Cellular mechanisms and physiological consequences of redox-dependent signalling
Abstract
Reactive oxygen species (ROS), which were originally characterized in terms of their harmful effects on cells and invading microorganisms, are increasingly implicated in various cell fate decisions and signal transduction pathways. The mechanism involved in ROS-dependent signalling involves the reversible oxidation and reduction of specific amino acids, with crucial reactive Cys residues being the most frequent target. In this Review, we discuss the sources of ROS within cells and what is known regarding how intracellular oxidant levels are regulated. We further discuss the recent observations that reduction-oxidation (redox)-dependent regulation has a crucial role in an ever-widening range of biological activities - from immune function to stem cell self-renewal, and from tumorigenesis to ageing.
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CAFs promote cancer growth and invasiveness, and both CAFs and ROS are linked through increases in ROS-generated CAFs to which most cancers respond by increasing expression of antioxidant genes.
“CAFs can also promote cancer growth and invasiveness, and both CAFS and ROS are linked through the increases in ROS-generated CAFs to which most cancers respond by increasing the expression of antioxidant genes52–54”
From ROS in cancer therapy: the bright side of the moon (2020) · cites this paper as [54]
The NADPH oxidase system is an important source of intracellular ROS and a key player in the generation of oxidative stress.
“In addition to mitochondria, the nicotinamide adenine dinucleotide phosphate (NADPH) oxidase system has been identified as an important source of intracellular ROS and a key player in the generation of oxidative stress.”
From Oxidative Stress and Ageing: The Influence of Environmental Pollution, Sunlight and Diet on Skin (2017) · cites this paper as [9]
Cites
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 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
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 · see citing works
(1994) · New England Journal of Medicine · doi:10.1056/nejm199404143301501 · Cited by 4,737 · see citing works
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 · see citing works
Self-citationModulation of oxidative stress as an anticancer strategy
Gorrini, C., Harris, I. S., & Mak, T. W. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4002 · Cited by 3,579 · see citing works
The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820 · see citing works
Physiological Roles of Mitochondrial Reactive Oxygen Species
Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632 · see citing works
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 · see citing works
Self-citationA model for p53-induced apoptosis
Polyak, K., Xia, Y., Zweier, J. L., Kinzler, K. W., & Vogelstein, B. (1997) · Nature · doi:10.1038/38525 · Cited by 2,500 · see citing works
Rajagopalan, S., Kurz, S. D., Münzel, T. F., Tarpey, M. M., Freeman, B. Α., Griendling, K. K., & Harrison, D. G. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118623 · Cited by 2,441 · see citing works
The role of iron and reactive oxygen species in cell death
Dixon, S. J., & Stockwell, B. R. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1416 · Cited by 2,381 · see citing works
Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
DeNicola, G. M., Karreth, F. A., Humpton, T. J., Gopinathan, A., Wei, C., Frese, K., Mangal, D., Yu, K. H., Yeo, C. J., Calhoun, E. S., et al. (2011) · Nature · doi:10.1038/nature10189 · Cited by 2,277 · see citing works
Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926 · see citing works
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724 · see citing works
Autophagy Suppresses Tumorigenesis through Elimination of p62
Mathew, R., Karp, C. M., Beaudoin, B., Vuong, N., Chen, G., Chen, H.-Y., Bray, K., Reddy, A., Bhanot, G. V., Gélinas, C., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.048 · Cited by 1,723 · see citing works
Tlr signalling augments macrophage bactericidal activity through mitochondrial ros
West, A. P., Brodsky, I. E., Rahner, C., Woo, D. K., Erdjument-Bromage, H., Tempst, P., Walsh, M. C., Choi, Y., Shadel, G. S., & Ghosh, S. (2011) · Nature · doi:10.1038/nature09973 · Cited by 1,659 · see citing works
Inside the Neutrophil Phagosome: Oxidants, Myeloperoxidase, and Bacterial Killing
Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1998) · Blood · doi:10.1182/blood.v92.9.3007.421k47_3007_3017 · Cited by 1,640 · see citing works
Mitogenic Signaling Mediated by Oxidants in Ras-Transformed Fibroblasts
Irani, K., Xia, Y., Zweier, J. L., Sollott, S. J., Der, C. J., Fearon, E. R., Sundaresan, M., Finkel, T., & Goldschmidt-Clermont, P. J. (1997) · Science · doi:10.1126/science.275.5306.1649 · Cited by 1,588 · see citing works
Self-citationAntioxidants prevent health-promoting effects of physical exercise in humans
Ristow, M., Zarse, K., Oberbach, A., Klöting, N., Birringer, M., Kiehntopf, M., Stumvoll, M., Kahn, C. R., & Blüher, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903485106 · Cited by 1,582 · see citing works
Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress
Kops, G. J. P. L., Dansen, T. B., Polderman, P. E., Saarloos, I., Wirtz, K. W. A., Coffer, P. J., Huang, T.-T., Bos, J. L., Medema, R. H., & Burgering, B. M. T. (2002) · Nature · doi:10.1038/nature01036 · Cited by 1,580 · see citing works
FoxOs Are Critical Mediators of Hematopoietic Stem Cell Resistance to Physiologic Oxidative Stress
Tothova, Z., Kollipara, R., Huntly, B. J., Lee, B. H., Castrillon, D. H., Cullen, D. E., McDowell, E. P., Lazo-Kallanian, S., Williams, I. R., Sears, C., et al. (2007) · Cell · doi:10.1016/j.cell.2007.01.003 · Cited by 1,562 · see citing works
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480 · see citing works
Molecular mechanisms of the Keap1-Nrf2 pathway in stress response and cancer evolution
Taguchi, K., Motohashi, H., & Yamamoto, M. (2011) · Genes to Cells · doi:10.1111/j.1365-2443.2010.01473.x · Cited by 1,478 · see citing works
ROS-Generating Mitochondrial DNA Mutations Can Regulate Tumor Cell Metastasis
Ishikawa, K., Takenaga, K., Akimoto, M., Koshikawa, N., Yamaguchi, A., Imanishi, H., Nakada, K., Honma, Y., & Hayashi, J.-I. (2008) · Science · doi:10.1126/science.1156906 · Cited by 1,444 · see citing works
Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling
Wood, Z. A., Poole, L. B., & Karplus, P. A. (2003) · Science · doi:10.1126/science.1080405 · Cited by 1,369 · see citing works
Sena, L. A., Li, S., Jairaman, A., Prakriya, M., Ezponda, T., Hildeman, D. A., Wang, C.-R., Schumacker, P. T., Licht, J. D., Perlman, H., et al. (2013) · Immunity · doi:10.1016/j.immuni.2012.10.020 · Cited by 1,338 · see citing works
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 1,260 · see citing works
The sites and topology of mitochondrial superoxide production
Brand, M. D. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.003 · Cited by 1,217 · see citing works
Schulz, T. J., Zarse, K., Voigt, A., Urban, N., Birringer, M., & Ristow, M. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.08.011 · Cited by 1,209 · see citing works
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208 · see citing works
Anastasiou, D., Poulogiannis, G., Asara, J. M., Boxer, M. B., Jiang, J., Shen, M., Bellinger, G., Sasaki, A. T., Locasale, J. W., Auld, D. S., et al. (2011) · Science · doi:10.1126/science.1211485 · Cited by 1,196 · see citing works
Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells
Ito, K., Hirao, A., Arai, F., Matsuoka, S., Takubo, K., Hamaguchi, I., Nomiyama, K., Hosokawa, K., Sakurada, K., Nakagata, N., et al. (2004) · Nature · doi:10.1038/nature02989 · Cited by 1,175 · see citing works
A Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122 · see citing works
Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040 · see citing works
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945 · see citing works
Peroxiredoxins are conserved markers of circadian rhythms
Edgar, R. S., Green, E. W., Zhao, Y., Gerben Van Ooijen, A., Olmedo, M., Qin, X., Xu, Y. Q., Pan, M., Valekunja, U. K., Feeney, K. A., et al. (2012) · Nature · doi:10.1038/nature11088 · Cited by 915 · see citing works
Bulua, A. C., Simon, A., Maddipati, R., Pelletier, M., Park, H., Kim, K.-Y., Sack, M. N., Kastner, D. L., & Siegel, R. M. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20102049 · Cited by 860 · see citing works
Foxo3a is essential for maintenance of the hematopoietic stem cell pool
Miyamoto, K., Kazuhito, N., & Atsushi, H. (2009) · Kanazawa University Repository for Academic Resources (DSpace) (Kanazawa University) · Cited by 858 · see citing works
Prokaryotic Regulation of Epithelial Responses by Inhibition of IκB-α Ubiquitination
Neish, A. S., Gewirtz, A. T., Zeng, H., Young, A. N., Hobert, M. E., Karmali, V., Rao, A. S., & Madara, J. (2000) · Science · doi:10.1126/science.289.5484.1560 · Cited by 843 · see citing works
A Direct Role for Dual Oxidase in Drosophila Gut Immunity
Ha, E.-M., Oh, C.-T., Bae, Y. S., & Lee, W. (2005) · Science · doi:10.1126/science.1117311 · Cited by 824 · see citing works
Redox Regulation of Forkhead Proteins Through a <i>p66shc</i> -Dependent Signaling Pathway
Nemoto, S., & Finkel, T. (2002) · Science · doi:10.1126/science.1069004 · Cited by 818 · see citing works
Self-citationLe Belle, J. E., Orozco, N. M., Paucar, A. A., Saxe, J. P., Mottahedeh, J., Pyle, A. D., Wu, H., & Kornblum, H. I. (2011) · Cell Stem Cell · doi:10.1016/j.stem.2010.11.028 · Cited by 789 · see citing works
Integration of Notch and Wnt signaling in hematopoietic stem cell maintenance
Duncan, A. W., Rattis, F. M., DiMascio, L. N., Congdon, K. L., Pazianos, G., Zhao, C., Yoon, K., Cook, J. M., Willert, K., Gaiano, N., et al. (2005) · Nature Immunology · doi:10.1038/ni1164 · Cited by 770 · see citing works
Ushio‐Fukai, M., Zafari, A. M., Fukui, T., Ishizaka, N., & Griendling, K. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23317 · Cited by 766 · see citing works
Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation
Owusu-Ansah, E., & Banerjee, U. (2009) · Nature · doi:10.1038/nature08313 · Cited by 742 · see citing works
Van Remmen, H., Ikeno, Y., Hamilton, M., Pahlavani, M., Wolf, N., Thorpe, S. R., Alderson, N. L., Baynes, J. W., Epstein, C. J., Huang, T.-T., et al. (2003) · Physiological Genomics · doi:10.1152/physiolgenomics.00122.2003 · Cited by 734 · see citing works
Xanthoudakis, S., & Curran, T. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05097.x · Cited by 708 · see citing works
Ras Proteins Induce Senescence by Altering the Intracellular Levels of Reactive Oxygen Species
Lee, A. C., Fenster, B. E., Ito, H., Takeda, K., Bae, N. S., Hirai, T., Yu, Z.-X., Ferrans, V. J., Howard, B. H., & Finkel, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7936 · Cited by 691 · see citing works
Self-citationAquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
Miller, E. W., Dickinson, B. C., & Chang, C. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005776107 · Cited by 688 · see citing works
A mutation in succinate dehydrogenase cytochrome b causes oxidative stress and ageing in nematodes.
Ishii, N., Fujii, M., Hartman, P. S., Tsuda, M., Yasuda, K., Senoo-Matsuda, N., Yanase, S., Ayusawa, D., & Suzuki, K. (1998) · Nature · doi:10.1038/29331 · Cited by 687 · see citing works
Methods for Detection of Mitochondrial and Cellular Reactive Oxygen Species
Dikalov, S., & Harrison, D. G. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4886 · Cited by 639 · see citing works
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works
Redox regulation of PI 3‐kinase signalling via inactivation of PTEN
Leslie, N. R., Bennett, D., Lindsay, Y. E., Stewart, H., Gray, A., & Downes, C. P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg513 · Cited by 614 · see citing works
Woo, H. A., Yim, S. H., Shin, D. H., Kang, D., Yu, D., & Rhee, S. G. (2010) · Cell · doi:10.1016/j.cell.2010.01.009 · Cited by 613 · see citing works
Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603 · see citing works
Reactive oxygen species are downstream mediators of p53-dependent apoptosis.
Johnson, T. M., Yu, Z., Ferrans, V. J., Lowenstein, R. A., & Finkel, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11848 · Cited by 596 · see citing works
Self-citationZhang, Y., Choksi, S., Chen, K., Pobezinskaya, E. L., Linnoila, I. R., & Liu, Z.-G. (2013) · Cell Research · doi:10.1038/cr.2013.75 · Cited by 575 · see citing works
Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling
Tal, M. C., Sasai, M., Lee, H. K., Yordy, B., Shadel, G. S., & Iwasaki, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807694106 · Cited by 573 · see citing works
Boronate-based fluorescent probes for imaging cellular hydrogen peroxide.
Miller, E. W., Albers, A. E., Pralle, A., Isacoff, E., & Chang, C. J. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054474f · Cited by 530 · see citing works
Lo, Y. Y. C., & Cruz, T. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11727 · Cited by 530 · see citing works
Regulation of reactive-oxygen-species generation in fibroblasts by Rac 1
Sundaresan, M., Yu, Z., Ferrans, V. J., Sulciner, D. J., Gutkind, J. S., Irani, K., Goldschmidt‐Clermont, P. J., & Finkel, T. (1996) · Biochemical Journal · doi:10.1042/bj3180379 · Cited by 486 · see citing works
Self-citationBmi1 regulates mitochondrial function and the DNA damage response pathway
Liu, J., Cao, L., Chen, J., Song, S., Lee, I. H., Quijano, C., Liu, H., Keyvanfar, K., Chen, H., Cao, L.-Y., et al. (2009) · Nature · doi:10.1038/nature08040 · Cited by 474 · see citing works
Self-citationPeroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity
Paulsen, C. E., Truong, T. H., García, F., Homann, A., Gupta, V., Leonard, S. E., & Carroll, K. S. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.736 · Cited by 473 · see citing works
Regulation of ROS signal transduction by NADPH oxidase 4 localization
Chen, K., Kirber, M. T., Xiao, H. Q., Yang, Y., & Keaney, J. F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709049 · Cited by 468 · see citing works
Molecular imaging of hydrogen peroxide produced for cell signaling
Miller, E. W., Tulyathan, O., Isacoff, E. Y., & Chang, C. J. (2007) · Nature Chemical Biology · doi:10.1038/nchembio871 · Cited by 450 · see citing works
Zarse, K., Schmeisser, S., Groth, M., Priebe, S., Beuster, G., Kuhlow, D., Guthke, R., Platzer, M., Kahn, C. R., & Ristow, M. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.02.013 · Cited by 430 · see citing works
Jones, R. M., Luo, L., Ardita, C., Richardson, A. N., Kwon, Y. M., Mercante, J. W., Alam, A. M., Gates, C. L., Wu, H., Swanson, P. A., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.224 · Cited by 393 · see citing works
Role for mitochondrial oxidants as regulators of cellular metabolism
Nemoto, S., Takeda, K., Yu, Z.-X., Ferrans, V. J., & Finkel, T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7311-7318.2000 · Cited by 393 · see citing works
Self-citationFunato, Y., Michiue, T., Asashima, M., & Miki, H. (2006) · Nature Cell Biology · doi:10.1038/ncb1405 · Cited by 378 · see citing works
Modulation of intracellular ROS levels by TIGAR controls autophagy
Bensaad, K., Cheung, E. C., & Vousden, K. H. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.242 · Cited by 361 · see citing works
Atg7 Modulates p53 Activity to Regulate Cell Cycle and Survival During Metabolic Stress
Lee, I. H., Kawai, Y., Fergusson, M. M., Rovira, I. I., Bishop, A. J. R., Motoyama, N., Cao, L., & Finkel, T. (2012) · Science · doi:10.1126/science.1218395 · Cited by 357 · see citing works
Self-citationOxidants, antioxidants and the current incurability of metastatic cancers
Watson, J. (2013) · Open Biology · doi:10.1098/rsob.120144 · Cited by 355 · see citing works
Liu, X., Jiang, N., Hughes, B., Bigras, E., Shoubridge, E., & Hekimi, S. (2005) · Genes & Development · doi:10.1101/gad.1352905 · Cited by 345 · see citing works
Protective Coupling of Mitochondrial Function and Protein Synthesis via the eIF2α Kinase GCN-2
Baker, B. M., Nargund, A. M., Sun, T., & Haynes, C. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002760 · Cited by 326 · see citing works
Hamanaka, R. B., Glasauer, A., Hoover, P., Yang, S., Blatt, H., Mullen, A. R., Getsios, S., Gottardi, C. J., DeBerardinis, R. J., Lavker, R. M., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2003638 · Cited by 315 · see citing works
Regulation of Yeast Chronological Life Span by TORC1 via Adaptive Mitochondrial ROS Signaling
Pan, Y., Schroeder, E. A., Ocampo, A., Barrientos, A., & Shadel, G. S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.018 · Cited by 313 · see citing works
Cochemé, H. M., Quin, C., McQuaker, S. J., Cabreiro, F., Logan, A., Prime, T. A., Abakumova, I., Patel, J. V., Fearnley, I. M., James, A. M., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.003 · Cited by 313 · see citing works
SIRT3 regulation of mitochondrial oxidative stress
Bause, A. S., & Haigis, M. C. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.007 · Cited by 311 · see citing works
Beckman, K. B., & Ames, B. N. (2000) · Elsevier eBooks · doi:10.1016/b978-044482650-3/50027-4 · Cited by 307 · see citing works
Measuring EGSH and H2O2 with roGFP2-based redox probes
Morgan, B., Sobotta, M. C., & Dick, T. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.035 · Cited by 295 · see citing works
Regulation of reactive oxygen species in stem cells and cancer stem cells
Kobayashi, C. I., & Suda, T. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22764 · Cited by 290 · see citing works
Lee, C., Lee, S. M., Mukhopadhyay, P., Kim, S. J., Lee, S. C., Ahn, W.-S., Yu, M., Storz, G., & Ryu, S. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb856 · Cited by 281 · see citing works
Nox2 redox signaling maintains essential cell populations in the brain
Dickinson, B. C., Peltier, J., Stone, D., Schaffer, D. V., & Chang, C. J. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.497 · Cited by 273 · see citing works
Commensal bacteria modulate cullin‐dependent signaling via generation of reactive oxygen species
Kumar, A., Wu, H., Collier-Hyams, L. S., Hansen, J. M., Li, T., Yamoah, K., Pan, Z., Jones, D. P., & Neish, A. S. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601867 · Cited by 264 · see citing works
Zhang, J., Kim, J., Alexander, A., Cai, S., Tripathi, D. N., Dere, R., Tee, A. R., Tait-Mulder, J., Di Nardo, A., Han, J. M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2822 · Cited by 258 · see citing works
ROS Are Required for Mouse Spermatogonial Stem Cell Self-Renewal
Morimoto, H., Iwata, K., Ogonuki, N., Inoue, K., Ogura, A., Kanatsu‐Shinohara, M., Morimoto, T., Yabe‐Nishimura, C., & Shinohara, T. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.04.001 · Cited by 246 · see citing works
Lee, B. C., Péterfi, Z., Hoffmann, F. W., Moore, R. E., Kaya, A., Avanesov, A. S., Tarrago, L., Zhou, Y., Weerapana, E., Fomenko, D. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.019 · Cited by 244 · see citing works
SOD1 Integrates Signals from Oxygen and Glucose to Repress Respiration
Reddi, A. R., & Culotta, V. (2013) · Cell · doi:10.1016/j.cell.2012.11.046 · Cited by 225 · see citing works
Prdm16 promotes stem cell maintenance in multiple tissues, partly by regulating oxidative stress
Chuikov, S., Levi, B. P., Smith, M. L., & Morrison, S. J. (2010) · Nature Cell Biology · doi:10.1038/ncb2101 · Cited by 224 · see citing works
p53, ROS and senescence in the control of aging
Vigneron, A., & Vousden, K. H. (2010) · Aging · doi:10.18632/aging.100189 · Cited by 221 · see citing works
Savitsky, P. A., & Finkel, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201589200 · Cited by 218 · see citing works
Self-citationEarly Mitochondrial Dysfunction in Long-lived Mclk1+/- Mice
Lapointe, J., & Hekimi, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803287200 · Cited by 207 · see citing works
Redox Regulation of Epidermal Growth Factor Receptor Signaling through Cysteine Oxidation
Truong, T. H., & Carroll, K. S. (2012) · Biochemistry · doi:10.1021/bi301441e · Cited by 198 · see citing works
The physiological role of reversible methionine oxidation
Drazic, A., & Winter, J. (2014) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2014.01.001 · Cited by 198 · see citing works
Coant, N., Mkaddem, S. B., Pédruzzi, E., Guichard, C., Tréton, X., Ducroc, R. A., Freund, J., Cazals-Hatem, D. L., Bouhnik, Y., Woerther, P., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01194-09 · Cited by 191 · see citing works
Epigenetic silencing mediates mitochondria stress-induced longevity
Schroeder, E. A., Raimundo, N., & Shadel, G. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.003 · Cited by 186 · see citing works
Kil, I. S., Lee, S. K., Ryu, K. W., Woo, H. A., Hu, M., Bae, S. H., & Rhee, S. G. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.030 · Cited by 184 · see citing works
Li, T., & Marbán, E. (2010) · Stem Cells · doi:10.1002/stem.438 · Cited by 171 · see citing works
Yang, W., Li, J., & Hekimi, S. (2007) · Genetics · doi:10.1534/genetics.107.080788 · Cited by 171 · see citing works
Redox regulation of stem/progenitor cells and bone marrow niche
Urao, N., & Ushio‐Fukai, M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.532 · Cited by 168 · see citing works
Redox-Dependent Control of FOXO/DAF-16 by Transportin-1
Putker, M., Madl, T., Vos, H. R., de Ruiter, H., Visscher, M., van den Berg, M. C. W., Kaplan, M., Korswagen, H. C., Boelens, R., Vermeulen, M., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.014 · Cited by 163 · see citing works
Deubiquitinases as a Signaling Target of Oxidative Stress
Cotto-Rios, X. M., Békés, M., Chapman, J. R., Ueberheide, B. M., & Huang, T. T. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.11.011 · Cited by 161 · see citing works
Nox enzymes from fungus to fly to fish and what they tell us about Nox function in mammals
Aguirre, J., & Lambeth, J. D. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.07.027 · Cited by 158 · see citing works
SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics
Hung, R., Spaeth, C. S., Yesilyurt, H. G., & Terman, J. R. (2013) · Nature Cell Biology · doi:10.1038/ncb2871 · Cited by 149 · see citing works
Pk, J. (1966) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/0926-6593(66)90057-9 · Cited by 147 · see citing works
Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells
Lee, J., Baek, K., Soetandyo, N., & Ye, Y. (2013) · Nature Communications · doi:10.1038/ncomms2532 · Cited by 147 · see citing works
Chatoo, W., Abdouh, M., David, J., Champagne, M.-P., Ferreira, J., Rodier, F., & Bernier, G. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.5303-08.2009 · Cited by 146 · see citing works
Abbas, H. A., Macció, D. R., Coşkun, S., Jackson, J. G., Hazen, A. L., Sills, T., You, M. J., Hirschi, K. K., & Lozano, G. (2010) · Cell stem cell · doi:10.1016/j.stem.2010.09.013 · Cited by 141 · see citing works
Regulation of A20 and other OTU deubiquitinases by reversible oxidation
Kulathu, Y., García, F., Mevissen, T. E. T., Busch, M., Arnaudo, N., Carroll, K. S., Barford, D., & Komander, D. (2013) · Nature Communications · doi:10.1038/ncomms2567 · Cited by 136 · see citing works
Forkhead Box O as a Sensor, Mediator, and Regulator of Redox Signaling
de Keizer, P. L. J., Burgering, B. M. T., & Dansen, T. B. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3403 · Cited by 131 · see citing works
Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression
Jeong, W., Bae, S. H., Tolédano, M. B., & Rhee, S. G. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.020 · Cited by 129 · see citing works
Autophagy, Stress, and Cancer Metabolism: What Doesn't Kill You Makes You StrongerPreprint
Mathew, R., & White, E. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2012.76.011015 · Cited by 123 · see citing works
Mitochondrial proticity and ROS signaling: lessons from the uncoupling proteins
Mailloux, R. J., & Harper, M. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.04.004 · Cited by 122 · see citing works
A crucial role for Nox 1 in redox‐dependent regulation of Wnt‐β‐catenin signaling
Seheli, K., Mondol, A. S., Nagasawa, A., Zhang, Y., Kato, M., Matsuno, K., Yabe‐Nishimura, C., & Kamata, T. (2012) · The FASEB Journal · doi:10.1096/fj.11-196360 · Cited by 109 · see citing works
Mutation of the Cyba gene encoding p22phox causes vestibular and immune defects in mice
Nakano, Y., Longo-Guess, C. M., Bergstrom, D. E., Nauseef, W. M., Jones, S. M., & Bánfi, B. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33835 · Cited by 108 · see citing works
Pk, J. (1966) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/0926-6593(66)90058-0 · Cited by 74 · see citing works
Regulation of Protein Tyrosine Phosphatase Oxidation in Cell Adhesion and Migration
Frijhoff, J., Dagnell, M., Godfrey, R., & Östman, A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5643 · Cited by 66 · see citing works
Bacterial-modulated host immunity and stem cell activation for gut homeostasis: Figure 1.Preprint
Lee, W. (2009) · Genes & Development · doi:10.1101/gad.1858709 · Cited by 55 · see citing works
Chapter 8 Monitoring Starvation‐Induced Reactive Oxygen Species Formation
Scherz‐Shouval, R., & Elazar, Z. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)03608-2 · Cited by 24 · see citing works
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Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works
Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654 · see citing works
Oxidative stress and autophagy: The clash between damage and metabolic needs
Filomeni, G., De Zio, D., & Cecconi, F. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.150 · Cited by 2,195 · see citing works
ROS in cancer therapy: the bright side of the moon
Perillo, B., Di Donato, M., Pezone, A., Di Zazzo, E., Giovannelli, P., Galasso, G., Castoria, G., & Migliaccio, A. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0384-2 · Cited by 2,176 · see citing works
Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148 · see citing works
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Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750 · see citing works
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
Sies, H., Belousov, V. V., Chandel, N. S., Davies, M. J., Jones, D. P., Mann, G. E., Murphy, M. P., Yamamoto, M., & Winterbourn, C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00456-z · Cited by 1,735 · see citing works
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Rojo de la Vega, M., Chapman, E., & Zhang, D. D. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.022 · Cited by 1,672 · see citing works
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Görlach, A., Bertram, K., Hudecova, S., & Krizanova, O. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.010 · Cited by 1,546 · see citing works
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Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063 · see citing works
Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives
Hajam, Y. A., Rani, R., Ganie, S. Y., Sheikh, T. A., Javaid, D., Qadri, S. S., Pramodh, S., Alsulimani, A., Alkhanani, M. F., Harakeh, S., et al. (2022) · Cells · doi:10.3390/cells11030552 · Cited by 915 · see citing works
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Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723 · see citing works
Reactive oxygen species (ROS) in macrophage activation and function in diabetes
Rendra, E., Riabov, V., Mossel, D. M., Sevastyanova, T., Harmsen, M. C., & Kzhyshkowska, J. (2019) · Immunobiology · doi:10.1016/j.imbio.2018.11.010 · Cited by 636 · see citing works
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Eisner, V., Picard, M., & Hajnóczky, G. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0133-0 · Cited by 622 · see citing works
Tan, H.-Y., Wang, N., Li, S., Hong, M., Wang, X., & Feng, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2795090 · Cited by 657 · see citing works
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Vaccaro, A., Kaplan Dor, Y., Nambara, K., Pollina, E. A., Lin, C., Greenberg, M. E., & Rogulja, D. (2020) · Cell · doi:10.1016/j.cell.2020.04.049 · Cited by 541 · see citing works
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“This will lead to the formation of unstable sulfenic acid intermediates that are subsequently reduced to a disulfide bond by reaction with glutathione or inter- or intramolecular protein thiols [119].”
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Yang, Z., Shen, Y., Oishi, H., Matteson, E. L., Tian, L., Goronzy, J. J., & Weyand, C. M. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad7151 · Cited by 275 · see citing works
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Abuaita, B. H., Schultz, T. L., & O’Riordan, M. X. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.10.005 · Cited by 223 · see citing works
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Niki, E. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.11.017 · Cited by 209 · see citing works
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Haslund‐Vinding, J., McBean, G., Jaquet, V, & Vilhardt, F. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13425 · Cited by 169 · see citing works
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Nakayama, H., & Otsu, K. (2018) · Biochemical Journal · doi:10.1042/bcj20170714 · Cited by 160 · see citing works
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Liao, N., Shi, Y., Zhang, C., Zheng, Y., Wang, Y., Zhao, B., Zeng, Y., Liu, X., & Liu, J. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1404-9 · Cited by 127 · see citing works
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Herb, M., Gluschko, A., Wiegmann, K., Farid, A., Wolf, A., Utermöhlen, O., Krut, O., Krönke, M., & Schramm, M. (2019) · Science Signaling · doi:10.1126/scisignal.aar5926 · Cited by 119 · see citing works
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Wlaschek, M., Singh, K., Sindrilaru, A., Crisan, D., & Scharffetter-Kochanek, K. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.036 · Cited by 76 · see citing works
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Halliwell, B. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.10.010 · Cited by 75 · see citing works
Sadowska, M., Narbutt, J., & Lesiak, A. (2021) · Life · doi:10.3390/life11070670 · Cited by 74 · see citing works
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Gambardella, J., De Rosa, M., Sorriento, D., Prevete, N., Fiordelisi, A., Ciccarelli, M., Trimarco, B., De Luca, N., & Iaccarino, G. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/9582319 · Cited by 58 · see citing works
Stagni, V., Cirotti, C., & Barilà, D. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00073 · Cited by 52 · see citing works
MicroRNAs, Long Non-Coding RNAs, and Circular RNAs in the Redox Control of Cell Senescence
Lettieri-Barbato, D., Aquilano, K., Punziano, C., Minopoli, G., & Faraonio, R. (2022) · Antioxidants · doi:10.3390/antiox11030480 · Cited by 51 · see citing works
Leu, J. I.-J., Murphy, M. E., & George, D. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009943117 · Cited by 47 · see citing works
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. (2020) · Angewandte Chemie · doi:10.1002/ange.201906793 · Cited by 45 · see citing works
Cobley, J. N., Margaritelis, N. V., Morton, J. P., Close, G. L., Nikolaidis, M. G., & Malone, J. K. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00182 · Cited by 43 · see citing works
Liu, B., Hutchison, A. T., Thompson, C. H., Lange, K., Wittert, G. A., & Heilbronn, L. K. (2021) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaa707 · Cited by 39 · see citing works
Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A
Göbl, C., Morris, V. K., van Dam, L., Visscher, M., Polderman, P. E., Hartlmüller, C., de Ruiter, H., Hora, M., Liesinger, L., Birner-Gruenberger, R., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101316 · Cited by 29 · see citing works
Foti, A., Dorendorf, F., & Leimkühler, S. (2017) · PLOS ONE · doi:10.1371/journal.pone.0182061 · Cited by 26 · see citing works
Chang, W., Weaver, C., Medalla, M., Moore, T., & Luebke, J. (2022) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.09.012 · Cited by 20 · see citing works
Nrf2 signaling pathway: focus on oxidative stress in osteoporosis
Gu, H.-Y., Liu, N., Lin, F.-X., & Yin, J. (2025) · Osteoporosis International · doi:10.1007/s00198-025-07592-0 · Cited by 10 · see citing works
Not aging but calorie restriction strongly affects protein oxidation in heart and brain mitochondria
Fan, S., Ramallo‐Guevara, C., Frenzel, M., Yanai, S., Goto, S., Sugawa, M. D., Dencher, N. A., & Poetsch, A. (2026) · Aging Cell · doi:10.1111/acel.70339 · Cited by 1 · see citing works
- Authors
- Holmström, K. M., & Finkel, T.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Finkel, Toren
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2014-05-23
- Volume
- 15
- Issue
- 6
- Pages
- 411-421
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2007636933
- Cited by
- 2,093
- References
- 121
- Citations by year
- 2026: 128 · 2025: 154 · 2024: 192 · 2023: 175 · 2022: 174 · 2021: 212 · 2020: 195 · 2019: 163 · 2018: 207 · 2017: 192 · 2016: 152 · 2015: 114 · 2014: 32
- FWCI
- 15.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fondation Leducq
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- reactive oxygen species, redox signaling, cysteine oxidation, protein oxidation, signal transduction, innate immunity, stem cell self-renewal, carcinogenesis, aging, metabolic regulation
- MeSH terms
- Aging, Animals, Cell Physiological Phenomena, Humans, Neoplasms, 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 ›
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