The DOI matches its Crossref record; 295 of the 295 references it cites were found in a registry or an index.
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.
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
“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
In the citing paper
“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
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
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
Flagged first, then by citations
Cited by
Sorted by citations
Items 801–900 of 999
Shih, J., Chiu, C., Ma, K., Huang, Y., Shiue, C., Yeh, T.-Y., Kao, L., Lin, Y., & Li, I. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.02.026 · Cited by 23
Meng, Y., Wu, C., Yu, B., Li, H., Chen, M., & Qi, G. (2018) · Folia Biologica · doi:10.14712/fb2018064030103 · Cited by 23
Nita, M., & Grzybowski, A. E. (2020) · EXCLI journal · doi:10.17179/excli2020-2915 · Cited by 22
Cafe, S. L., Nixon, B., Ecroyd, H. W., Martin, J. H., Skerrett-Byrne, D. A., & Bromfield, E. G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.660626 · Cited by 23
Qian, Y., Kachroo, A. H., Yellman, C. M., Marcotte, E. M., & Johnson, K. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.526418 · Cited by 25
Nassar, A. M. K., Abdel-Halim, K. Y., & Abbassy, M. A. (2020) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2020.108949 · Cited by 22
Paraventricular Nucleus Infusion of Oligomeric Proantho Cyanidins Improves Renovascular Hypertension
Yu, X., Xin, G.-R., Liu, K., Liu, X.-J., Fu, L., Qi, J., Kang, K. B., Meng, T.-T., Yi, Q.-Y., Li, Y., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.642015 · Cited by 21
Lee, H., Jiang, X., Perwaiz, I., Yu, P., Wang, J., Wang, Y., Hüttemann, M., Felder, R. A., Sibley, D. R., Polster, B. M., et al. (2021) · Hypertension Research · doi:10.1038/s41440-021-00646-w · Cited by 22
Jin, X., Zhang, J., Yi, Q., Meng, F., Yu, J., Ji, Y., Mo, J. Q., Tong, Y., Jiang, P., & Guan, M. (2021) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.62.7.22 · Cited by 22
Self-citationTalaat, S. M., Elnaggar, Y. S. R., El-Ganainy, S. O., Gowayed, M. A., Abdel-Bary, A., & Abdallah, O. Y. (2022) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2022.122184 · Cited by 22
WANG, Q.-W., WANG, Y., Wang, T., ZHANG, K.-B., JIANG, C.-Y., Hu, F., Yuan, Y., Bian, J., Liu, X., Gu, J., et al. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3755 · Cited by 22
Astrocytes Role in Parkinson: A Double-Edged Sword
Cabezas, R., Fidel, M., Torrente, D., El-Bachá, R. D. S., Morales, L., González, J., & George, E. (2013) · InTech eBooks · doi:10.5772/54305 · Cited by 22
Targets, trafficking, and timing of cardiac autophagy
Rotter, D., & Rothermel, B. A. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.10.001 · Cited by 23
Ochoa-Ruiz, E., Díaz-Ruiz, R., Hernández-Vázquez, A. D. J., Ibarra‐González, I., Ortíz-Plata, A., Rembao, D., Ortega-Cuéllar, D., Viollet, B., Uribe‐Carvajal, S., Corella, J. A., et al. (2015) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2015.08.009 · Cited by 22
A Review of Biological and Pharmacological Actions of Melatonin: Oxidant and Prooxidant Properties
Eghbal, M. A. (2024) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.5281/zenodo.10691421 · Cited by 22
Sun, G., Meng, F., Cai, H., Diao, X.-B., Zhang, B., & Xiu-ping, B. (2020) · Cardiovascular Diagnosis and Therapy · doi:10.21037/cdt.2020.01.02 · Cited by 23
Sen, U., Pushpakumar, S. B., Amin, M., & Tyagi, S. C. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.06.006 · Cited by 22
Aging and energetics’ ‘Top 40’ future research opportunities 2010-2013
Allison, D. B., Antoine, L. H., Ballinger, S. W., Bamman, M. M., Biga, P. R., Darley-Usmar, V. M., Fisher, G., Gohlke, J. M., Halade, G. V., Hartman, J. L., et al. (2014) · F1000Research · doi:10.12688/f1000research.5212.1 · Cited by 21
Self-citationLiu, Q., Sun, Y., Lv, Y., Le, Z., Xin, Y., Zhang, P., & Liu, Y. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2673 · Cited by 22
Equisetin Targets Intracellular Staphylococcus aureus through a Host Acting Strategy
Tian, J., Chen, S., Liu, F., Zhu, Q., Shen, J., Lin, W., & Zhu, K. (2022) · Marine Drugs · doi:10.3390/md20110656 · Cited by 21
Exercise and vascular function in sedentary lifestyles in humans
Fasipe, B., Li, S., & Laher, I. (2023) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-023-02828-6 · Cited by 22
Yusri, K., Kumar, S., Fong, S., Gruber, J., & Sorrentino, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126793 · Cited by 23
Cholesterol load of microglia: Contribution of membrane architecture changes to neurotoxic power?
Račková, L. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.06.015 · Cited by 22
Citreoviridin induces ROS-dependent autophagic cell death in human liver HepG2 cells
Liu, Y., Wang, Y., Liu, X., Jiang, L., Yang, G., Sun, X., Geng, C., Li, Q., Chen, M., & Yao, X. (2014) · Toxicon · doi:10.1016/j.toxicon.2014.12.014 · Cited by 21
Elevated autophagy and mitochondrial dysfunction in the Smith–Lemli–Opitz Syndrome
Chang, S., Ren, G., Steiner, R. D., Merkens, L. S., Roullet, J., Korade, Ž., DiMuzio, P. J., & Tulenko, T. N. (2014) · Molecular Genetics and Metabolism Reports · doi:10.1016/j.ymgmr.2014.09.005 · Cited by 21
2,5-Hexanedione induces autophagic death of VSC4.1 cells via a PI3K/Akt/mTOR pathway
Guan, H., Piao, H. Z., Qian, Z., Zhou, X., Sun, Y., Gao, C., Li, S., & Piao, F. (2017) · Molecular BioSystems · doi:10.1039/c7mb00001d · Cited by 21
DJ-1 based peptide, ND-13, promote functional recovery in mouse model of focal ischemic injury
Molcho, L., Ben‐Zur, T., Barhum, Y., & Offen, D. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192954 · Cited by 21
Tonazzi, A., Console, L., & Indiveri, C. (2013) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2013.01.006 · Cited by 21
Zhou, S., Liu, R. R., Yuan, K., Yi, T., Zhao, X., Huang, C., & Wei, Y. (2012) · Mass Spectrometry Reviews · doi:10.1002/mas.21362 · Cited by 21
Protein S-nitrosylation during induced autophagy in Triticum aestivum
Mazina, A. B., Gazizova, N., Daminova, A. G., & Minibayeva, F. V. (2021) · AIP conference proceedings · doi:10.1063/5.0069510 · Cited by 20
Exploring Evolutionary Adaptations and Genomic Advancements to Improve Heat Tolerance in Chickens
Nawaz, A. H., Setthaya, P., & Feng, C. (2024) · Animals · doi:10.3390/ani14152215 · Cited by 24
Ransdell-Green, E. C., Baranowska‐Kortylewicz, J., & Wang, D. (2025) · Antioxidants · doi:10.3390/antiox14010079 · Cited by 21
Kurhaluk, N., Ткаченко, Г. М., & Лукаш, О. В. (2020) · Chronobiology International · doi:10.1080/07420528.2020.1830792 · Cited by 20
Song, C., Liu, B., Ge, X., Liu, B., Liu, B., & Xu, P. (2021) · Aquaculture · doi:10.1016/j.aquaculture.2021.737441 · Cited by 20
Peng, J., Wang, Q. L., Zhou, J., Zhao, S., Pan, D., Chen, Y., Tao, L., Du, Q., Shen, X., & Chen, Y. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.720777 · Cited by 20
Rapamycin ameliorates age-related hearing loss in C57BL/6J mice by enhancing autophagy in the SGNs
Liu, H., Li, F., Li, X., Wu, Q., & Dai, C. (2022) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136493 · Cited by 21
Lizzo, G., Migliavacca, E., Lamers, D., Frézal, A., Corthésy, J., Vinyes-Parès, G., Bosco, N., Karagounis, L. G., Hövelmann, U., Heise, T., et al. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.852569 · Cited by 20
Ren, Y., He, X., Yan, X., Yang, Y., Li, Q., Yao, T., Lu, L., Peng, L., & Zou, L. (2022) · Molecules · doi:10.3390/molecules27175722 · Cited by 20
Wang, R., Santos, J. M., Dufour, J. M., Stephens, E. R., Miranda, J. M., Washburn, R. L., Hibler, T., Kaur, G., Lin, D., & Shen, C. (2022) · Nutrients · doi:10.3390/nu14204384 · Cited by 25
Bak, S. B., Song, Y. R., Bae, S.-J., Lee, W.-Y., & Kim, Y. W. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.02.016 · Cited by 20
Role of autophagy in arsenite-induced neurotoxicity: The involvement of α-synuclein
Teng, Y. C., Jeng, C., Huang, H.-J., & Lin, A. M. (2015) · Toxicology Letters · doi:10.1016/j.toxlet.2015.01.018 · Cited by 20
Oxidative stress and free radicals related diseases of the newborn
Perrone, S., Tataranno, M. L., Stazzoni, G., & Buonocore, G. (2012) · Advances in Bioscience and Biotechnology · doi:10.4236/abb.2012.327127 · Cited by 20
May Autophagy be a Novel Biomarker and Antitumor Target in Colorectal Cancer?
Gil, J., Pesz, K. A., & Sasiadek, M. M. (2016) · Biomarkers in Medicine · doi:10.2217/bmm-2016-0083 · Cited by 20
Hao, M., Wang, X., & Jiao, K. (2017) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2017.4048 · Cited by 20
Peres, G. B., Schor, N., & Michelacci, Y. M. C. D. S. (2017) · Biochimie · doi:10.1016/j.biochi.2017.02.004 · Cited by 21
Tazarotene-Induced Gene 1 Enhanced Cervical CellAutophagy through Transmembrane Protein 192
Shyu, R., Wang, C., Wu, C., Chen, M., Lee, M., Wang, L., Jiang, S., & Tsai, F. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.0161 · Cited by 20
Díaz-Casado, M. E., Rusanova, I., Aranda‐Martínez, P., Fernández‐Ortiz, M., Sayed, R. K. A., Fernández-Gil, B. I., Hidalgo‐Gutiérrez, A., Escames, G., López, L. C., & Acuña-Castroviejo, D. (2017) · Zebrafish · doi:10.1089/zeb.2017.1479 · Cited by 21
Zhang, Y., Pan, Y., Xiong, R., Zheng, J., Li, Q., Zhang, S., Li, X., Pan, X., & Yang, S. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.157 · Cited by 20
Hu, T., Sun, H., Deng, W., Huang, W.-Q., & Liu, Q. (2018) · Shock · doi:10.1097/shk.0000000000001250 · Cited by 20
Calcitriol promotes survival of experimental random pattern flap via activation of autophagy.
Chen, L., Zhou, K., Chen, H. A., Li, S., Lin, D., & Zhou, D. (2017) · PubMed Central · Cited by 20
Shi, W., Guo, Z., Ji, Y. S., & Feng, J. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173132 · Cited by 20
Shimizu, Y., Dobashi, K., Nagase, H., Ohta, K., Sano, T., Matsuzaki, S., Ishii, Y., Satoh, T., Koka, M., Yokoyama, A., et al. (2014) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.14-44 · Cited by 20
Dong, Y., Yu, Q., Chen, Y., Xu, N., Zhao, Q., Jia, C., Zhang, B., Zhang, K., Zhang, B., Xing, L., et al. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.10.002 · Cited by 20
Role of beclin 1-dependent autophagy in cardioprotection of ischemic preconditioning
Peng, W., Liu, Y., Xu, W., & Xia, Q.-H. (2013) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-013-1070-6 · Cited by 20
Chen, H., Yang, G., Xu, D.-E., Du, Y.-T., Zhu, C., Hu, H., Luo, L., Feng, L., Huang, W., Sun, Y., et al. (2024) · Neuroscience Bulletin · doi:10.1007/s12264-024-01292-1 · Cited by 19
Tain, Y., Chan, S. H. H., & Chan, J. Y. H. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.014 · Cited by 20
The Liver: Oxidative Stress and Dietary Antioxidants
Aseervatham, G. S. B., Ananth, D. A., & Thilagar, S. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-803951-9.00020-3 · Cited by 20
Zhang, Y., Wu, J., Jin, W., Shen, M., Yin, S., Lai, X., Ma, H., Jiang, M., Sun, D., & Yan, J. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9233749 · Cited by 19
Wei, Y., Wang, H., Fan, Y., Gu, J., Zhang, X., Gong, X.-H., & Hao, Z. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.114527 · Cited by 19
BU, X.-F., Wang, M., Zhang, Z., Zhao, Y., Li, M., & Yan, Y. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3039 · Cited by 20
c-Ski Inhibits Autophagy of Vascular Smooth Muscle Cells Induced by oxLDL and PDGF
Li, J., Li, Z., Yang, T., Zeng, Y., & Yang, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098902 · Cited by 19
Park, E., Lee, S. Y., Lee, G., Kim, D., Kim, Y., Cho, M., & Kim, J. H. (2014) · Toxicology Letters · doi:10.1016/j.toxlet.2014.07.027 · Cited by 19
Constructing de Novo H2O2 Signaling via Induced Protein Proximity
Zeng, G., Zhang, R., Xuan, W., Wang, W., & Liang, F. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00170 · Cited by 19
Santofimia‐Castaño, P., Izquierdo-Álvarez, A., Plaza‐Dávila, M., Martı́nez-Ruiz, A., Fernández‐Bermejo, M., Mateos-Rodríguez, J. M., Salido, G. M., & González, A. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26280 · Cited by 19
Huang, Y., & Hu, Z. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26602 · Cited by 19
Cesarini, E., Cerioni, L., Canonico, B., Sario, G. D., Guidarelli, A., Lattanzi, D., Savelli, D., Guescini, M., Nasoni, M. G., Bigini, N., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0203001 · Cited by 20
Pas Kinase Deficiency Triggers Antioxidant Mechanisms in the Liver
Dongil, P., Pérez-García, A., Hurtado-Carneiro, V., Herrero-de-Dios, C. M., Blázquez, E., Álvarez, E., & Sanz, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-32192-w · Cited by 19
Upregulation of autophagy by Ginsenoside Rg2 in MCF-7 cells
Chung, Y., Jeong, S., Choi, H. S., Ro, S., Lee, J. S., & Park, J. K. (2018) · Animal Cells and Systems · doi:10.1080/19768354.2018.1545696 · Cited by 19
Self-citationVegh, C., Stokes, K., Ma, D., Wear, D., Cohen, J. S., Ray, S. D., & Pandey, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181230 · Cited by 19
Vegh, C., Pupulin, S., Wear, D., Culmone, L., Huggard, R., Ma, D., & Pandey, S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7404815 · Cited by 19
ROS regulation of RAS and vulva development in Caenorhabditis elegans
Kramer‐Drauberg, M., Liu, J., Desjardins, D., Wang, Y., Branicky, R. S., & Hekimi, S. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008838 · Cited by 19
Pan, X., Liu, D., Wang, J., Zhang, X., Yan, M., Zhang, D., Zhang, J., & Liu, W. (2013) · Cancer Science · doi:10.1111/cas.12253 · Cited by 19
Self-citationOxidant Stress, Antioxidant Defense, and Liver Injury
McGill, M. R., & Jaeschke, H. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-387817-5.00004-2 · Cited by 19
Chaves, R. S., Kazi, A. I., Silva, C. M., Almeida, M. F., Lima, R. S., Carrettiero, D. C., Demasi, M., & Ferrari, M. (2016) · IBRO Reports · doi:10.1016/j.ibror.2016.09.001 · Cited by 20
Coskun, P. E., Helguera, P. R., Nemati, Z., Bohannan, R. C., Thomas, J., Samuel, S. E., Argueta, J., Doran, E. W., Wallace, D. C., Lott, I. T., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160278 · Cited by 19
Zhang, L., Zhao, S., Yuan, L., Wu, H., Jiang, H., Zhao, S., Luo, G., & Xue, X. (2015) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-015-2494-z · Cited by 19
Bal‐Price, A., Leist, M., Schildknecht, S., Monnet‐Tschudi, F., Paini, A., & Terron, A. (2018) · OECD series on adverse outcome pathways · doi:10.1787/b46c3c00-en · Cited by 22
mTOR Signaling and Potential Therapeutic Targeting in Meningioma
Pinker, B., & Barciszewska, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23041978 · Cited by 18
Nootkatone Supplementation Attenuates Carbon Tetrachloride Exposure-Induced Nephrotoxicity in Mice
Dai, C., Liu, M., Zhang, Q., Gupta, S., Tang, S., & Shen, J. (2023) · Antioxidants · doi:10.3390/antiox12020370 · Cited by 18
Chrysoeriol Improves In Vitro Porcine Embryo Development by Reducing Oxidative Stress and Autophagy
Wang, C., Ji, H., He, S., Liu, R., Wang, X., Wang, J., Huang, C., Xu, Y., Li, Y., & Kim, N. (2023) · Veterinary Sciences · doi:10.3390/vetsci10020143 · Cited by 18
The Interplay between Dysregulated Metabolism and Epigenetics in Cancer
Bassal, M. A. (2023) · Biomolecules · doi:10.3390/biom13060944 · Cited by 19
Pan, Y., Suzuki, T., Sakai, K., Hirano, Y., Ikeda, H., Hattori, A., Dohmae, N., Nishio, K., & Kakeya, H. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176156 · Cited by 18
Shu, J., Xing, L., Ding, G., Luo, Q., Liu, X., Yan, Q., Sheng, J., & Huang, H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0082334 · Cited by 18
Kawano, T., Murata, M., Hyodo, F., Eto, H., Kosem, N., Nakata, R., Hamano, N., Piao, J. S., Narahara, S., Akahoshi, T., et al. (2016) · Scientific Reports · doi:10.1038/srep32604 · Cited by 18
The frequency of yeast [PSI+] prion formation is increased during chronological ageing
Speldewinde, S. H., & Grant, C. M. (2017) · Microbial Cell · doi:10.15698/mic2017.04.568 · Cited by 18
The Tucumã of Amazonas— Astrocaryum aculeatum
Santos, R. C. V., Sagrillo, M. R., Ribeiro, E. E., & da Cruz, I. B. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-803138-4.00056-3 · Cited by 18
Effect of magnesium on reducing the UV‐induced oxidative damage in marrow mesenchymal stem cells
Chen, Y., Xiong, S., Zhao, F., Lu, X., Wu, B., & Yang, B. (2019) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.36634 · Cited by 18
Mitophagy is involved in chromium (VI)-induced mitochondria damage in DF-1 cells
Xu, Y., Wang, X., Geng, N., Zhu, Y., Zhang, S., Liu, Y., & Liu, J. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.110414 · Cited by 18
Zehra, M., Curry, J. C., Pillai, S. S., Lakhani, H. V., Edwards, C. E., & Sodhi, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134737 · Cited by 17
Mattam, U., Talari, N. K., Paripati, A. K., Krishnamoorthy, T., & Sepuri, N. B. V. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118852 · Cited by 19
Hepatoprotection by Traditional Essence of Ginseng against Carbon Tetrachloride—Induced Liver Damage
Hsu, Y.-J., Wang, C., Lee, M., & Huang, C. (2020) · Nutrients · doi:10.3390/nu12103214 · Cited by 18
Sharma, P., Yadav, P., Sundaram, S., Venkatraman, G., Bera, A. K., & Karunagaran, D. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.120727 · Cited by 18
Kalogeris, T. J., Baines, C. P., & Korthuis, R. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098459 · Cited by 18
Silkworm Storage Protein 1 Inhibits Autophagy-Mediated Apoptosis
Kang, S. J., & Rhee, W. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020318 · Cited by 19
Reduced Retinal Degeneration in an Oxidative Stress Organ Culture Model through an iNOS-Inhibitor
Mueller‐Buehl, A. M., Tsai, T., Hurst, J., Theiß, C., Peters, L., Hofmann, L., Herms, F., Kuehn, S., Schnichels, S., & Joachim, S. C. (2021) · Biology · doi:10.3390/biology10050383 · Cited by 18
Eder, K., Ringseis, R., & Geßner, D. K. (2025) · Animals · doi:10.3390/ani15111536 · Cited by 19
Wang, Y., Li, P., Zhang, X., Li, L., Liu, M., Li, X., Dai, Y., Zhang, C., & Li, S. (2021) · ACS Omega · doi:10.1021/acsomega.1c03265 · Cited by 17
The Role of Mitochondrial Dynamin in Stroke
Li, C., Chen, C., Qin, H., Ao, C., Chen, J., Tan, J., & Zeng, L. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2504798 · Cited by 19
Modulation of Reactive Oxygen Species Homeostasis as a Pleiotropic Effect of Commonly Used Drugs
Thomas, C., Wurzer, L., Malle, E., Ristow, M., & Madreiter‐Sokolowski, C. T. (2022) · Frontiers in Aging · doi:10.3389/fragi.2022.905261 · Cited by 18
The Yin and Yang dualistic features of autophagy in thermal burn wound healing
Totan, A., Greabu, M., Stănescu-Spînu, I.-I., Imre, M. M., Spînu, T. C., Miricescu, D., Ilinca, R., Coculescu, E. C., Bădoiu, S. C., Coculescu, B.-I., et al. (2022) · International Journal of Immunopathology and Pharmacology · doi:10.1177/03946320221125090 · Cited by 18
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
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