The DOI matches its Crossref record; 100 of the 100 references it cites were found in a registry or an index.
Signal transduction by reactive oxygen species
Open accessAbstract
Although historically viewed as purely harmful, recent evidence suggests that reactive oxygen species (ROS) function as important physiological regulators of intracellular signaling pathways. The specific effects of ROS are modulated in large part through the covalent modification of specific cysteine residues found within redox-sensitive target proteins. Oxidation of these specific and reactive cysteine residues in turn can lead to the reversible modification of enzymatic activity. Emerging evidence suggests that ROS regulate diverse physiological parameters ranging from the response to growth factor stimulation to the generation of the inflammatory response, and that dysregulated ROS signaling may contribute to a host of human diseases.
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 source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“high levels of ROS generated by ongoing aerobic glycolysis followed by pyruvate oxidation in mitochondria (the Warburg effect), increase receptor and oncogene activity, and the stimulation of growth factor-dependent pathways or oxidizing enzymes induce genetic instability3,4.”
From ROS in cancer therapy: the bright side of the moon (2020) · cites this paper as [4]
Experimental — accuracy not yet measuredIn the citing paper
“Indeed, the generation of superoxide and hydrogen peroxide, among others, has been shown to mediate critical processes such as angiogenesis, hypoxic adaptation, and energy homeostasis (96, 249, 291, 720, 778, 825, 960).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [291]
In the citing paper
“As outlined above, ROS have origin from two main sources: mitochondrial oxidative metabolism and processes of cellular response to xenobiotics, bacteria, and cytokines during which ROS are formed as a part of either signal transduction pathways or a cellular defense mechanism (Finkel 2011).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Finkel 2011
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
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413
Self-citationAging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602
Mitochondria, Oxidants, and Aging
Balaban, R. S., Nemoto, S., & Finkel, T. (2005) · Cell · doi:10.1016/j.cell.2005.02.001 · Cited by 4,388
Self-citationNakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734
Reactive oxygen species have a causal role in multiple forms of insulin resistance
Houstis, N., Rosen, E. D., & Lander, E. S. (2006) · Nature · doi:10.1038/nature04634 · Cited by 2,525
Requirement for Generation of H 2 O 2 for Platelet-Derived Growth Factor Signal Transduction
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520
Self-citationMammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 1,006
Qiu, X., Yu, Y., Liu, H., Li, X., Sun, W., Wu, W., Liu, C., & Miao, L. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.08.009 · Cited by 93
Zhou, J., Ye, S., Fujiwara, T., Manolagas, S. C., & Zhao, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.478750 · Cited by 88
Holding our breath in our modern world: will mitochondria keep the pace with climate changes?
Blier, P. U., Lemieux, H., & Pichaud, N. (2013) · Canadian Journal of Zoology · doi:10.1139/cjz-2013-0183 · Cited by 92
Sprouty2, PTEN, and PP2A interact to regulate prostate cancer progression
Patel, R., Gao, M., Ahmad, I., Fleming, J., Singh, L. B., Singh, T., McKie, A. B., Seywright, M. M., Barnetson, R. J., Edwards, J., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci63672 · Cited by 92
Shi, H., Cheng, Y. H., Ye, J., Cai, P., Zhang, J., Li, R., Yang, Y., Wang, Z., Zhang, H., Lin, C., et al. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.11921 · Cited by 91
Park, S., Pekas, E. J., Headid, R. J., Son, W., Wooden, T. K., Song, J., Layec, G., Yadav, S. K., Mishra, P. K., & Pipinos, I. I. (2020) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00235.2020 · Cited by 91
NOXious signaling in pain processing
Kallenborn-Gerhardt, W., Schröder, K., Geißlinger, G., & Schmidtko, A. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.11.001 · Cited by 93
Biological signaling by small inorganic molecules
Basudhar, D., Ridnour, L. A., Cheng, R. Y. S., Kesarwala, A. H., Heinecke, J. L., & Wink, D. A. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.06.001 · Cited by 93
New Insight into the Role of Reactive Oxygen Species (ROS) in Cellular Signal-Transduction Processes
Russell, E. G., & Cotter, T. G. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.07.004 · Cited by 95
Biochemical and cellular basis of oxidative stress: Implications for disease onset
Aramouni, K., Assaf, R., Shaito, A. A., Fardoun, M., Al‐Asmakh, M., Sahebkar, A., & Eid, A. H. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.31071 · Cited by 97
Host stress drives tolerance and persistence: The bane of anti-microbial therapeutics
Hélaine, S., Conlon, B. P., Davis, K. M., & Russell, D. G. (2024) · Cell Host & Microbe · doi:10.1016/j.chom.2024.04.019 · Cited by 90
The NADPH oxidase NOX4 inhibits hepatocyte proliferation and liver cancer progression
Crosas‐Molist, E., Bertrán, E., Sancho, P., López‐Luque, J., Fernando, J., Sánchez, A., Fernández, M., Navarro, E., & Fabregat, I. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.040 · Cited by 90
Kozlov, S., Waardenberg, A. J., Engholm‐Keller, K., Arthur, J. W., Graham, M. E., & Lavin, M. F. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.055723 · Cited by 92
Hydrogen peroxide reactivity and specificity in thiol-based cell signalling
Winterbourn, C. C. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190049 · Cited by 89
Modulating Mitochondrial Intracellular Location as a Redox Signal
Murphy, M. P. (2012) · Science Signaling · doi:10.1126/scisignal.2003386 · Cited by 88
Implications of red Panax ginseng in oxidative stress associated chronic diseases
Lee, Y.-M., Yoon, H., Park, H., Song, B. C., & Yeum, K. (2016) · Journal of Ginseng Research · doi:10.1016/j.jgr.2016.03.003 · Cited by 93
Ultrasensitive ROS-Responsive Coassemblies of Tellurium-Containing Molecules and Phospholipids
Wang, L., Fan, F., Cao, W., & Xu, H. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b04419 · Cited by 89
Cadoná, F. C., Dantas, R. F., de Mello, G. H., & Silva, F. P. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1913091 · Cited by 90
Reactive Oxygen Species: Not Omnipresent but Important in Many Locations
Herb, M., Gluschko, A., & Schramm, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.716406 · Cited by 93
Wang, X., Zhang, Y., Li, T., Tian, W., Zhang, Q., & Cheng, Y. (2013) · Langmuir · doi:10.1021/la3046077 · Cited by 88
Gokhale, A., Larimore, J., Werner, E., So, L., Moreno-De-Luca, A., Lese-Martin, C., Lupashin, V. V., Smith, Y., & Faundez, V. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5640-11.2012 · Cited by 85
Oxygen in the tumor microenvironment: effects on dendritic cell function
Paardekooper, L. M., de Vos, W., & van den Bogaart, G. (2019) · Oncotarget · doi:10.18632/oncotarget.26608 · Cited by 89
Long-term exposure to a hypomagnetic field attenuates adult hippocampal neurogenesis and cognition
Zhang, B., Wang, L., Zhan, A., Wang, M., Tian, L., Guo, W., & Pan, Y. (2021) · Nature Communications · doi:10.1038/s41467-021-21468-x · Cited by 86
Chen, Y., Thompson, D. C., Koppaka, V., Jester, J. V., & Vasiliou, V. (2012) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2012.10.001 · Cited by 88
Lunov, O., Zablotskii, V., Churpita, O., Chánová, E. M., Syková, E., Dejneka, A., & Kubinová, Š. (2014) · Scientific Reports · doi:10.1038/srep07129 · Cited by 90
Monitoring Dynamic Cellular Redox Homeostasis Using Fluorescence-Switchable Graphene Quantum Dots
Li, N., Than, A., Sun, C., Tian, J., Chen, J., Pu, K., Dong, X., & Chen, P. (2016) · ACS Nano · doi:10.1021/acsnano.6b07237 · Cited by 87
The Quest for Selective Nox Inhibitors and Therapeutics: Challenges, Triumphs and Pitfalls
Cifuentes-Pagano, E., Meijles, D. N., & Pagano, P. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5620 · Cited by 84
Crosstalk between the Rb pathway and AKT signaling forms a quiescence-senescence switch.
Imai, Y., Takahashi, A., Hanyu, A., Hori, S., Sato, S., Naka, K., Hirao, A., Ohtani, N., & Hara, E. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.006 · Cited by 84
Chemical approaches to detect and analyze protein sulfenic acids
Furdui, C. M., & Poole, L. B. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21384 · Cited by 88
Erdélyi, K., Ditrói, T., Johansson, H. J., Czikora, Á., Balog, N., Silwal‐Pandit, L., Ida, T., Olasz, J., Hajdú, D., Mátrai, Z., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100050118 · Cited by 85
NADPH Oxidases NOXs and DUOXs as Putative Targets for Cancer Therapy
Weyemi, U., Redon, C. E., Parekh, P. R., Dupuy, C., & Bonner, W. M. (2013) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520611313030013 · Cited by 86
Milković, L., Gašparović, A. Č., & Žarković, N. (2014) · Free Radical Research · doi:10.3109/10715762.2014.999056 · Cited by 85
A midlife crisis for the mitochondrial free radical theory of aging
Stuart, J. A., Maddalena, L. A., Merilovich, M., & Robb, E. L. (2014) · Longevity & Healthspan · doi:10.1186/2046-2395-3-4 · Cited by 84
Zhang, Z., Fan, J., Zhao, Y., Kang, Y., Du, J., & Peng, X. (2018) · ACS Sensors · doi:10.1021/acssensors.8b00082 · Cited by 83
The Role of Lipoxidation in the Pathogenesis of Diabetic Retinopathy
Augustine, J., Troendle, E. P., Barabás, P., McAleese, C. A., Friedel, T., Stitt, A. W., & Curtis, T. M. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.621938 · Cited by 85
Redox-capacitor to connect electrochemistry to redox-biology
Kim, E., Leverage, W. T., Liu, Y., White, I. M., Bentley, W. E., & Payne, G. F. (2013) · The Analyst · doi:10.1039/c3an01632c · Cited by 84
Expression, regulation and clinical relevance of the ATPase inhibitory factor 1 in human cancers
Sánchez‐Aragó, M., Formentini, L., Martínez‐Reyes, I., García‐Bermúdez, J., Santacatterina, F., Sánchez-Cenizo, L., Willers, I. M., Aldea, M., Nájera, L., Juarranz, Á., et al. (2013) · Oncogenesis · doi:10.1038/oncsis.2013.9 · Cited by 83
Ji, S.-H., Kim, J., Lee, C.-H., Seo, H.-S., Chun, S., Oh, J., Choi, E. H., & Park, G. (2019) · Scientific Reports · doi:10.1038/s41598-018-38026-z · Cited by 83
Hydrogen peroxide (H2O2) controls axon pathfinding during zebrafish development
Gauron, C., Meda, F., Dupont, E., Albadri, S., Quenech’Du, N., Ipendey, E., Volovitch, M., Bene, F. D., Joliot, A., Rampon, C., et al. (2016) · Developmental Biology · doi:10.1016/j.ydbio.2016.05.004 · Cited by 83
CISD2 maintains cellular homeostasis
Shen, Z., Huang, Y., Teng, Y., Wang, T.-W., Kao, C., Yeh, C., & Tsai, T. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118954 · Cited by 83
Oxidative stress in melanogenesis and melanoma development
Kamiński, K., Kazimierczak, U., & Kolenda, T. (2022) · Współczesna Onkologia · doi:10.5114/wo.2021.112447 · Cited by 83
Busch, A. W. U., & Montgomery, B. L. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.010 · Cited by 85
Qi, S., Feng, Z., Li, Q., Qi, Z., & Zhang, Y. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9738745 · Cited by 82
Exposure to Static Magnetic and Electric Fields Treats Type 2 Diabetes
Carter, C. S., Huang, S. C., Searby, C. C., Cassaidy, B., Miller, M. J., Grzesik, W. J., Piorczynski, T. B., Pak, T. K., Walsh, S. A., Acevedo, M., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.09.012 · Cited by 85
González-Jiménez, I., Perlin, D. S., & Shor, E. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1276406 · Cited by 88
Single-Atom-Based Nanoenzyme in Tissue Repair
Fu, Z., Fan, K., He, X., Wang, Q., Yuan, J., Lim, K. S., Tang, J., Xie, F., & Cui, X. (2024) · ACS Nano · doi:10.1021/acsnano.4c00308 · Cited by 83
The role of manganese superoxide dismutase in skin aging
Treiber, N., Maity, P., Singh, K., Negoita, F., Wlaschek, M., & Scharffetter‐Kochanek, K. (2012) · Dermato-Endocrinology · doi:10.4161/derm.21819 · Cited by 86
Denzel, M. S., Lapierre, L. R., & Mack, H. I. D. (2018) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2018.08.001 · Cited by 82
Wang, Y., Lilienfeldt, N., & Hekimi, S. (2024) · Physiological Reviews · doi:10.1152/physrev.00040.2023 · Cited by 88
Novel insights into redox system and the mechanism of redox regulation
Wang, X., & Hai, C. (2016) · Molecular Biology Reports · doi:10.1007/s11033-016-4022-y · Cited by 84
Follicular Fluid redox involvement for ovarian follicle growth
Freitas, C., Neto, A. C., Matos, L., Silva, E., Ribeiro, Â., Silva-Carvalho, J. L., & Almeida, H. (2017) · Journal of Ovarian Research · doi:10.1186/s13048-017-0342-3 · Cited by 80
Liu, Y., Yang, H., Luo, N., Fu, Y., Qiu, F., Pan, Z., Li, X., Jian, W., Yang, X., Xue, Q., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04345-7 · Cited by 79
The microbial contribution to reactive oxygen species dynamics in marine ecosystems
Zinser, E. R. (2018) · Environmental Microbiology Reports · doi:10.1111/1758-2229.12626 · Cited by 78
Anestopoulos, I., Kiousi, D. E., Klavaris, A., Galanis, Α., Sałek, K., Euston, S. R., Pappa, A., & Panayiotidis, M. I. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12070688 · Cited by 82
The impact of thiol peroxidases on redox regulation
Flohé, L. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1046858 · Cited by 82
Recent Advances in the Study of Age-Related Hearing Loss: A Mini-Review
Kidd, A. R., & Bao, J. (2012) · Gerontology · doi:10.1159/000338588 · Cited by 79
Gobert, A. P., & Wilson, K. T. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.024 · Cited by 79
Oxidative stress and gene expression of earthworm ( Eisenia fetida ) to clothianidin
Liu, T., Wang, X., You, X., Chen, D., Li, Y., & Wang, F. (2017) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2017.04.012 · Cited by 80
Redox-dependent regulation of epidermal growth factor receptor signaling
Heppner, D. E., & van der Vliet, A. (2015) · Redox Biology · doi:10.1016/j.redox.2015.12.002 · Cited by 78
Telomeres, Nutrition, and Longevity: Can We Really Navigate Our Aging?
Vidaček, N. Š., Nanić, L., Ravlić, S., Sopta, M., Gerić, M., Gajski, G., Garaj‐Vrhovac, V., & Rubelj, I. (2017) · The Journals of Gerontology Series A · doi:10.1093/gerona/glx082 · Cited by 80
Nanoparticle-induced oxidation of corona proteins initiates an oxidative stress response in cells
Jayaram, D. T., Runa, S., Kemp, M. L., & Payne, C. K. (2017) · Nanoscale · doi:10.1039/c6nr09500c · Cited by 77
Redox Signaling, Neuroinflammation, and Neurodegeneration
Aguilera, G., Colín-González, A. L., Rangel‐López, E., Chavarría, A., & Santamaría, A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7099 · Cited by 81
Isoform-selective NADPH oxidase inhibitor panel for pharmacological target validation
Dao, V. T.-V., Elbatreek, M. H., Altenhöfer, S., Casas, A. I., Pachado, M. P., Neullens, C. T., Knaus, U. G., & Schmidt, H. H. H. W. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.12.038 · Cited by 81
Zhou, H., Zhang, F., Zhai, F., Su, Y., Zhou, Y., Ge, Z., Tilak, P., Eirich, J., Finkemeier, I., Fu, L., et al. (2021) · Molecular Plant · doi:10.1016/j.molp.2021.11.006 · Cited by 77
ROS as Signaling Molecules to Initiate the Process of Plant Acclimatization to Abiotic Stress
Fedoreyeva, L. I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252111820 · Cited by 77
Porto, M. L., Rodrigues, B. P., Menezes, T. N., Ceschim, S. L., Casarini, D. E., Gava, A. L., Pereira, T. D. M. C., Vasquez, E. C., Campagnaro, B. P., & Meyrelles, S. S. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0201-8 · Cited by 82
Mitochondrial Ion Channels/Transporters as Sensors and Regulators of Cellular Redox Signaling
O‐Uchi, J., Ryu, S.-Y., Jhun, B. S., Hurst, S., & Sheu, S. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5681 · Cited by 76
Zaffagnini, M., de Mia, M., Morisse, S., Giacinto, N. D., Marchand, C. H., Maes, A., Lemaire, S. D., & Trost, P. (2016) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2016.02.006 · Cited by 81
Ishimoto, Y., Tanaka, T., Yoshida, Y., & Inagi, R. (2018) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13018 · Cited by 78
Inhibiting the Activity of NADPH Oxidase in Cancer
Konaté, M. M., Antony, S., & Doroshow, J. H. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8046 · Cited by 81
Ashrafizadeh, M., Rafiei, H., Mohammadinejad, R., Farkhondeh, T., & Samarghandian, S. (2021) · Cancer Cell International · doi:10.1186/s12935-021-01773-7 · Cited by 79
Mitochondrial remodeling in cancer metabolism and survival: Potential for new therapies
Barbosa, I. A., Machado, N. G., Skildum, A. J., Scott, P. M., & Oliveira, P. J. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.04.005 · Cited by 81
Moringa Isothiocyanate Activates Nrf2: Potential Role in Diabetic Nephropathy
Cheng, D., Gao, L., Su, S., Sargsyan, D., Wu, R., Raskin, I., & Kong, A. T. (2019) · The AAPS Journal · doi:10.1208/s12248-019-0301-6 · Cited by 80
Ribosomal Protein Mutations Induce Autophagy through S6 Kinase Inhibition of the Insulin Pathway
Heijnen, H. F. G., van Wijk, R., Pereboom, T. C., Goos, Y. J., Seinen, C. W., van Oirschot, B. A., van Dooren, R., Gastou, M., Giles, R. H., van Solinge, W. W., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004371 · Cited by 78
Resveratrol Protects against Helicobacter pylori-Associated Gastritis by Combating Oxidative Stress
Zhang, X., Jiang, A., Qi, B., Ma, Z., Xiong, Y., Dou, J., & Wang, J. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161126061 · Cited by 75
Fujii, J., Homma, T., Kobayashi, S., & Seo, H. G. (2018) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v9.i1.1 · Cited by 75
Zhang, Y., Han, C. Y., Duan, F., Fan, X., Yao, X., Parks, R. J., Tang, Y., Wang, M., Liu, L., Tsang, B. K., et al. (2019) · Cancer Cell International · doi:10.1186/s12935-019-0910-2 · Cited by 76
Caveolin‐1: An Oxidative Stress‐Related Target for Cancer Prevention
Wang, S., Wang, N., Zheng, Y., Zhang, J., Zhang, F., & Wang, Z. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7454031 · Cited by 74
Sulfur metabolism and its contribution to malignancy
Ward, N. P., & DeNicola, G. M. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.05.001 · Cited by 74
Synergistic antitumor activity of sorafenib and artesunate in hepatocellular carcinoma cells
Yao, X., Zhao, C., Yin, H., Wang, K., & Gao, J. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0395-5 · Cited by 74
Carinci, M., Vezzani, B., Patergnani, S., Ludewig, P., Lessmann, K., Magnus, T. U., Casetta, I., Pugliatti, M., Pinton, P., & Giorgi, C. (2021) · Biomedicines · doi:10.3390/biomedicines9020169 · Cited by 80
Distelmaier, F., Valsecchi, F., Forkink, M., Vries, S. E. V. E., Swarts, H. G. P., Rodenburg, R. J., Verwiel, E. T. P., Smeitink, J. A. M., Willems, P. H. G. M., & Koopman, W. J. H. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4294 · Cited by 79
Mitochondrial dysfunction is an acute response of articular chondrocytes to mechanical injury
Delco, M. L., Bonnevie, E. D., Bonassar, L. J., & Fortier, L. A. (2017) · Journal of Orthopaedic Research® · doi:10.1002/jor.23651 · Cited by 74
ROS-induced Oxidative Injury involved in Pathogenesis of Fungal Keratitis via p38 MAPK Activation
Hua, X., Chi, W., Su, L., Li, J., Zhang, Z., & Yuan, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-09636-w · Cited by 74
Dual Roles of Oxidative Stress in Metal Carcinogenesis
Xu, J., Wise, J. T. F., Wang, L., Schumann, K., Zhang, Z., & Shi, X. (2017) · Journal of Environmental Pathology Toxicology and Oncology · doi:10.1615/jenvironpatholtoxicoloncol.2017025229 · Cited by 78
Beyond ROS clearance: Peroxiredoxins in stress signaling and aging
Detienne, G., Haes, W. D., Mergan, L., Edwards, S. L., Temmerman, L., & Bael, S. V. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.03.005 · Cited by 77
Tobore, T. O. (2020) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.112560 · Cited by 73
Imaging dynamic redox processes with genetically encoded probes
Ezeriņa, D., Morgan, B., & Dick, T. P. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.12.023 · Cited by 73
Kamiński, M. M., Röth, D., Krammer, P. H., & Gülow, K. (2013) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-013-0235-0 · Cited by 73
Association of Oxidative Stress with Psychiatric Disorders
Hassan, W., Noreen, H., Gomes, V. D. C., Mohammadzai, I., da Rocha, J. B. T., & Landeira-Fernández, J. (2016) · Current Pharmaceutical Design · doi:10.2174/1381612822666160307145931 · Cited by 76
Rat Aquaporin-5 Is pH-Gated Induced by Phosphorylation and Is Implicated in Oxidative Stress
Rodrigues, C., Mósca, A. F., Martins, A. P., Nobre, T. V., Prista, C., Antunes, F., Gašparović, A. Č., & Soveral, G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122090 · Cited by 73
Amaroli, A., Ferrando, S., & Benedicenti, S. (2018) · Photochemistry and Photobiology · doi:10.1111/php.13032 · Cited by 73
Mitochondrial dependency in progression of acute myeloid leukemia
Basak, N. P., & Banerjee, S. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.01.006 · Cited by 75
Zeng, F., Sherry, J. P., & Bols, N. C. (2016) · Chemosphere · doi:10.1016/j.chemosphere.2016.04.079 · Cited by 72
Tiberi, J., Cesarini, V., Stefanelli, R., Canterini, S., Fiorenza, M. T., & Rosa, P. L. (2023) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2023.111802 · Cited by 75
Sendtner, N., Seitz, R., Brandl, N., Müller, M., & Gülow, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262010240 · Cited by 81
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
Hydrogen gas: from clinical medicine to an emerging ergogenic molecule for sports athletes
LeBaron, T. W., Laher, I., Kura, B., & Slezák, J. (2019) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2019-0067 · Cited by 76
Michelucci, A., Chen, L., Protasi, F., & Dirksen, R. T. (2021) · Metabolites · doi:10.3390/metabo11070424 · Cited by 75
Insights into the Role of Oxidative Stress in Ovarian Cancer
Ding, D., Xie, L., Shen, Y., Li, J., Guo, Y., Fu, Y., Liu, F.-Y., & Han, F. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8388258 · Cited by 74
Metadata
- Authors
- Finkel, T.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Finkel, Toren
- ORCID
- Finkel, Toren
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2011-07-11
- Volume
- 194
- Issue
- 1
- Pages
- 7-15
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3135394
- OpenAlex
- W2115708356
- Cited by
- 2,322
- References
- 100
- Citations by year
- 2026: 90 · 2025: 120 · 2024: 134 · 2023: 166 · 2022: 187 · 2021: 223 · 2020: 187 · 2019: 188 · 2018: 130 · 2017: 168 · 2016: 161 · 2015: 164 · 2014: 155 · 2013: 129 · 2012: 107
- FWCI
- 11.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- reactive oxygen species, redox signaling, cysteine oxidation, post-translational modification, intracellular signaling, growth factor signaling, inflammation, disease
- MeSH terms
- Animals, Humans, Models, Biological, Oxidation-Reduction, Signal Transduction, Reactive Oxygen Species
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