The DOI matches its Crossref record; 225 of the 225 references it cites were found in a registry or an index.
Reactive oxygen species, cellular redox systems, and apoptosis
Open accessAbstract
Reactive oxygen species (ROS) are products of normal metabolism and xenobiotic exposure, and depending on their concentration, ROS can be beneficial or harmful to cells and tissues. At physiological low levels, ROS function as "redox messengers" in intracellular signaling and regulation, whereas excess ROS induce oxidative modification of cellular macromolecules, inhibit protein function, and promote cell death. Additionally, various redox systems, such as the glutathione, thioredoxin, and pyridine nucleotide redox couples, participate in cell signaling and modulation of cell function, including apoptotic cell death. Cell apoptosis is initiated by extracellular and intracellular signals via two main pathways, the death receptor- and the mitochondria-mediated pathways. Various pathologies can result from oxidative stress-induced apoptotic signaling that is consequent to ROS increases and/or antioxidant decreases, disruption of intracellular redox homeostasis, and irreversible oxidative modifications of lipid, protein, or DNA. In this review, we focus on several key aspects of ROS and redox mechanisms in apoptotic signaling and highlight the gaps in knowledge and potential avenues for further investigation. A full understanding of the redox control of apoptotic initiation and execution could underpin the development of therapeutic interventions targeted at oxidative stress-associated disorders.
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
“ROS are highly chemically reactive molecules, derived from the deficient reduction in molecular oxygen (O2) and playing a critical role as signaling molecules in tumorigenesis [68], including asbestos-mediated carcinogenesis [15,66,69].”
From Chronic Inflammation, Oxidative Stress and Metabolic Plasticity: Three Players Driving the Pro-Tumorigenic Microenvironment in Malignant Mesothelioma (2023) · cites this paper as [69]
Experimental — accuracy not yet measured
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
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Oxidants, antioxidants, and the degenerative diseases of aging.
Ames, B. N., Shigenaga, M. K., & Hagen, T. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.7915 · Cited by 5,958
Meister, A., & Anderson, M. E. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.003431 · Cited by 5,694
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
Molecular characterization of mitochondrial apoptosis-inducing factor
Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Harris, J. R., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,546
Cited by
Sorted by citations
Items 101–200 of 1,006
Redox interplay between mitochondria and peroxisomes
Lismont, C., Nordgren, M., Van Veldhoven, P. P., & Fransen, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00035 · Cited by 214
Protocatechuic Acid and Human Disease Prevention: Biological Activities and Molecular Mechanisms
Masella, R., Santangelo, C., D’Archivio, M., Volti, G. L., Giovannini, C., & Galvano, F. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712800672102 · Cited by 216
Redox biology of the intestine
Circu, M. L., & Aw, T. Y. (2011) · Free Radical Research · doi:10.3109/10715762.2011.611509 · Cited by 215
Self-citationThe Role of Nrf2-Mediated Pathway in Cardiac Remodeling and Heart Failure
Zhou, S., Sun, W., Zhang, Z., & Zheng, Y. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/260429 · Cited by 205
Wu, J., Sun, J., & Yang, X. (2010) · Toxicology Letters · doi:10.1016/j.toxlet.2010.09.009 · Cited by 205
Compounds from Allium species with cytotoxic and antimicrobial activity
Lanzotti, V., Scala, F., & Bonanomi, G. (2014) · Phytochemistry Reviews · doi:10.1007/s11101-014-9366-0 · Cited by 207
Intraperoxisomal redox balance in mammalian cells: oxidative stress and interorganellar cross-talk
Ivashchenko, O., Veldhoven, P. P. V., Brees, C., Ho, Y.-S., Terlecky, S. R., & Fransen, M. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-11-0919 · Cited by 208
Sources and implications of NADH/NAD+ redox imbalance in diabetes and its complications
Yan, L.-J., Wu, J., Jin, Z., & Zheng, H. (2016) · Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy · doi:10.2147/dmso.s106087 · Cited by 198
Otero, P., Carpena, M., Garcia‐Oliveira, P., Echave, J., Soria-López, A., García-Pérez, P., Fraga‐Corral, M., Cao, H., Nie, S., Xiao, J., et al. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1969534 · Cited by 207
Effects of Atmospheric Pressure Plasmas on Isolated and Cellular DNA—A Review
Arjunan, K. P., Sharma, V. K., & Ptasińska, S. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16022971 · Cited by 198
Phthalate induced oxidative stress and DNA damage in earthworms (Eisenia fetida)
Song, P., Gao, J., Li, X., Zhang, C., Zhu, L., Wang, J., & Wang, J. (2019) · Environment International · doi:10.1016/j.envint.2019.04.074 · Cited by 200
Sun, D., Zou, Y., Song, L., Han, S., Yang, H., Chu, D., Dai, Y., Ma, J., O’Driscoll, C. M., Yu, Z., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.06.005 · Cited by 201
Regulation of NF-B-Induced Inflammatory Signaling by Lipid Peroxidation-Derived Aldehydes
Yadav, U. C. S., & Ramana, K. V. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/690545 · Cited by 203
Nrf2-A regulator of keratinocyte redox signaling
Schäfer, M., & Werner, S. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.018 · Cited by 192
Xiao, W. H., & Bennett, G. J. (2012) · Pain · doi:10.1016/j.pain.2011.12.011 · Cited by 192
Redox toxicology of environmental chemicals causing oxidative stress
Zheng, F., Gonçalves, F. M., Abiko, Y., Li, H., Kumagai, Y., & Aschner, M. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101475 · Cited by 198
Oxidative Stress and Antioxidant Treatments in Cardiovascular Diseases
Wang, W., & Kang, P. M. (2020) · Antioxidants · doi:10.3390/antiox9121292 · Cited by 199
Interactions between reactive oxygen species and autophagy
Redza-Dutordoir, M., & Averill‐Bates, D. A. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119041 · Cited by 199
Fission and proliferation of peroxisomes
Schrader, M., Bonekamp, N. A., & Islinger, M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.014 · Cited by 189
Mechanisms of chemotherapy-induced behavioral toxicities
Vichaya, E. G., Chiu, G. S., Krukowski, K., Lacourt, T. E., Kavelaars, A., Dantzer, R., Heijnen, C. J., & Walker, A. K. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00131 · Cited by 197
Xiong, P., Huang, X., Ye, N., Lu, Q., Zhang, G., Peng, S., Wang, H., & Liu, Y. (2022) · Advanced Science · doi:10.1002/advs.202106049 · Cited by 191
Murray, C. I., Uhrigshardt, H., O’Meally, R. N., Cole, R. N., & Eyk, J. E. V. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.013441 · Cited by 189
MacGarvey, N. C., Suliman, H. B., Bartz, R. R., Fu, P. P., Withers, C. M., Welty‐Wolf, K. E., & Piantadosi, C. A. (2012) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201106-1152oc · Cited by 185
Liu, J., Wen, X.-Y., Lu, J.-F., Kan, J., & Jin, C. (2014) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2014.01.021 · Cited by 184
Self-Assembling Nucleic Acid Nanostructures Functionalized with Aptamers
Krissanaprasit, A., Key, C. M., Pontula, S., & LaBean, T. H. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01332 · Cited by 187
Mazzone, P., Tierney, W., Hossain, M., Puvenna, V., Janigro, D., & Cucullo, L. (2010) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph7124111 · Cited by 183
Bridges between mitochondrial oxidative stress, ER stress and mTOR signaling in pancreatic β cells
Wang, J., Yang, X., & Zhang, J. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.05.007 · Cited by 181
Wang, D., Lee, M. M. S., Xu, W., Kwok, R. T. K., Lam, J. W. Y., & Tang, B. Z. (2018) · Theranostics · doi:10.7150/thno.27787 · Cited by 182
Role of oxidative stress in epileptogenesis and potential implications for therapy
Borowicz, K. K., & Czuczwar, S. J. (2020) · Pharmacological Reports · doi:10.1007/s43440-020-00143-w · Cited by 181
Olson, K. R., Gao, Y., Arif, F., Arora, K., Patel, S., DeLeon, E. R., Sutton, T. R., Feelisch, M., Cortese-Krott, M. M., & Straub, K. D. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.009 · Cited by 178
Azizi, M., Ghourchian, H., Yazdian, F. A., Bagherifam, S., Bekhradnia, S., & Nyström, B. (2017) · Scientific Reports · doi:10.1038/s41598-017-05461-3 · Cited by 179
Versatile Fluorescent Probes for Imaging the Superoxide Anion in Living Cells and In Vivo
Xiao, H., Zhang, W., Li, P., Zhang, W., Wang, X., & Tang, B. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201906793 · Cited by 176
Multiple aspects of the interaction of biomacromolecules with inorganic surfaces
Fenoglio, I., Fubini, B., Ghibaudi, E. M., & Turci, F. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.08.001 · Cited by 176
Kim, K. A., Yu, S. N., Lee, S.-Y., Chun, S.-S., Choi, Y.-L., Park, Y.-M., Song, C. S., Chatterjee, B., & Ahn, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.08.054 · Cited by 176
Molecular mechanism on cadmium-induced activity changes of catalase and superoxide dismutase
Wang, J., Zhang, H., Zhang, T., Zhang, R., Liu, R., & Chen, Y. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.02.037 · Cited by 173
MOF-Mediated Destruction of Cancer Using the Cell’s Own Hydrogen Peroxide
Ranji‐Burachaloo, H., Karimi, F., Xie, K., Fu, Q., Gurr, P. A., Dunstan, D. E., & Qiao, G. G. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b07981 · Cited by 174
Impact of ROS Generated by Chemical, Physical, and Plasma Techniques on Cancer Attenuation
Mitra, S., Nguyen, L. N., Akter, M., Park, G., Choi, E. H., & Kaushik, N. K. (2019) · Cancers · doi:10.3390/cancers11071030 · Cited by 179
β-Hydroxybutyrate induces bovine hepatocyte apoptosis via an ROS-p38 signaling pathway
Song, Y., Li, N., Gu, J., Fu, S., Peng, Z., Zhao, C., Zhang, Y., Li, X., Wang, Z., Li, X., et al. (2016) · Journal of Dairy Science · doi:10.3168/jds.2016-11219 · Cited by 172
Inflammation and Oxidative Stress in Multiple Sclerosis: Consequences for Therapy Development
Pegoretti, V., Swanson, K. A., Bethea, J. R., Probert, L., Eisel, U. L. M., & Fischer, R. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7191080 · Cited by 187
Mary, V. S., Theumer, M. G., Arias, S. L., & Rubinstein, H. R. (2012) · Toxicology · doi:10.1016/j.tox.2012.08.012 · Cited by 171
Applications of nanozymes in the environment
Meng, Y., Li, W., Pan, X., & Gadd, G. M. (2020) · Environmental Science Nano · doi:10.1039/c9en01089k · Cited by 172
Abdelshafy, A. M., Belwal, T., Liang, Z., Wang, L., Li, D., Luo, Z., & Li, L. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1898335 · Cited by 187
Zhang, Z., Teruya, K., Eto, H., & Shirahata, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027441 · Cited by 167
Li, J., Shu, Y., Hao, T., Wang, Y., Qian, Y., Duan, C., Sun, H., Lin, Q., & Wang, C. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.08.031 · Cited by 165
Azzariti, A., Iacobazzi, R. M., Fonte, R., Porcelli, L., Gristina, R., Favia, P., Fracassi, F., Trizio, I., Silvestris, N., Guida, G., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40637-z · Cited by 164
A Review of the Application of Inflammatory Biomarkers in Epidemiologic Cancer Research
Brenner, D. R., Scherer, D., Muir, K. R., Schildkraut, J. M., Boffetta, P., Spitz, M. R., Marchand, L. L., Chan, A. T., Goode, E. L., Ulrich, C. M., et al. (2014) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-14-0064 · Cited by 171
Mayola, E., Gallerne, C., Esposti, D. D., Martel, C., Pervaiz, S., Larue, L., Debuire, B., Lemoine, A., Brenner, C., & Lemaire, C. (2011) · APOPTOSIS · doi:10.1007/s10495-011-0625-x · Cited by 168
Lin, P., Niimi, H., Ohsugi, Y., Tsuchiya, Y., Shimohira, T., Komatsu, K., Liu, A., Shiba, T., Aoki, A., Iwata, T., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168900 · Cited by 164
8-Oxo-7,8-dihydroguanine: Links to gene expression, aging, and defense against oxidative stress
Radak, Z. O., & Boldogh, I. R. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.008 · Cited by 164
Mitochondrial Sirtuins and Their Relationships with Metabolic Disease and Cancer
Kumar, S., & Lombard, D. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6213 · Cited by 160
Gu, Z., Wang, H., Li, L., Liu, Y. S., Deng, X. B., Huo, S., Yuan, F., Liu, Z. F., Tong, H., & Su, L. (2014) · Scientific Reports · doi:10.1038/srep04469 · Cited by 161
Characterization of the Usage of the Serine Metabolic Network in Human Cancer
Mehrmohamadi, M., Liu, X., Shestov, A. A., & Locasale, J. W. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.026 · Cited by 158
A Robust Oxygen-Carrying Hemoglobin-Based Natural Sonosensitizer for Sonodynamic Cancer Therapy
Yuan, M., Liang, S., Zhou, Y., Xiao, X., Liu, B., Yang, C., Ma, P., Cheng, Z., & Lin, J. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c01220 · Cited by 157
Liposomal Antioxidants for Protection against Oxidant-Induced Damage
Suntres, Z. E. (2011) · Journal of Toxicology · doi:10.1155/2011/152474 · Cited by 164
Zhu, L., Yuan, H. Y., Guo, C., Lu, Y., Deng, S., Yang, Y., Wei, Q., Wen, L., & He, Z. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22906 · Cited by 154
The role of mitochondrial DNA mutation on neurodegenerative diseases
Cha, M.-Y., Kim, D. K., & Mook‐Jung, I. (2015) · Experimental & Molecular Medicine · doi:10.1038/emm.2014.122 · Cited by 157
Morris, G., Berk, M., Carvalho, A. F., Maes, M. H. J., Walker, A. J., & Puri, B. K. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.12.036 · Cited by 155
Redox Control of the Survival of Healthy and Diseased Cells
Zhang, Y., Du, Y., Le, W., Wang, K., Kieffer, N., & Zhang, J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3685 · Cited by 161
Nutrition and human health from a sex–gender perspective
Marino, M., Masella, R., Bulzomi, P., Campesi, I., Malorni, W., & Franconi, F. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.02.001 · Cited by 159
Einfalt, T., Witzigmann, D., Edlinger, C. R., Sieber, S., Goers, R., Najer, A., Spulber, M., Onaca, O., Huwyler, J., & Palivan, C. G. (2018) · Nature Communications · doi:10.1038/s41467-018-03560-x · Cited by 155
Wei, P., Yang, F., Zheng, Q., Tang, W., & Li, J. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00073 · Cited by 155
Huang, M., Chiang, S., Kalinowski, D. S., Bae, D.-H., Sahni, S., & Richardson, D. R. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6392763 · Cited by 155
Electrochemistry as a Tool for Studying Antioxidant Properties
Sochor, J., Dobes, J., Kryštofová, O., Ruttkay-Nedecký, B., Babula, P., Pohanka, M., Juríková, T., Zítka, O., Adam, V., Klejdus, B., et al. (2013) · International Journal of Electrochemical Science · doi:10.1016/s1452-3981(23)12902-6 · Cited by 155
Zhang, X., Wang, X., Wu, T., Li, B., Liu, T., Wang, R., Liu, Q., Liu, Z., Gong, Y., & Shao, C. (2015) · Scientific Reports · doi:10.1038/srep12579 · Cited by 156
Singh, N., Kumar, A., Gupta, V. K., & Sharma, B. (2018) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00193 · Cited by 161
Rather, R. A., & Bhagat, M. (2019) · Cancer Medicine · doi:10.1002/cam4.1411 · Cited by 157
Hecker, L. (2018) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00275.2017 · Cited by 154
New chalcone derivatives as potential antimicrobial and antioxidant agent
Okolo, E. N., Ugwu, D. I., Ezema, B. E., Ndefo, J. C., Eze, F. U., Ezema, C. G., Ezugwu, J. A., & Ujam, O. T. (2021) · Scientific Reports · doi:10.1038/s41598-021-01292-5 · Cited by 160
Olson, K. R., Gao, Y., DeLeon, E. R., Arif, M. S., Arif, F., Arora, N., & Straub, K. D. (2017) · Redox Biology · doi:10.1016/j.redox.2017.02.021 · Cited by 151
Dynamic PGAM5 multimers dephosphorylate BCL-xL or FUNDC1 to regulate mitochondrial and cellular fate
Ma, K., Zhang, Z., Chang, R., Cheng, H., Mu, C., Zhao, T., Chen, L., Zhang, C., Luo, Q., Lin, J., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0396-4 · Cited by 150
Martinez, R. M., Pinho-Ribeiro, F. A., Steffen, V. S., Caviglione, C. V., Vignoli, J. A., Barbosa, D. S., Baracat, M. M., Georgetti, S. R., Verri, W. A., Jr., & Casagrande, R. (2015) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5b00198 · Cited by 157
Antibacterial and antioxidant activities of aqueous extracts of eight edible mushrooms
Ren, L., Hémar, Y., Perera, C. O., Lewis, G. D., Krissansen, G. W., & Buchanan, P. (2014) · Bioactive Carbohydrates and Dietary Fibre · doi:10.1016/j.bcdf.2014.01.003 · Cited by 148
Taherishirazi, M., Gholami, H., Kavoosi, G., Rowshan, V., & Tafsiry, A. (2014) · Food Science & Nutrition · doi:10.1002/fsn3.85 · Cited by 148
Reactive Oxygen Species, Oxidative Damage and Cell Death
Ghosh, N., Das, A., Chaffee, S. M., Roy, S., & Sen, C. K. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805417-8.00004-4 · Cited by 158
Zhang, Y., Li, Z., Kholodkevich, S. V., Sharov, A. N., Feng, Y., Ren, N., & Sun, K. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.02.159 · Cited by 148
Huang, H., Zhang, S., Li, Y., Liu, Z., Mi, L., Cai, Y., Wang, X., Chen, L., Ran, H., Xiao, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24108-6 · Cited by 155
Regulation of Cellular Metabolism and Hypoxia by p53Preprint
Humpton, T. J., & Vousden, K. H. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026146 · Cited by 154
Chloride-Mediated Apoptosis-Inducing Activity of Bis(sulfonamide) Anionophores.
Saha, T., Hossain, M. S., Saha, D., Lahiri, M., & Talukdar, P. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b01723 · Cited by 96
Redox Regulation of Homeostasis and Proteostasis in Peroxisomes
Walker, C. L., Pomatto, L. C. D., Tripathi, D. N., & Davies, K. J. A. (2017) · Physiological Reviews · doi:10.1152/physrev.00033.2016 · Cited by 149
Wang, C., He, J., Xu, T., Han, H., Zhu, Z., Meng, L., Pang, Q., & Fan, R. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.111299 · Cited by 150
Cytotoxicity-Related Bioeffects Induced by Nanoparticles: The Role of Surface Chemistry
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
Messina, C. M., Faggio, C., Laudicella, V. A., Sanfilippo, M., Trischitta, F., & Santulli, A. (2014) · Aquatic Toxicology · doi:10.1016/j.aquatox.2014.10.001 · Cited by 143
Roles of melatonin in the field of reproductive medicine
Yong, W., Ma, H., Na, M., Gao, T., Zhang, Y., Hao, L., Yu, H., Yang, H., & Deng, X. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112001 · Cited by 143
Mitochondria are targets for peroxisome-derived oxidative stress in cultured mammalian cells
Wang, B., Veldhoven, P. P. V., Brees, C., Rubio, N., Nordgren, M., Apanasets, O., Kunze, M., Baes, M. I., Agostinis, P., & Fransen, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.173 · Cited by 146
Mitra, S., Anand, U., Jha, N. K., Shekhawat, M. S., Saha, S. C., Nongdam, P., Rengasamy, K. R. R., Proćków, J., & Dey, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.772418 · Cited by 151
Global DNA Methylation Levels are Modulated by Mitochondrial DNA Variants
Bellizzi, D., D’Aquila, P., Giordano, M., Montesanto, A., & Passarino, G. (2012) · Epigenomics · doi:10.2217/epi.11.109 · Cited by 141
Duan, D., Zhang, B., Yao, J., Liu, Y., Sun, J., Ge, C., Peng, S., & Fang, J. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.027 · Cited by 140
Ineffective Erythropoiesis in β ‐Thalassemia
Ribeil, J., Arlet, J., Dussiot, M., Moura, I. C., Courtois, G., & Hermine, O. (2013) · The Scientific World JOURNAL · doi:10.1155/2013/394295 · Cited by 149
Eastman, C. L., D’Ambrosio, R., & Ganesh, T. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107907 · Cited by 140
Nanozymes for regulation of reactive oxygen species and disease therapy
Dai, Y., Ding, Y., & Li, L. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.03.036 · Cited by 142
Shiizaki, S., Naguro, I., & Ichijo, H. (2012) · Advances in Biological Regulation · doi:10.1016/j.jbior.2012.09.006 · Cited by 138
Bao, D., Wang, J., Pang, X., & Liu, H. (2017) · Molecules · doi:10.3390/molecules22071122 · Cited by 135
Combined Fenton and starvation therapies using hemoglobin and glucose oxidase
Ranji‐Burachaloo, H., Reyhani, A., Gurr, P. A., Dunstan, D. E., & Qiao, G. G. (2019) · Nanoscale · doi:10.1039/c8nr09107b · Cited by 137
Recent advances in small-molecule fluorescent probes for studying ferroptosis
Qi, Y., Wang, H., Chen, L., Duan, Y., Yang, S., & Zhu, H. (2022) · Chemical Society Reviews · doi:10.1039/d1cs01167g · Cited by 138
An overview about oxidation in clinical practice of skin aging
Silva, S. A. M. E., Michniak-Kohn, B., & Leonardi, G. R. (2017) · Anais Brasileiros de Dermatologia · doi:10.1590/abd1806-4841.20175481 · Cited by 134
Cell Death-Associated Molecular-Pattern Molecules: Inflammatory Signaling and Control
Sangiuliano, B. A., Pérez-Sosa, M., Moreira, D., & Belizário, J. E. (2014) · Mediators of Inflammation · doi:10.1155/2014/821043 · Cited by 142
Tang, H., Li, C., Zhang, Y., Zheng, H., Cheng, Y., Zhu, J., Chen, X., Zhu, Z., Piao, J., & Li, F. (2020) · Theranostics · doi:10.7150/thno.46771 · Cited by 134
Traumatic Brain Injury and NADPH Oxidase: A Deep Relationship
Angeloni, C., Prata, C., Sega, F. V. D., Piperno, R., & Hrelia, S. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/370312 · Cited by 138
Mitochondria in cancer: at the crossroads of life and death
Fogg, V. C., Lanning, N. J., & MacKeigan, J. P. (2011) · 癌症:英文版 · doi:10.5732/cjc.011.10018 · Cited by 139
Targeting ROS-Mediated Crosstalk Between Autophagy and Apoptosis in Cancer
Gao, L., Loveless, J., Shay, C., & Teng, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-42667-5_1 · Cited by 135
Metadata
- Authors
- Circu, M. L., & Aw, T. Y.
- Affiliations
- Louisiana State University Health Sciences Center Shreveport (US)
- Corresponding author
- Aw, Tak Yee
- ORCID
- Circu, Magdalena L.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2010-03
- Volume
- 48
- Issue
- 6
- Pages
- 749-762
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC2823977
- OpenAlex
- W1977178308
- Cited by
- 3,340
- References
- 224
- Citations by year
- 2026: 116 · 2025: 134 · 2024: 154 · 2023: 190 · 2022: 262 · 2021: 243 · 2020: 243 · 2019: 298 · 2018: 264 · 2017: 287 · 2016: 240 · 2015: 217 · 2014: 210 · 2013: 163 · 2012: 152
- FWCI
- 13.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK044510, DK 44510)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Keywords
- reactive oxygen species, apoptosis, oxidative stress, redox signaling, glutathione, thioredoxin, pyridine nucleotides, death receptor signaling, mitochondrial apoptosis, antioxidant deficiency, redox homeostasis
- MeSH terms
- Animals, Humans, Oxidation-Reduction, Signal Transduction, Apoptosis, 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