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Unraveling the Biological Roles of Reactive Oxygen Species
Open accessAbstract
Reactive oxygen species are not only harmful agents that cause oxidative damage in pathologies, they also have important roles as regulatory agents in a range of biological phenomena. The relatively recent development of this more nuanced view presents a challenge to the biomedical research community on how best to assess the significance of reactive oxygen species and oxidative damage in biological systems. Considerable progress is being made in addressing these issues, and here we survey some recent developments for those contemplating research in this area.
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“Antioxidants are heterogeneous [159] they work in distinct ways and importantly they do not solely regulate ROS.”
From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [159]
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“Multiple key signalling pathways contribute to microglial immune activation, including NFκB and MAPKs (Figure 3) and there is evidence ROS is an important modulator of the immune response by influencing these cell signalling pathways in microglia.”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [137]
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“At physiological concentrations, ROS are vital secondary messengers in multiple cellular processes, including inflammation, cellular growth and differentiation [136,137].”
From ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease (2020) · cites this paper as [137]
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Citations
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Aging: 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
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Self-citationReconciling the chemistry and biology of reactive oxygen species
Winterbourn, C. C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.85 · Cited by 2,504
Self-citationWang, H., & Joseph, J. A. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00107-0 · Cited by 2,355
Halliwell, B., & Whiteman, M. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705776 · Cited by 2,238
Self-citationMitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
Kujoth, G. C., Hiona, A., Pugh, T. D., Someya, S., Panzer, K., Wohlgemuth, S. E., Hofer, T., Seo, A. Y., Sullivan, R., Jobling, W. A., et al. (2005) · Science · doi:10.1126/science.1112125 · Cited by 2,165
Molecular mechanisms of N-acetylcysteine actions
Zafarullah, M., Li, W. Q., Sylvester, J., & Ahmad, M. (2003) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s000180300001 · Cited by 1,343
Genetically encoded fluorescent indicator for intracellular hydrogen peroxide
Belousov, V. V., Fradkov, A. F., Lukyanov, K. A., Staroverov, D. B., Shakhbazov, K., Terskikh, A. V., & Lukyanov, S. (2006) · Nature Methods · doi:10.1038/nmeth866 · Cited by 1,286
Self-citationHanson, G. T., Aggeler, R., Oglesbee, D., Cannon, M., Capaldi, R. A., Tsien, R. Y., & Remington, S. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312846200 · Cited by 988
Flagged first, then by citations
Research works printed but not linked: 2
- Bjelakovic, 2008, Cochrane Database Syst. Rev., 2, CD007176
- Cochemé, 2010, Curr. Opin. Investig. Drugs, 11, 426
Cited by
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Metabolic, autophagic, and mitophagic activities in cancer initiation and progression
Hjelmeland, A. B., & Zhang, J. (2016) · Biomedical Journal · doi:10.1016/j.bj.2015.10.002 · Cited by 24
The Die Is Cast: Precision Electrophilic Modifications Contribute to Cellular Decision Making
Long, M. J. C., & Aye, Y. (2016) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.6b00261 · Cited by 24
Hu, H., Wang, A., Huang, L. Z., Zou, Y., Gu, Y., Chen, X., Zhao, Y., & Yang, Y. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.03.041 · Cited by 28
Two-photon Fluorescent Sensors for Visual Detection of Abnormal Superoxide Anion in Diabetes Mice
Song, W., Dong, B., Lu, Y., Li, Z., Zhang, W., & Lin, W. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.129537 · Cited by 24
Tracing the Trail of Protons through Complex I of the Mitochondrial Respiratory Chain
Mourier, A., & Larsson, N. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001129 · Cited by 24
Self-citationC. elegans screening strategies to identify pro-longevity interventions
Maglioni, S., Arsalan, N., & Ventura, N. (2016) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.07.010 · Cited by 25
Cairns, A. G., McQuaker, S. J., Murphy, M. P., & Hartley, R. C. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2288-8_3 · Cited by 22
Self-citationThe Role of Selenium in Oxidative Stress and in Nonthyroidal Illness Syndrome (NTIS): An Overview
Silvestrini, A., Mordente, A., Martino, G., Bruno, C., Vergani, E., Meucci, E., & Mancini, A. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180201111159 · Cited by 25
Παντελιά, Ά., Daskalaki, I., Cuquerella, M. C., Rotas, G., Miranda, M. A., & Vougioukalakis, G. C. (2019) · Molecules · doi:10.3390/molecules24213957 · Cited by 22
Zhao, Y., Xue, Y., Sun, J., Xuan, H., Xu, Y., Cui, Y., & Dong, J. (2020) · New Journal of Chemistry · doi:10.1039/d0nj02945a · Cited by 23
Kalyanaraman, B. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101721 · Cited by 26
Self-citationCho, M., Nghĩa, N. V., & Yoon, J. (2022) · ACS Measurement Science Au · doi:10.1021/acsmeasuresciau.1c00055 · Cited by 23
Mitochondrial fragmentation in liver cancer: Emerging player and promising therapeutic opportunities
Wang, Q., Yu, P., Liu, C., He, X., & Wang, G. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215912 · Cited by 24
Zhang, M., Deng, Y.-L., Liu, C., Lu, W., & Zeng, Q. (2023) · Chemosphere · doi:10.1016/j.chemosphere.2023.138808 · Cited by 23
Zhang, H., Wei, Z., Tong, Y., Song, X., Li, S., Sun, Y., Liu, C., Han, F., & Yu, J. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.116628 · Cited by 23
Muller, A. P., Zimmer, E. R., Kalinine, E., Haas, C. B., Oses, J. P., de Assis, A. M., Galina, A., Souza, D. O., & Portela, L. V. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112066 · Cited by 23
Alnuqaydan, A. M., & Rah, B. (2019) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201020666190318120103 · Cited by 23
Sestrin2, a Regulator of Thermogenesis and Mitohormesis in Brown Adipose Tissue
Ro, S., Semple, I. A., Ho, A., Park, H., & Lee, J. H. (2015) · Frontiers in Endocrinology · doi:10.3389/fendo.2015.00114 · Cited by 24
Redox regulation in diabetic kidney disease
Daehn, I. S., Ekperikpe, U. S., & Stadler, K. (2023) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00047.2023 · Cited by 23
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Marasco, V., & Spencer, K. A. (2015) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780198718666.003.0012 · Cited by 23
A novel MnO–CrN nanocomposite based non-enzymatic hydrogen peroxide sensor
Tareen, A. K., Khan, K., Ahmad, W., Khan, M. F., Khan, Q. U., & Liu, X. (2021) · RSC Advances · doi:10.1039/d1ra01485d · Cited by 22
Wani, M. Y., Ahmad, A., Aqlan, F. M., & Al‐Bogami, A. S. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105260 · Cited by 23
Pakfetrat, Z., Janfeshan, S., Masjedi, F., Rafiei, M., & Karimi, Z. (2021) · Drug and Chemical Toxicology · doi:10.1080/01480545.2021.1977024 · Cited by 22
Mccrimmon, A. N., Corbin, S., Shrestha, B., Roman, G. T., Dhungana, S., & Stadler, K. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102520 · Cited by 22
Thambiraj, J., Paulsamy, S., & Sevukaperumal, R. (2012) · Asian Pacific Journal of Tropical Biomedicine · doi:10.1016/s2221-1691(12)60142-7 · Cited by 22
Kaur, A., Jankowska, K., Pilgrim, C., Fraser, S. T., & New, E. J. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6495 · Cited by 26
Saputera, W. H., Scott, J. A., Tahini, H. A., Low, G. K.-C., Tan, X., Smith, S. C., Wang, D., & Amal, R. (2017) · ACS Catalysis · doi:10.1021/acscatal.7b00700 · Cited by 22
Sun, C., Du, W., Wang, P., Wu, Y., Wang, B., Wang, J., & Xie, W. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.10.123 · Cited by 22
Biological Chemistry of Reactive Oxygen Species
Winterbourn, C. C. (2012) · Wiley eBooks · doi:10.1002/9781119953678.rad077 · Cited by 22
Self-citationRedox control of enzymatic functions: The electronics of life's circuitry
Bonini, M. G., Consolaro, M. E. L., Hart, P. C., Mao, M., de Abreu, A. L. P., & Master, А. M. (2014) · IUBMB Life · doi:10.1002/iub.1258 · Cited by 21
Advances in techniques to study incubation
Smith, J. A., Cooper, C. B., & Reynolds, S. J. (2015) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780198718666.003.0015 · Cited by 22
Marchand, V., Charlier, N., Verrax, J., Calderón, P. B., Levêque, P., & Gallez, B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0172998 · Cited by 21
Παπανικολάου, Κ., Veskoukis, A. S., Draganidis, D., Baloyiannis, I., Deli, C. K., Poulios, A., Jamurtas, A. Z., & Fatouros, I. G. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.10.001 · Cited by 22
Ji, K., Shan, J., Wang, X., Tan, X., Hou, J., Liu, Y., & Song, Y. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.029 · Cited by 21
S3QELs protect against diet‐induced intestinal barrier dysfunction
Watson, M. A., Pattavina, B., Hilsabeck, T. A. U., Lopez-Dominguez, J. A., Kapahi, P., & Brand, M. D. (2021) · Aging Cell · doi:10.1111/acel.13476 · Cited by 21
Lu, H., Lü, Q., Sun, H., Wang, Z., Shi, X., Ding, Y., Ran, X., Pei, J., Pan, Y., & Zhang, Q. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c09320 · Cited by 21
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Cobley, J. N. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102936 · Cited by 24
Liu, F., Wang, S., Wang, Y.-P., Jiang, P., Miao, J., Zhao, B., & Lin, Z. (2024) · Talanta · doi:10.1016/j.talanta.2024.126135 · Cited by 21
Zhang, L., Qian, M., Xia, J., Chen, L., Cui, H., Xia, Y., Xu, L., Wang, J., & Peng, X. (2018) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2018.10.030 · Cited by 21
Regulations of reactive oxygen species in plants abiotic stress: an integrated overview
Liu, S., & Yang, R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818204-8.00017-5 · Cited by 21
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Xu, Q., Zhang, K., Fù, Y., Ma, H., & Zhu, F. (2020) · Crop Protection · doi:10.1016/j.cropro.2020.105272 · Cited by 21
Bottje, W. G. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819770-7.00043-8 · Cited by 22
Wang, X., Gou, Z., Lv, J., & Zuo, Y. (2022) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2022.121481 · Cited by 20
Yang, Y., Li, Y., Mei, X., Yang, M., Huang, H., Du, F., Wu, J., He, Y., Sun, J., Wang, H., et al. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.890534 · Cited by 20
Liu, D., & Bao, F. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.10.063 · Cited by 20
Huang, B. K., Langford, T. F., & Sikes, H. D. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6482 · Cited by 20
Macrophage-derived superoxide production and antioxidant response following skeletal muscle injury
Moal, E. L., Juban, G., Bernard, A. S., Varga, T., Policar, C., Chazaud, B., & Mounier, R. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.024 · Cited by 20
Recent Advances in ROS-Responsive Cell Sheet Techniques for Tissue Engineering
Koo, M.-A., Lee, M. H., & Park, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225656 · Cited by 20
Mohan, J. M., Amreen, K., Javed, A., Dubey, S. K., & Goel, S. (2020) · Applied Nanoscience · doi:10.1007/s13204-020-01480-1 · Cited by 20
Responsive Polymeric Nanoparticles for Biofilm-infection Control
Su, L., Liu, Y., Li, Y., An, Y., & Shi, L. (2021) · Chinese Journal of Polymer Science · doi:10.1007/s10118-021-2610-3 · Cited by 20
Sartori, A., Mano, C. M., Mantovani, M. C., Dyszy, F. H., Massari, J., Tokikawa, R., Nascimento, O. R., Nantes, I. L., & Bechara, E. J. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057790 · Cited by 20
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Cooper, C. B., Bailey, R. L., & Leech, D. I. (2015) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780198718666.003.0017 · Cited by 21
Liu, F., Bai, Q., Tang, W., Zhang, S., Guo, Y. H., Pan, S., Ma, X., Yang, Y., & Fan, H. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1505153 · Cited by 23
Bi, X., Wang, Y., Wang, D., Liu, L., Zhu, W. T., Zhang, J., & Zha, X. (2020) · RSC Advances · doi:10.1039/d0ra03905e · Cited by 19
Cheng, R., Guo, L., Fan, L., Jiang, J., & Zhao, Y. (2020) · Chemical Communications · doi:10.1039/d0cc03607b · Cited by 19
Lorenzo-Anota, H. Y., Zárate-Triviño, D. G., Uribe-Echeverría, J. A., Ávila-Ávila, A., Rangel-López, J. R., Martínez‐Torres, A. C., & Rodríguez-Padilla, C. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13070942 · Cited by 21
Tian, L., Chen, C., Gong, J., Han, Q., Shi, Y., Li, M., Cheng, L., Wang, L., & Dong, B. (2023) · Sensors · doi:10.3390/s23104641 · Cited by 19
Guo, H., Aleyasin, H., Howard, S. S., Dickinson, B. C., Lin, V., Xu, C., Chen, Y., Ratan, R. R., & Haskew-Layton, R. E. (2013) · Journal of Biomedical Optics · doi:10.1117/1.jbo.18.10.106002 · Cited by 19
Marrakchi, M., Liu, X., & Andreescu, S. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-06068-2_23 · Cited by 20
Eder, K., Siebers, M., Most, E., Scheibe, S., Weißmann, N., & Geßner, D. K. (2017) · Nutrition & Metabolism · doi:10.1186/s12986-017-0225-z · Cited by 19
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Noguera, J. C. (2017) · PeerJ · doi:10.7717/peerj.3094 · Cited by 19
Zhang, Y., Xia, M., Ao, R., Gao, L., Tang, Y., Huang, J., Luo, Y., Chen, Z., Wang, B., & Huang, Z. (2021) · Nanomaterials · doi:10.3390/nano11112875 · Cited by 18
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Gao, L., Ortega‐Sáenz, P., Moreno‐Domínguez, A., & López‐Barneo, J. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0255 · Cited by 18
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Sabharwal, S. S., Dudley, V. J., Landwerlin, C., & Schumacker, P. T. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104624 · Cited by 18
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Margaritelis, N. V. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.06.004 · Cited by 18
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Cornell, A., & Williams, T. D. (2017) · Journal of Experimental Biology · doi:10.1242/jeb.162248 · Cited by 18
Song, Z., Hou, Y., Bai, F., & Fang, J. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104520 · Cited by 18
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Noble, A., Guille, M., & Cobley, J. N. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.08.018 · Cited by 18
Wang, Y., Hougaard, A. B., Paulander, W., Skibsted, L. H., Ingmer, H., & Andersen, M. L. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.01199-15 · Cited by 18
Nie, Y., Hu, J., Hou, Q., Zheng, W., Zhang, X., Yang, T., Ma, L., & Yan, X. (2019) · The FASEB Journal · doi:10.1096/fj.201900253rr · Cited by 18
Delsuc, N., Hammouda, Y. B. H., Coulibaly, K., Bathily, A., Han, M. T. S., & Policar, C. (2022) · Molecules · doi:10.3390/molecules27175476 · Cited by 18
Tuncay, A., Crabtree, D. R., Muggeridge, D. J., Husi, H., & Cobley, J. N. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.05.006 · Cited by 17
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Gómez, M. A., Fernández-Santos, M. R., Jurado‐Campos, A., Soria‐Meneses, P. J., Montoro, V., Soler, A. J., Garde, J. J., & Robledo, V. R. (2023) · Antioxidants · doi:10.3390/antiox12081626 · Cited by 17
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Chang‐Chien, J., Huang, J., Tsai, H., Wang, S.-L., Kuo, M., & Yao, T. (2024) · Respiratory Research · doi:10.1186/s12931-024-02951-7 · Cited by 18
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Birchard, G. F., & Deeming, D. C. (2015) · Oxford University Press eBooks · doi:10.1093/acprof:oso/9780198718666.003.0009 · Cited by 18
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Bottje, W. G. (2019) · Journal of Animal Science · doi:10.1093/jas/skz219 · Cited by 18
Arcos, M. L. B., Sterle, H., Vercelli, C. A., Valli, E., Cayrol, M. F., Klecha, A. J., Paulazo, M. A., Flaqué, M. C. D., Franchi, A. M., & Cremaschi, G. (2013) · APOPTOSIS · doi:10.1007/s10495-013-0869-8 · Cited by 17
Morgan, B. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140101 · Cited by 18
Jackson, M. J. (2016) · The Journal of Physiology · doi:10.1113/jp270657 · Cited by 18
Overcoming Reductant Interference in Peroxidase-Based Assays for Hydrogen Peroxide Quantification
Jiang, S., & Penner, M. H. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b02248 · Cited by 17
Li, S., Luo, S., Chen, H., Zheng, Y., Lin, L., Yao, H., & Lin, X. (2019) · Drug Design Development and Therapy · doi:10.2147/dddt.s201816 · Cited by 17
Reactive Oxygen Species in Aqueous Media (A Review)
Belovolova, L. V. (2020) · Optics and Spectroscopy · doi:10.1134/s0030400x20070036 · Cited by 16
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Mattioli, S., Dimauro, C., Cesarani, A., Bosco, A. D., Bartolini, D., Galli, F., Migni, A., Sebastiani, B., Signorini, C., Oger, C., et al. (2022) · Antioxidants · doi:10.3390/antiox11030531 · Cited by 16
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Song, Y., Zhang, Z., Cao, Y., & Yu, Z. (2022) · ChemBioChem · doi:10.1002/cbic.202200497 · Cited by 16
Vitamin E reduces oxidative stress in brains of male albino male rats undergoing immobilization
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Qin, X., Li, P., Casas-Martinez, J. C., Miranda‐Vizuete, A., McDermott, E. A., Dockery, P., Goljanek‐Whysall, K., & McDonagh, B. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.102003 · Cited by 17
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Metadata
- Authors
- Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., Rhee, S. G., Thornalley, P. J., Partridge, L., Gems, D., Nyström, T., Belousov, V., Schumacker, P. T., & Winterbourn, C. C.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- Karolinska Institutet (SE)
- Max Planck Institute for Biology of Ageing (DE)
- National University of Singapore (SG)
- Howard Hughes Medical Institute (US)
- Medical College of Wisconsin (US)
- Ewha Womans University (KR)
- University Hospital Coventry (GB)
- University College London (GB)
- University of Gothenburg (SE)
- Institute of Bioorganic Chemistry (RU)
- Northwestern University (US)
- University of Otago (NZ)
- Corresponding author
- Murphy, Michael P.
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2011-04
- Volume
- 13
- Issue
- 4
- Pages
- 361-366
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4445605
- OpenAlex
- W1967236260
- Cited by
- 836
- References
- 49
- Citations by year
- 2026: 31 · 2025: 44 · 2024: 49 · 2023: 55 · 2022: 61 · 2021: 64 · 2020: 61 · 2019: 47 · 2018: 51 · 2017: 53 · 2016: 66 · 2015: 64 · 2014: 60 · 2013: 59 · 2012: 48
- FWCI
- 24.69
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- National University of Singapore (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Wellcome Trust (081394)
- Medical Research Council (MC_G0901472)
- Biotechnology and Biological Sciences Research Council (BB/D020786/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Keywords
- reactive oxygen species, oxidative damage, redox signaling, biological regulation, oxidative stress, redox biology
- MeSH terms
- Antioxidants, Signal Transduction, Reactive Oxygen Species, Oxidative Stress
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