, A. (2020) · Antioxidants · doi:10.3390/antiox9080761 · Cited by 171
Bio‐Coreactant‐Enhanced Electrochemiluminescence Microscopy of Intracellular Structure and Transport
Ma, C., Wu, S., Zhou, Y., Wei, H., Zhang, J., Chen, Z., Zhu, J., Lin, Y., & Zhu, W. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202012171 · Cited by 158
Self-citationDing, Z., Wang, X., Schnackenberg, L. K., Khaidakov, M., Liu, S., Singla, S., Dai, Y., & Mehta, J. L. (2013) · International Journal of Cardiology · doi:10.1016/j.ijcard.2012.12.045 · Cited by 154
Oxidative stress induces autophagy in response to multiple noxious stimuli in retinal ganglion cells
Lin, W., & Kuang, H. (2014) · Autophagy · doi:10.4161/auto.36076 · Cited by 154
Ma, K., Shao, Z., Yang, S., Wang, J., Wang, B., Xiong, L., Wu, Q., & Chen, S.-F. (2013) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2013.10.002 · Cited by 153
The promising future of nano-antioxidant therapy against environmental pollutants induced-toxicities
Eftekhari, A., Dizaj, S. M., Chodari, L., Sunar, S., Hasanzadeh, A., Ahmadian, E., & Hasanzadeh, M. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.04.126 · Cited by 151
Crosstalks between inflammasome and autophagy in cancer
Chung, C., Seo, W., Silwal, P., & Jo, E. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00936-9 · Cited by 149
Autophagy Dysregulation in ALS: When Protein Aggregates Get Out of Hand
Ramesh, N., & Pandey, U. B. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00263 · Cited by 161
Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview
Pockley, A. G., & Henderson, B. E. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0522 · Cited by 149
The Link between Chronic Stress and Accelerated Aging
Yegorov, Y. E., Poznyak, A. V., Nikiforov, N. G., Sobenin, I. A., & Orekhov, A. N. (2020) · Biomedicines · doi:10.3390/biomedicines8070198 · Cited by 147
Jurcău, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111847 · Cited by 152
Promising cannabinoid-based therapies for Parkinson’s disease: motor symptoms to neuroprotection
More, S. V., & Choi, D. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0012-0 · Cited by 148
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Sun, H., Jiang, C., Wu, L., Bai, X., & Zhai, S. (2019) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00414 · Cited by 151
Oxidative stress in the lung – The essential paradox
Rogers, L. K., & Cismowski, M. J. (2017) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2017.09.001 · Cited by 148
Fasting enhances cold resistance in fish through stimulating lipid catabolism and autophagy
Lu, D., Ma, Q., Wang, J., Li, L., Han, S., Limbu, S. M., Li, D., Chen, L., Zhang, M., & Du, Z. (2019) · The Journal of Physiology · doi:10.1113/jp277091 · Cited by 148
Talbert, E. E., Smuder, A. J., Min, K., Kwon, O. S., Szeto, H. H., & Powers, S. K. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00471.2013 · Cited by 143
Landis, G. N., Shen, J., & Tower, J. (2012) · Aging · doi:10.18632/aging.100499 · Cited by 142
Oxidative stress-induced apoptosis and autophagy: Balancing the contrary forces in spermatogenesis
Sharma, P., Kaushal, N., Saleth, L. R., Ghavami, S., Dhingra, S., & Kaur, P. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166742 · Cited by 148
Redox Mechanisms in Neurodegeneration: From Disease Outcomes to Therapeutic Opportunities
Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7321 · Cited by 149
Roles of sigma-1 receptors on mitochondrial functions relevant to neurodegenerative diseases
Weng, T.-Y., Tsai, S., & Su, T. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0380-6 · Cited by 142
Chen, Y., Qiao, L., Ji, L., & Chao, H. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.09.051 · Cited by 137
Role of AMPK activation in oxidative cell damage: Implications for alcohol-induced liver disease
Sid, B., Verrax, J., & Calderón, P. B. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.05.007 · Cited by 141
Differential regulation of autophagy and mitophagy in pulmonary diseases
Aggarwal, S., Mannam, P., & Zhang, J. (2016) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00128.2016 · Cited by 137
Self-citationMitophagy mechanisms and role in human diseases
Redmann, M., Dodson, M. B., Boyer‐Guittaut, M., Darley-Usmar, V. M., & Zhang, J. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.05.010 · Cited by 138
Self-citationCadmium-Based Quantum Dot Induced Autophagy Formation for Cell Survival via Oxidative Stress
Luo, Y.-H., Wu, S., Wei, Y., Chen, Y.-C., Tsai, M., Ho, C.-C., Lin, S., Yang, C., & Lin, P. (2013) · Chemical Research in Toxicology · doi:10.1021/tx300455k · Cited by 135
Augmenting Tumor‐Starvation Therapy by Cancer Cell Autophagy Inhibition
Yang, B., Ding, L., Chen, Y., & Shi, J. (2020) · Advanced Science · doi:10.1002/advs.201902847 · Cited by 137
Zhang, J. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.003 · Cited by 141
Self-citationLionaki, E., Markaki, M., Palikaras, K., & Tavernarakis, N. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.04.010 · Cited by 137
Cross-cancer profiling of molecular alterations within the human autophagy interaction network
Lebovitz, C. B., Robertson, A. G., Goya, R., Jones, S. J. M., Morin, R. D., Marra, M. A., & Gorski, S. M. (2015) · Autophagy · doi:10.1080/15548627.2015.1067362 · Cited by 136
Redox state and methods to evaluate oxidative stress in liver damage: From bench to bedside.
Arauz, J., Ramos‐Tovar, E., & Muriel, P. (2016) · PubMed · doi:10.5604/16652681.1193701 · Cited by 132
The interaction mechanism between autophagy and apoptosis in colon cancer
Xie, Q., Liu, Y., & Li, X. (2020) · Translational Oncology · doi:10.1016/j.tranon.2020.100871 · Cited by 141
Lipid-induced NOX2 activation inhibits autophagic flux by impairing lysosomal enzyme activity
Jaishy, B. P., Zhang, Q., Chung, H. S., Riehle, C., Soto, J. E., Jenkins, S., Abel, P., Cowart, L. A., Eyk, J. E. V., & Abel, E. D. (2014) · Journal of Lipid Research · doi:10.1194/jlr.m055152 · Cited by 132
Feng, Y., Jia, Y., Su, L., Wang, D., Lv, L., Xu, L., & Yao, Y. (2013) · Autophagy · doi:10.4161/auto.25468 · Cited by 130
Lin, Z., Wu, F., Lin, S., Pan, X., Jin, L., Lü, T., Shi, L., Wang, Y., Xu, A., & Li, X. (2014) · Journal of Hepatology · doi:10.1016/j.jhep.2014.05.033 · Cited by 129
Modulation of three key innate immune pathways for the most common retinal degenerative diseases
Akhtar‐Schäfer, I., Wang, L., Krohne, T. U., Xu, H., & Langmann, T. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708259 · Cited by 129
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Genova, M. L., & Lenaz, G. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6214 · Cited by 129
Heidari, R., Ahmadi, A., Mohammadi, H., Ommati, M. M., Azarpira, N., & Niknahad, H. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.08.050 · Cited by 126
Shiroto, T., Romero, N., Sugiyama, T., Sartoretto, J. L., Kalwa, H., Yan, Z., Shimokawa, H., & Michel, T. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087871 · Cited by 125
Michalak, K. P., & Michalak, A. Z. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1558263 · Cited by 148
Members, E. W. E., Terron, A., Bal-Price, A., Paini, A., Monnet-Tschudi, F., Bennekou, S. H., Leist, M., & Schildknecht, S. (2018) · Archives of Toxicology · doi:10.1007/s00204-017-2133-4 · Cited by 124
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Peters, A. E., Mihalas, B. P., Bromfield, E. G., Roman, S. D., Nixon, B., & Sutherland, J. M. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7986 · Cited by 125
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Piantadosi, C. A., & Suliman, H. B. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022516-034322 · Cited by 124
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Fan, X., Wheatley, E., & Villeda, S. (2017) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-072116-031357 · Cited by 132
Hassanzadeh, K., & Rahimmi, A. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26865 · Cited by 126
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Xie, K., Song, Y., Zhang, W., Hao, J., Liu, Z., & Chen, Y. (2018) · Technological Forecasting and Social Change · doi:10.1016/j.techfore.2018.01.021 · Cited by 121
Ou, J., Ball, J. M., Luan, Y., Zhao, T., Miyagishima, K. J., Xu, Y., Zhou, H., Chen, J., Merriman, D. K., Xie, Z., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.010 · Cited by 123
Addis, R., Campesi, I., Fois, M., Capobianco, G., Dessole, S., Fenu, G., Montella, A., Cattaneo, M. G., Vicentini, L. M., & Franconi, F. (2014) · Biology of Sex Differences · doi:10.1186/s13293-014-0018-2 · Cited by 120
Singh, N., Lawana, V., Luo, J. D., Phong, P., Abdalla, A., Palanisamy, B. N., Rokad, D., Sarkar, S., Jin, H., Anantharam, V., et al. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.05.019 · Cited by 120
Nitric oxide and its derivatives in the cancer battlefield
Kamm, A., Przychodzen, P., Kuban-Jankowska, A., Jacewicz, D., Dabrowska, A. M., Nussberger, S., Wozniak, M., & Gorska-Ponikowska, M. (2019) · Nitric Oxide · doi:10.1016/j.niox.2019.09.005 · Cited by 120
Loss of conserved Gsdma3 self-regulation causes autophagy and cell death
Shi, P., Tang, A., Xian, L., Hou, S., Zou, D., Lv, Y.-S., Huang, Z., Wang, Q., Song, A., Lin, Z., et al. (2015) · Biochemical Journal · doi:10.1042/bj20150204 · Cited by 115
Aging: Molecular Pathways and Implications on the Cardiovascular System
de Almeida, A. J. P. O., Ribeiro, T. P., & de Medeiros, I. A. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7941563 · Cited by 120
cGAS-mediated autophagy protects the liver from ischemia-reperfusion injury independently of STING
Lei, Z., Deng, M., Yi, Z., Sun, Q., Shapiro, R. A., Xu, H., Li, T., Loughran, P., Griepentrog, J. E., Huang, H., et al. (2018) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00326.2017 · Cited by 122
Amiel, E., Everts, B., Fritz, D. I., Beauchamp, S., Ge, B., Pearce, E. L., & Pearce, E. J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302498 · Cited by 120
Sen, U., Pushpakumar, S. B., Kundu, S., Givvimani, S., Coley, D. M., Mishra, P. K., Qipshidze, N., Tyagi, N., Metreveli, N. S., & Tyagi, S. C. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00398.2011 · Cited by 118
Boyer‐Guittaut, M., Poillet-Perez, L., Liang, Q., Bôle‐Richard, E., Ouyang, X., Benavides, G. A., Chakrama, F. Z., Fraîchard, A., Darley-Usmar, V. M., Despouy, G., et al. (2014) · Autophagy · doi:10.4161/auto.28390 · Cited by 121
Self-citationSebori, R., Kuno, A., Hosoda, R., Hayashi, T., & Horio, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9179270 · Cited by 114
Tapia, C., Bianchi, M., Pallaske, G., & Bassi, A. M. (2021) · European Planning Studies · doi:10.1080/09654313.2020.1867511 · Cited by 135
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Nakahira, K., Cloonan, S. M., Mizumura, K., Choi, A. M. K., & Ryter, S. W. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5373 · Cited by 115
Mitochondrial toxicity of tobacco smoke and air pollution
Fetterman, J. L., Sammy, M. J., & Ballinger, S. W. (2017) · Toxicology · doi:10.1016/j.tox.2017.08.002 · Cited by 117
He, J., Liu, J., Huang, Y., Tang, X., Xiao, H., & Hu, Z. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.641157 · Cited by 115
Autophagy and Energy Metabolism
Yang, J., Zhou, R., & Ma, Z. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-0602-4_16 · Cited by 111
Molecular Pathophysiological Mechanisms in Huntington’s Disease
Jurcău, A. (2022) · Biomedicines · doi:10.3390/biomedicines10061432 · Cited by 118
Excessive autophagy induces the failure of trophoblast invasion and vasculature
Gao, L. Q., Qi, H., Kc, K., Zhang, X., Zhang, H., & Baker, P. N. (2014) · Journal of Hypertension · doi:10.1097/hjh.0000000000000366 · Cited by 111
Exercise induces TFEB expression and activity in skeletal muscle in a PGC-1α-dependent manner
Erlich, A. T., Brownlee, D., Beyfuss, K. A., & Hood, D. A. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00162.2017 · Cited by 112
Xie, C., Wu, W., Tang, A., Luo, N., & Tan, Y. (2019) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s228654 · Cited by 113
Oxidative Stress in the Anterior Ocular Diseases: Diagnostic and Treatment
Dammak, A., Pastrana, C., Martín‐Gil, A., Carpena‐Torres, C., Cerda, A. P., Simovart, M., Alarma‐Estrany, P., Huete‐Toral, F., & Carracedo, G. (2023) · Biomedicines · doi:10.3390/biomedicines11020292 · Cited by 111
Implications of autophagy for vascular smooth muscle cell function and plasticity
Salabei, J. K., & Hill, B. G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.003 · Cited by 108
Inomata, M., Xu, S., Chandra, P., Meydani, S. N., Takemura, G., Philips, J. A., & Leong, J. M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015368117 · Cited by 108
Deng, Y., Shi, J., Liu, J., & Qu, Q. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.04.005 · Cited by 105
Algae as an Attractive Source for Cosmetics to Counter Environmental Stress
Aslam, A., Bahadar, A., Liaquat, R., Saleem, M., Waqas, A., & Zwawi, M. (2021) · Science of The Total Environment · doi:10.1016/j.scitotenv.2020.144905 · Cited by 105
Emerging Paradigm of Crosstalk between Autophagy and the Ubiquitin-Proteasome System.
Nam, T., Han, J. H., Devkota, S., & Lee, H. (2017) · Europe PMC (PubMed Central) · doi:10.14348/molcells.2017.0226 · Cited by 114
Liu, D., Cui, W., Liu, B., Hu, H., Liu, J., Xie, R., Yang, X., Gu, G., Zhang, J., & Zheng, H. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356656 · Cited by 104
Self-citationGarbarino, V. R., Orr, M. E., Rodriguez, K. A., & Buffenstein, R. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.01.029 · Cited by 104
Jang, W., Kim, H., Li, H., Jo, K. D., Lee, M. K., Song, S. H., & Yang, H. O. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.07.081 · Cited by 104
Carson, J. A., Hardee, J. P., & VanderVeen, B. N. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.11.005 · Cited by 109
Retta, S. F., & Glading, A. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.09.011 · Cited by 105
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Metadata
- Authors
- Lee, J., Giordano, S., & Zhang, J.
- Affiliations
- University of Alabama at Birmingham (US)
- Corresponding author
- Zhang, Jianhua
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2011-12-21
- Volume
- 441
- Issue
- 2
- Pages
- 523-540
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC3258656
- OpenAlex
- W2124105006
- Cited by
- 1,438
- References
- 295
- Citations by year
- 2026: 45 · 2025: 58 · 2024: 65 · 2023: 68 · 2022: 98 · 2021: 99 · 2020: 110 · 2019: 116 · 2018: 143 · 2017: 119 · 2016: 104 · 2015: 115 · 2014: 118 · 2013: 118 · 2012: 62
- FWCI
- 11.18
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochemical Journal (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs
- National Institute for Health and Care Research
- National Institutes of Health (NS064090)
- National Institute of Neurological Disorders and Stroke (R01NS064090)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- autophagy, mitophagy, oxidative stress, redox signaling, reactive oxygen species, reactive nitrogen species, mitochondrial dysfunction, autophagy-related proteins, autophagosome formation, lysosomal degradation, mitochondrial turnover, cell death, degenerative diseases
- MeSH terms
- Protein Deglycase DJ-1, PTEN-Induced Putative Kinase, Animals, Autophagy, Cardiovascular Diseases, Humans, Hydrogen Peroxide, Lysosomes, Mitochondria, Neoplasms, Nitric Oxide, Oxidation-Reduction, Parkinson Disease, Protein Kinases, Transcription, Genetic, Signal Transduction, Oncogene Proteins, Reactive Oxygen Species, Oxidative Stress, Reactive Nitrogen Species, Intracellular Signaling Peptides and Proteins, TOR Serine-Threonine Kinases
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