ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
Abstract
Reactive oxygen species (ROS) have been shown to be toxic but also function as signalling molecules. This biological paradox underlies mechanisms that are important for the integrity and fitness of living organisms and their ageing. The pathways that regulate ROS homeostasis are crucial for mitigating the toxicity of ROS and provide strong evidence about specificity in ROS signalling. By taking advantage of the chemistry of ROS, highly specific mechanisms have evolved that form the basis of oxidant scavenging and ROS signalling systems.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Superoxide's anionic charge limits its reactivity to compounds with electron-rich centres.
“Its anionic charge which limits its reactivity to compounds with electron-rich centres [63].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [63]
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 · see citing works
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990 · see citing works
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634 · see citing works
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 · see citing works
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 · see citing works
St-Pierre, J., Drori, S., Uldry, M., Silvaggi, J. M., Rhee, J., Jäger, S., Handschin, C., Zheng, K., Lin, J., Yang, W., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.024 · Cited by 2,233 · see citing works
Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224 · see citing works
Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,206 · see citing works
Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947 · 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
Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480 · see citing works
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393 · 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
Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex
Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,262 · 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
Activation of the OxyR Transcription Factor by Reversible Disulfide Bond Formation
Zheng, M., Åslund, F., & Storz, G. (1998) · Science · doi:10.1126/science.279.5357.1718 · Cited by 1,197 · see citing works
The antioxidant function of the p53 tumor suppressor
Sablina, A. A., Budanov, A. V., Ilyinskaya, G. V., Agapova, L. S., Kravchenko, J. E., & Chumakov, P. M. (2005) · Nature Medicine · doi:10.1038/nm1320 · Cited by 1,110 · see citing works
Membrane transport of hydrogen peroxide
Bienert, G. P., Schjoerring, J. K., & Jahn, T. P. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.02.015 · Cited by 1,079 · see citing works
Cullinan, S. B., Gordan, J. D., Jin, J., Harper, J. W., & Diehl, J. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8477-8486.2004 · Cited by 986 · see citing works
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
Biteau, B., Labarre, J., & Tolédano, M. B. (2003) · Nature · doi:10.1038/nature02075 · Cited by 970 · see citing works
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951 · see citing works
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945 · see citing works
A Thiol Peroxidase Is an H2O2 Receptor and Redox-Transducer in Gene Activation
Delaunay, A., Pflieger, D., Barrault, M., Vinh, J., & Tolédano, M. B. (2002) · Cell · doi:10.1016/s0092-8674(02)01048-6 · Cited by 902 · see citing works
Keap1-null mutation leads to postnatal lethality due to constitutive Nrf2 activation
Wakabayashi, N., Itoh, K., Wakabayashi, J., Motohashi, H., Noda, S., Takahashi, S., Imakado, S., KOTSUJI, T., Otsuka, F., Roop, D. R., et al. (2003) · Nature Genetics · doi:10.1038/ng1248 · Cited by 881 · see citing works
Kobayashi, M., & Yamamoto, M. P. (2006) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.01.007 · Cited by 855 · see citing works
A Conserved MST-FOXO Signaling Pathway Mediates Oxidative-Stress Responses and Extends Life Span
Lehtinen, M. K., Yuan, Z., Boag, P. R., Yang, Y., Villén, J., Becker, E. B. E., DiBacco, S., de la Iglesia, N., Gygi, S. P., Blackwell, T. K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.046 · Cited by 842 · see citing works
Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
Winterbourn, C. C., & Metodiewa, D. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00051-9 · Cited by 799 · see citing works
FOXO transcription factor activation by oxidative stress mediated by the small GTPase Ral and JNK
Essers, M. A., Weijzen, S., de Vries‐Smits, A. M., Saarloos, I., de Ruiter, N. D., Bos, J. L., & Burgering, B. M. T. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600476 · Cited by 798 · see citing works
Seaver, L. C., & Imlay, J. A. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.24.7173-7181.2001 · Cited by 797 · see citing works
Molecular and Cellular Aspects of Thiol–Disulfide Exchange
Gilbert, H. (1990) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123096.ch2 · Cited by 759 · see citing works
Tong, K. I., Katoh, Y., Kusunoki, H., Itoh, K., Tanaka, T., & Yamamoto, M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.8.2887-2900.2006 · Cited by 759 · cited 3× · see citing works
“Zinc coordination by Cys residues in KeaP1 is reminiscent of Hsp33 and Rsra, suggesting that, in a similar way to 103,131 .”
BackgroundFurukawa, M., & Xiong, Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.162-171.2005 · Cited by 746 · see citing works
Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer
Padmanabhan, B., Tong, K. I., Ohta, T., Nakamura, Y., Scharlock, M., Ohtsuji, M., Kang, M.-I., Kobayashi, A., Yokoyama, S., & Yamamoto, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.013 · Cited by 735 · see citing works
Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD
Budanov, A. V., Sablina, A. A., Feinstein, E., Koonin, E. V., & Chumakov, P. M. (2004) · Science · doi:10.1126/science.1095569 · Cited by 731 · see citing works
Redox Redux: Revisiting PTPs and the Control of Cell Signaling
Tonks, N. K. (2005) · Cell · doi:10.1016/j.cell.2005.05.016 · Cited by 702 · see citing works
Novel domains of the prokaryotic two-component signal transduction systems
Galperin, M. Y., Nikolskaya, A. N., & Koonin, E. V. (2001) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2001.tb10814.x · Cited by 652 · see citing works
Cell cycle and death control: long live Forkheads
Burgering, B. M. T., & Kops, G. J. P. L. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02113-8 · Cited by 648 · see citing works
Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
van Montfort, R. L. M., Congreve, M., Tisi, D., Carr, R. A. E., & Jhoti, H. (2003) · Nature · doi:10.1038/nature01681 · Cited by 642 · see citing works
Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling
Lo, S., Li, X., Henzl, M. T., Beamer, L. J., & Hannink, M. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601243 · Cited by 604 · see citing works
Protein Sulfenic Acids in Redox Signaling
Poole, L. B., Karplus, P. A., & Claiborne, A. (2004) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.44.101802.121735 · Cited by 598 · see citing works
Åslund, F., Zheng, M., Beckwith, J., & Storz, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6161 · Cited by 586 · see citing works
cell cycle and death control: long live Forkheads
Burgering, B. M. T., Medema, R. H., & Kops, G. J. P. L. (2002) · GBM Annual Fall meeting Halle 2002 · doi:10.1240/sav_gbm_2002_h_000075 · Cited by 586 · see citing works
Structural Basis of the Redox Switch in the OxyR Transcription Factor
Choi, H., Kim, S.-J., Mukhopadhyay, P., Cho, S., Woo, J.-R., Storz, G., & Ryu, S.-E. (2001) · Cell · doi:10.1016/s0092-8674(01)00300-2 · Cited by 560 · see citing works
Levonen, A., Landar, A. L., Ramachandran, A., CEASER, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., & Darley-Usmar, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031049 · Cited by 559 · see citing works
Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation
Woo, H. A., Chae, H. Z., Hwang, S. C., Yang, K., Kang, S. W., Kim, K., & Rhee, S. G. (2003) · Science · doi:10.1126/science.1080273 · Cited by 558 · see citing works
Miao, Y., Lv, D., Wang, P., Wang, X., Chen, J., Miao, C., & Song, C. (2006) · The Plant Cell · doi:10.1105/tpc.106.044230 · Cited by 555 · see citing works
The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
Lee, J.-W., & Helmann, J. D. (2006) · Nature · doi:10.1038/nature04537 · Cited by 547 · see citing works
FOXO4 Is Acetylated upon Peroxide Stress and Deacetylated by the Longevity Protein hSir2
van der Horst, A., Tertoolen, L. G. J., Smits, L. M. M., Frye, R. A., Medema, R. H., & Burgering, B. M. T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401138200 · Cited by 541 · see citing works
H2O2 sensing through oxidation of the Yap1 transcription factor
Delaunay, A., Isnard, A., & Tolédano, M. B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.19.5157 · Cited by 529 · see citing works
Iron Metabolism and the IRE/IRP Regulatory System: An Update
Pantopoulos, K. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.001 · Cited by 505 · see citing works
Kim, S. O., Merchant, K., Nudelman, R., Beyer, W. F., Keng, T., DeAngelo, J. D., Hausladen, A., & Stamler, J. S. (2002) · Cell · doi:10.1016/s0092-8674(02)00723-7 · Cited by 481 · see citing works
Eggler, A. L., Liu, G., Pezzuto, J. M., van Breemen, R. B., & Mesecar, A. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502402102 · Cited by 459 · see citing works
Yang, K.-S., Kang, S. W., Woo, H. A., Hwang, S. C., Chae, H. Z., Kim, K., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206626200 · Cited by 458 · see citing works
Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling
Nathan, C. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200318174 · Cited by 455 · 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
Schwartz, C. J., Giel, J. L., Patschkowski, T., Luther, C., Ruzicka, F. J., Beinert, H., & Kiley, P. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251550898 · Cited by 442 · see citing works
Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
Choi, M. H., Lee, I. K., Kim, G. W., Kim, B. U., Han, Y.-H., Yu, D.-Y., Park, H. S., Kim, K. Y., Lee, J. S., Choi, C., et al. (2005) · Nature · doi:10.1038/nature03587 · Cited by 403 · see citing works
Proteomics Analysis of Cellular Response to Oxidative Stress
Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106585200 · Cited by 393 · see citing works
Tolédano, M. B., Kullik, I., Trinh, F., Baird, P. T., Schneider, T. D., & Storz, G. (1994) · Cell · doi:10.1016/s0092-8674(94)90702-1 · Cited by 389 · see citing works
Chang, T.-S., Cho, C.-S., Park, S., Yu, S., Kang, S. W., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407707200 · Cited by 388 · see citing works
Localizing NADPH Oxidase–Derived ROS
Ushio‐Fukai, M. (2006) · Science s STKE · doi:10.1126/stke.3492006re8 · Cited by 387 · see citing works
The Role of Keap1 in Cellular Protective Responses
Dinkova‐Kostova, A. T., Holtzclaw, W. D., & Kensler, T. W. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050217c · Cited by 378 · see citing works
Nitrosative Stress: Activation of the Transcription Factor OxyR
Hausladen, A., Privalle, C. T., Keng, T., DeAngelo, J., & Stamler, J. S. (1996) · Cell · doi:10.1016/s0092-8674(00)80147-6 · Cited by 359 · see citing works
Cellular Regulation by Hydrogen Peroxide
Rhee, S. G., Chang, T.-S., Bae, Y. S., Lee, S.-R., & Kang, S. W. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000077404.45564.7e · Cited by 348 · see citing works
Khoroshilova, N., Popescu, C. V., Münck, E., Beinert, H., & Kiley, P. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6087 · Cited by 346 · see citing works
An iron‐sulfur center essential for transcriptional activation by the redox‐sensing SoxR protein.
Hidalgo, E., & Demple, B. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06243.x · Cited by 341 · see citing works
Nguyen, T., Sherratt, P. J., Nioi, P., Yang, C. S., & Pickett, C. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503074200 · Cited by 341 · see citing works
Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses
Gilles‐Gonzalez, M., & GONZALEZ, G. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.11.006 · Cited by 328 · see citing works
Åslund, F., & Beckwith, J. (1999) · Cell · doi:10.1016/s0092-8674(00)80584-x · Cited by 298 · see citing works
Regulation of inducible peroxide stress responses
Mongkolsuk, S., & Helmann, J. D. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03015.x · Cited by 293 · 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
Gao, L., Wang, J., Sekhar, K. R., Yin, H., Yared, N. F., Schneider, S. N., Sasi, S., Dalton, T. P., Anderson, M. E., Chan, J. Y., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607622200 · Cited by 278 · see citing works
Zinc and Sulfur: A Critical Biological Partnership
Maret, W. (2004) · Biochemistry · doi:10.1021/bi036340p · Cited by 270 · see citing works
ReviewRegulation of protein function by glutathionylation
Ghezzi, P. (2005) · Free Radical Research · doi:10.1080/10715760500072172 · Cited by 270 · see citing works
Conrad, M., Moreno, S. G., Sinowatz, F., Ursini, F., Kölle, S., Roveri, A., Brielmeier, M., Wurst, W., Maiorino, M., & Bornkamm, G. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.17.7637-7644.2005 · Cited by 270 · see citing works
Yeast signaling pathways in the oxidative stress response
Ikner, A., & Shiozaki, K. (2004) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2004.09.006 · Cited by 267 · see citing works
Crm1p mediates regulated nuclear export of a yeast AP‐1‐like transcription factor
Yan, C. T., Lee, L. H., & Davis, L. I. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7416 · Cited by 264 · see citing works
A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR
Lee, J., Soonsanga, S., & Helmann, J. D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702081104 · Cited by 244 · see citing works
Regulation of Peroxiredoxin I Activity by Cdc2-mediated Phosphorylation
Chang, T., Jeong, W., Choi, S. Y., Yu, S. J., Kang, S. W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110432200 · Cited by 244 · see citing works
A cysteine-sulfinic acid in peroxiredoxin regulates H 2 O 2 -sensing by the antioxidant Pap1 pathway
Vivancos, A. P., Castillo, E. A., Biteau, B., Nicot, C., Ayté, J., Tolédano, M. B., & Hidalgo, E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503251102 · Cited by 244 · see citing works
RsrA, an anti‐sigma factor regulated by redox change
Kang, J., Paget, M. S. B., Seok, Y., Hahn, M., Bae, J., Hahn, J., Kleanthous, C., Buttner, M. J., & Roe, J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.15.4292 · Cited by 239 · see citing works
Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon.
Liochev, S. I., & Fridovich, I. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.5892 · Cited by 237 · see citing works
Velichkova, M., & Hasson, T. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.11.4501-4513.2005 · Cited by 237 · see citing works
Structure of an OhrR-ohrA Operator Complex Reveals the DNA Binding Mechanism of the MarR Family
Hong, M., Fuangthong, M., Helmann, J. D., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.013 · Cited by 236 · see citing works
Helmann, J. D., Wu, M. F. W., Gaballa, A., Kobel, P. A., Morshedi, M. M., Fawcett, P., & Paddon, C. J. (2002) · Journal of Bacteriology · doi:10.1128/jb.185.1.243-253.2003 · Cited by 232 · see citing works
Fuangthong, M., & Helmann, J. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.102483199 · Cited by 231 · see citing works
Li, Q., Harraz, M. M., Zhou, W., Zhang, L. N., Ding, W., Zhang, Y., Eggleston, T., Yeaman, C. A., Bánfi, B., & Engelhardt, J. F. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.140-154.2006 · Cited by 230 · see citing works
Herbig, A. F., & Helmann, J. D. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02543.x · Cited by 224 · see citing works
Yeo, W., Lee, J., Lee, K., & Roe, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05220.x · Cited by 218 · see citing works
Veal, E. A., Findlay, V. J., Day, A. M., Bozonet, S. M., Evans, J. M., Quinn, J., & Morgan, B. A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.021 · Cited by 215 · see citing works
An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus
Chen, P. R., Bae, T., Williams, W. A., Duguid, E. M., Rice, P. A., Schneewind, O., & He, C. (2006) · Nature Chemical Biology · doi:10.1038/nchembio820 · Cited by 213 · see citing works
Fuangthong, M., Atichartpongkul, S., Mongkolsuk, S., & Helmann, J. D. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.14.4134-4141.2001 · Cited by 212 · see citing works
Mukhopadhyay, P., Zheng, M., Bedzyk, L. A., LaRossa, R. A., & Storz, G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307741100 · Cited by 210 · see citing works
Quinn, J., Findlay, V. J., Dawson, K., Millar, J. B. A., Jones, N., Morgan, B. A., & Toone, W. M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-06-0288 · Cited by 209 · see citing works
c-Myc Phosphorylation Is Required for Cellular Response to Oxidative Stress
Benassi, B., Fanciulli, M., Fiorentino, F., Porrello, A., Chiorino, G., Loda, M. F., Zupi, G., & Biroccio, A. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.009 · Cited by 207 · see citing works
A reducing system of the superoxide sensor SoxR in Escherichia coli
Koo, M., Lee, J., Rah, S., Yeo, W., Lee, J., Lee, K., Koh, Y., Kang, S., & Roe, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg252 · Cited by 206 · see citing works
Parsonage, D., Youngblood, D. S., Sarma, G. N., Wood, Z. A., Karplus, P. A., & Poole, L. B. (2005) · Biochemistry · doi:10.1021/bi050448i · Cited by 201 · see citing works
Redox Switch of Hsp33 Has a Novel Zinc-binding Motif
Jakob, U., Eser, M., & Bardwell, J. C. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005957200 · Cited by 193 · see citing works
Winter, J., Linke, K., Jatzek, A., & Jakob, U. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.027 · Cited by 186 · see citing works
Catalase Activity Is Regulated by c-Abl and Arg in the Oxidative Stress Response
Cao, C., Leng, Y., & Kufe, D. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301292200 · Cited by 186 · see citing works
Structural basis for redox regulation of Yap1 transcription factor localization
Wood, M. J. A., Storz, G., & Tjandra, N. (2004) · Nature · doi:10.1038/nature02790 · Cited by 177 · see citing works
The phagocyte NADPH oxidase depends on cholesterol‐enriched membrane microdomains for assembly
Vilhardt, F., & van Deurs, B. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600066 · Cited by 171 · see citing works
The Saccharomyces cerevisiae Proteome of Oxidized Protein Thiols
Le Moan, N., Clement, G., Le Maout, S., Tacnet, F., & Toledano, M. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513346200 · Cited by 170 · see citing works
Kuge, S., Toda, T., Iizuka, N., & Nomoto, A. (1998) · Genes to Cells · doi:10.1046/j.1365-2443.1998.00209.x · Cited by 166 · see citing works
Catalytic Mechanism of Thiol Peroxidase from Escherichia coli
Baker, L. M. S., & Poole, L. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209888200 · Cited by 165 · see citing works
Peroxide Sensors for the Fission Yeast Stress-activated Mitogen-activated Protein Kinase Pathway
Buck, V., Quinn, J., Soto, T., Martı́n, H., Saldanha, J. W., Makino, K., Morgan, B. A., & Millar, J. B. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.2.407 · Cited by 164 · see citing works
Axis determination by inhibition of Wnt signaling in XenopusPreprint
Itoh, K., & Sokol, S. Y. (1999) · Genes & Development · doi:10.1101/gad.13.17.2328 · Cited by 163 · see citing works
Bozonet, S. M., Findlay, V. J., Day, A. M., Cameron, J., Veal, E. A., & Morgan, B. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502757200 · Cited by 162 · see citing works
Nguyen, A. N., Lee, A., Place, W. R., & Shiozaki, K. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.4.1169 · Cited by 162 · see citing works
Ybp1 Is Required for the Hydrogen Peroxide-induced Oxidation of the Yap1 Transcription Factor
Veal, E. A., Ross, S. J., Malakasi, P., Peacock, E., & Morgan, B. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303542200 · Cited by 156 · see citing works
Microbial H2O2 sensors as archetypical redox signaling modules
Tolédano, M. B., Delaunay, A., Monceau, L., & Tacnet, F. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.05.005 · Cited by 152 · see citing works
Response ofBacillus subtilisto Nitric Oxide and the Nitrosating Agent Sodium Nitroprusside
Moore, C. M., NAKANO, M. M., Wang, T., Ye, R. W., & Helmann, J. D. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.14.4655-4664.2004 · Cited by 147 · see citing works
Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step Mechanism
Graumann, J., Lilie, H., Tang, X., Tucker, K. A., Hoffmann, J. H., Vijayalakshmi, J., Saper, M. A., Bardwell, J. C. A., & Jakob, U. (2001) · Structure · doi:10.1016/s0969-2126(01)00599-8 · Cited by 145 · see citing works
Izawa, S., Maeda, K., Sugiyama, K., Mano, J., Inoue, Y., & Kimura, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28459 · Cited by 138 · see citing works
Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling
Azevedo, D., Tacnet, F., Delaunay, A., Rodrigues‐Pousada, C., & Tolédano, M. B. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00434-9 · Cited by 133 · see citing works
Glutathione Peroxidase 1 Is Regulated by the c-Abl and Arg Tyrosine Kinases
Cao, C., Leng, Y., Huang, W., Liu, X., & Kufe, D. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305770200 · Cited by 128 · see citing works
Crack, J. C., Green, J. D., Cheesman, M. R., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609514104 · Cited by 123 · see citing works
Carmel‐Harel, O., Stearman, R. S., Gasch, A. P., Botstein, D., Brown, P. O., & Storz, G. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02255.x · Cited by 122 · see citing works
Vivancos, A. P., Castillo, E. A., Jones, N., Ayté, J., & Hidalgo, E. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04065.x · Cited by 117 · see citing works
Panmanee, W., Vattanaviboon, P., Poole, L. B., & Mongkolsuk, S. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.4.1389-1395.2006 · Cited by 115 · see citing works
Activation of the Redox-regulated Chaperone Hsp33 by Domain Unfolding
Graf, P. C. F., Martinez‐Yamout, M. A., VanHaerents, S. A., Lilie, H., Dyson, H. J., & Jakob, U. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401764200 · Cited by 101 · see citing works
Li, W., Bottrill, A. R., Bibb, M. J., Buttner, M. J., Paget, M. S. B., & Kleanthous, C. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.08.038 · Cited by 97 · see citing works
D’Autréaux, B., Horner, O., Oddou, J., Jeandey, C., Gambarelli, S., Berthomieu, C., Latour, J., & Michaud‐Soret, I. (2004) · Journal of the American Chemical Society · doi:10.1021/ja031671a · Cited by 96 · see citing works
Self-citationMammalian Antioxidant Defenses Are Not Inducible by H2O2
Desaint, S., Luriau, S., Aude, J.-C., Rousselet, G., & Tolédano, M. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401888200 · Cited by 96 · see citing works
Sukchawalit, R., Loprasert, S., Atichartpongkul, S., et al. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.15.4405-4412.2001 · Cited by 94 · see citing works
Maiorino, M., Roveri, A., Benazzi, L., Bosello-Travain, V., Mauri, P., Toppo, S., Tosatto, S. C. E., & Ursini, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505983200 · Cited by 93 · see citing works
Oxidant-specific Folding of Yap1p Regulates Both Transcriptional Activation and Nuclear Localization
Gulshan, K., Rovinsky, S. A., Coleman, S. T., & Moye-Rowley, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504716200 · Cited by 89 · see citing works
Zinc Center as Redox Switch—New Function for an Old Motif
Ilbert, M., Graf, P. C. F., & Jakob, U. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.835 · Cited by 88 · see citing works
Castillo, E. A., Ayté, J., Chiva, C., Moldón, A., Carrascal, M., Abián, J., Jones, N., & Hidalgo, E. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03020.x · Cited by 87 · see citing works
Dual Role of Peroxiredoxin I in Macrophage-derived Foam Cells
Conway, J., & Kinter, M. T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605026200 · Cited by 66 · see citing works
Assignment of the Zinc Ligands in RsrA, a Redox-Sensing ZAS Protein from Streptomyces coelicolor
Zdanowski, K., Doughty, P. A., Jakimowicz, P., O'Hara, L., Buttner, M. J., Paget, M. S. B., & Kleanthous, C. (2006) · Biochemistry · doi:10.1021/bi060711v · Cited by 65 · see citing works
Reversible Redox- and Zinc-Dependent Dimerization of the <i>Escherichia coli</i> Fur Protein
D'Autréaux, B., Pecqueur, L., Gonzalez de Peredo, A., Diederix, R. E. M., Caux-Thang, C., Tabet, L., Bersch, B., Forest, E., & Michaud-Soret, I. (2007) · Biochemistry · doi:10.1021/bi061636r · Cited by 48 · see citing works
Self-citationThermodynamic Basis for Redox Regulation of the Yap1 Signal Transduction Pathway
Mason, J. T., Kim, S., Knaff, D. B., & Wood, M. J. A. (2006) · Biochemistry · doi:10.1021/bi061136y · Cited by 38 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
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
Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520 · see citing works
Reconciling the chemistry and biology of reactive oxygen species
Winterbourn, C. C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.85 · Cited by 2,504 · see citing works
Chemistry and biology of reactive oxygen species in signaling or stress responses
Dickinson, B. C., & Chang, C. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.607 · Cited by 1,821 · see citing works
Thiol chemistry and specificity in redox signaling
Winterbourn, C. C., & Hampton, M. B. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.004 · Cited by 1,226 · see citing works
Radical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213 · see citing works
Oxidative Stress in Aging Human Skin
Rinnerthaler, M., Bischof, J., Streubel, M., Trost, A., & Richter, K. (2015) · Biomolecules · doi:10.3390/biom5020545 · Cited by 1,053 · see citing works
Role of oxidative stress in the pathogenesis of nonalcoholic steatohepatitis
Rolo, A. P., Teodoro, J. S., & Palmeira, C. M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.003 · Cited by 955 · see citing works
Oxidative stress in normal and impaired wound repair
SCHAFER, M., & WERNER, S. (2008) · Pharmacological Research · doi:10.1016/j.phrs.2008.06.004 · Cited by 902 · see citing works
Glutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function
Hu, W., Zhang, C., Wu, R., Sun, Y., Levine, A., & Feng, Z. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001006107 · Cited by 862 · see citing works
Estrogens and androgens in skeletal physiology and pathophysiology
Almeida, M., Laurent, M. R., Dubois, V., Claessens, F., O'Brien, C. A., Bouillon, R., Vanderschueren, D., & Manolagas, S. C. (2017) · Physiological Reviews · doi:10.1152/physrev.00033.2015 · Cited by 860 · see citing works
T cell lipid peroxidation induces ferroptosis and prevents immunity to infection
Matsushita, M., Freigang, S., Schneider, C., Conrad, M., Bornkamm, G. W., & Kopf, M. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20140857 · Cited by 672 · see citing works
“Although apoptosis has long been considered the primary form of programmed cell death, recent studies have identified that necroptosis can also occur by inactivation of caspase 8 and complex formation of RIP kinase 1 and 3 (Cho et al., 2009; Declercq et al., 2009).”
BackgroundJones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · 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
The Two Faces of Reactive Oxygen Species in Cancer
Reczek, C. R., & Chandel, N. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041916-065808 · Cited by 602 · see citing works
Sleep Loss Can Cause Death through Accumulation of Reactive Oxygen Species in the Gut
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
Redox-responsive polymers for drug delivery: from molecular design to applications
Huo, M., Yuan, J., Tao, L., & Wei, Y. (2014) · Polym. Chem. · doi:10.1039/c3py01192e · Cited by 561 · see citing works
Evolution of Mitochondria as Signaling Organelles
Chandel, N. S. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.013 · Cited by 555 · see citing works
The redox stress hypothesis of aging
Sohal, R. S., & Orr, W. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.445 · Cited by 473 · see citing works
Rhee, S. G., & Woo, H. A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3393 · Cited by 463 · see citing works
The multifaceted role of reactive oxygen species in tumorigenesis
Kirtonia, A., Sethi, G., & Garg, M. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03536-5 · Cited by 452 · see citing works
Mammalian Mitochondrial Complex I: Biogenesis, Regulation, and Reactive Oxygen Species Generation
Koopman, W. J. H., Nijtmans, L. G. J., Dieteren, C. E. J., Roestenberg, P., Valsecchi, F., Smeitink, J. A. M., & Willems, P. H. G. M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2743 · Cited by 411 · see citing works
Mitochondrial ROS regulation of proliferating cells
Diebold, L., & Chandel, N. S. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.198 · Cited by 391 · see citing works
Rigoulet, M., Yoboue, E. D., & Devin, A. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3363 · Cited by 394 · see citing works
Mitochondria: Central Organelles for Melatonin′s Antioxidant and Anti-Aging Actions
Reiter, R., Tan, D., Rosales-Corral, S., Galano, A., Zhou, X., & Xu, B. (2018) · Molecules · doi:10.3390/molecules23020509 · Cited by 393 · see citing works
Thiol-based redox switches in eukaryotic proteins
Brandes, N., Schmitt, S., & Jakob, U. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2285 · Cited by 373 · see citing works
Lipid Metabolism and Ferroptosis
Lee, J.-Y., Kim, W. K., Bae, K.-H., Lee, S. C., & Lee, E.-W. (2021) · Biology · doi:10.3390/biology10030184 · Cited by 374 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
The antioxidant paradox: less paradoxical now?
Halliwell, B. (2013) · British Journal of Clinical Pharmacology · doi:10.1111/j.1365-2125.2012.04272.x · Cited by 318 · see citing works
Functional role of mitochondrial respiratory supercomplexes
Genova, M. L., & Lenaz, G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.11.002 · Cited by 306 · see citing works
Oxidative stress and metabolic pathologies: from an adipocentric point of view
Le Lay, S., Simard, G., Martinez, M. C., & Andriantsitohaina, R. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/908539 · Cited by 291 · see citing works
Plant salt response: Perception, signaling, and tolerance
Xiao, F., & Zhou, H. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2022.1053699 · Cited by 286 · see citing works
The sirtuins, oxidative stress and aging: an emerging link
Merksamer, P. I., Liu, Y., He, W., Hirschey, M. D., Chen, D., & Verdin, E. (2013) · Aging · doi:10.18632/aging.100544 · Cited by 275 · see citing works
Redox signaling across cell membranes
Fisher, A. B. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2378 · Cited by 269 · see citing works
T cells and reactive oxygen species
Belikov, A. V., Schraven, B., & Simeoni, L. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0194-3 · Cited by 264 · see citing works
Redox regulation of cell migration and adhesion
Hurd, T. R., DeGennaro, M., & Lehmann, R. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.11.002 · Cited by 263 · see citing works
Go, Y.-M., & Jones, D. P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.464131 · Cited by 260 · see citing works
Mitochondrial quality control: An integrated network of pathways
Fischer, F., Hamann, A., & Osiewacz, H. D. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.02.004 · Cited by 248 · see citing works
Glutathione peroxidase 4 prevents necroptosis in mouse erythroid precursors
Canli, Ö., Alankuş, Y. B., Grootjans, S., Vegi, N., Hültner, L., Hoppe, P. S., Schroeder, T., Vandenabeele, P., Bornkamm, G. W., & Greten, F. R. (2016) · Blood · doi:10.1182/blood-2015-06-654194 · Cited by 247 · see citing works
Thiol/disulfide redox states in signaling and sensing
Go, Y.-M., & Jones, D. P. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.764840 · Cited by 241 · see citing works
Cannito, S., Novo, E., di Bonzo, L. V., Busletta, C., Colombatto, S., & Parola, M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2737 · Cited by 239 · see citing works
Wilson, C., & González-Billault, C. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00381 · Cited by 238 · see citing works
Oxidative Stress and Huntington’s Disease: The Good, the Bad, and the Ugly
Kumar, A., & Ratan, R. R. (2016) · Journal of Huntington s Disease · doi:10.3233/jhd-160205 · Cited by 236 · see citing works
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · Stresses · doi:10.3390/stresses2030019 · Cited by 218 · see citing works
Iron and Reactive Oxygen Species: Friends or Foes of Cancer Cells?
Bystrom, L. M., Guzman, M. L., & Rivella, S. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5014 · Cited by 212 · see citing works
Mitochondrial and Cytoplasmic ROS Have Opposing Effects on Lifespan
Schaar, C. E., Dues, D. J., Spielbauer, K. K., Machiela, E., Cooper, J. F., Senchuk, M., Hekimi, S., & Van Raamsdonk, J. M. (2015) · PLOS Genetics · doi:10.1371/journal.pgen.1004972 · Cited by 203 · see citing works
Muri, J., Thut, H., Bornkamm, G. W., & Kopf, M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.070 · Cited by 198 · see citing works
Redox-sensitive cysteines bridge p300/CBP-mediated acetylation and FoxO4 activity
Dansen, T. B., Smits, L. M. M., van Triest, M. H., de Keizer, P. L. J., van Leenen, D., Koerkamp, M. G., Szypowska, A., Meppelink, A., Brenkman, A. B., Yodoi, J., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.194 · Cited by 201 · see citing works
Small molecules regulating reactive oxygen species homeostasis for cancer therapy
Zhang, J., Duan, D., Song, Z., Liu, T., Hou, Y., & Fang, J. (2021) · Medicinal Research Reviews · doi:10.1002/med.21734 · Cited by 184 · see citing works
A Model of Redox Kinetics Implicates the Thiol Proteome in Cellular Hydrogen Peroxide Responses
Adimora, N. J., Jones, D. P., & Kemp, M. L. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2968 · Cited by 175 · see citing works
Li, F., Han, X., Li, F., Wang, R., Wang, H., Gao, Y., Wang, X., Fang, Z., Zhang, W., Yao, S., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.04.001 · Cited by 169 · see citing works
The role of tumor suppressor p53 in the antioxidant defense and metabolism
Budanov, A. V. (2014) · Subcellular Biochemistry · doi:10.1007/978-94-017-9211-0_18 · Cited by 157 · see citing works
NADPH oxidase deficiency underlies dysfunction of aged CD8+ Tregs
Wen, Z., Shimojima, Y., Shirai, T., Li, Y., Ju, J., Yang, Z., Tian, L., Goronzy, J. J., & Weyand, C. M. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84181 · Cited by 146 · see citing works
Activation of AMPK under Hypoxia: Many Roads Leading to Rome
Dengler, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072428 · Cited by 133 · see citing works
Which NADPH Oxidase Isoform Is Relevant for Ischemic Stroke? The Case for Nox 2
Kahles, T., & Brandes, R. P. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4721 · Cited by 125 · see citing works
Ayer, A., Gourlay, C. W., & Dawes, I. W. (2014) · FEMS Yeast Research · doi:10.1111/1567-1364.12114 · Cited by 125 · see citing works
Influence of vitamin C and vitamin E on redox signaling: implications for exercise adaptations
Cobley, J. N., McHardy, H., Morton, J. P., Nikolaidis, M. G., & Close, G. L. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.018 · Cited by 118 · see citing works
Sethumadhavan, S., Silva, M., Philbrook, P., Nguyen, T., Hatfield, S. M., Ohta, A., & Sitkovsky, M. V. (2017) · PLOS ONE · doi:10.1371/journal.pone.0187314 · Cited by 119 · see citing works
Gusarova, G. A., Dada, L. A., Kelly, A. M., Brodie, C., Witters, L. A., Chandel, N. S., & Sznajder, J. I. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00054-09 · Cited by 118 · see citing works
The Plasma Membrane: A Platform for Intra- and Intercellular Redox Signaling
Nordzieke, D. E., & Medraño-Fernandez, I. (2018) · Antioxidants · doi:10.3390/antiox7110168 · Cited by 90 · see citing works
The cytotoxic mechanisms of disulfiram and copper(ii) in cancer cells
Tawari, P. E., Wang, Z., Najlah, M., Tsang, C. W., Kannappan, V., Liu, P., McConville, C., He, B., Armesilla, A. L., & Wang, W. (2015) · Toxicology Research · doi:10.1039/c5tx00210a · Cited by 86 · see citing works
Chlorinative Stress in Age-Related Diseases: A Literature Review
Casciaro, M., Di Salvo, E., Pace, E., Ventura-Spagnolo, E., Navarra, M., & Gangemi, S. (2017) · Immunity & Ageing · doi:10.1186/s12979-017-0104-5 · Cited by 85 · see citing works
Gao, Y., Ray, S., Dai, S., Ivanov, A. R., Abu‐Absi, N. R., Lewis, A. M., Huang, Z., Xing, Z., Borys, M. C., Li, Z. J., et al. (2016) · Biotechnology Journal · doi:10.1002/biot.201600030 · Cited by 76 · see citing works
Ali, S. S., Marcondes, M.-C. G., Bajova, H., Dugan, L. L., & Conti, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.155432 · Cited by 71 · see citing works
Mitochondrial health, the epigenome and healthspan
Aon, M. A., Cortassa, S., Juhaszova, M., & Sollott, S. J. (2016) · Clinical Science · doi:10.1042/cs20160002 · Cited by 66 · see citing works
Mitochondrial stress-dependent regulation of cellular protein synthesis
Topf, U., Uszczynska-Ratajczak, B., & Chacinska, A. (2019) · Journal of Cell Science · doi:10.1242/jcs.226258 · Cited by 52 · see citing works
Oxidative stress, DNA damage, and c-Abl signaling: At the crossroad in neurodegenerative diseases?
Gonfloni, S., Maiani, E., Di Bartolomeo, C., Diederich, M., & Cesareni, G. (2012) · International Journal of Cell Biology · doi:10.1155/2012/683097 · Cited by 63 · see citing works
Vitamin C Administration Attenuates Overload-Induced Skeletal Muscle Hypertrophy in Rats
Makanae, Y., Kawada, S., Sasaki, K., Nakazato, K., & Ishii, N. (2013) · Acta Physiologica · doi:10.1111/apha.12042 · Cited by 59 · see citing works
The role of mitochondria in <scp>mTOR</scp>‐regulated longevity
Wei, Y., Zhang, Y., Cai, Y., & Xu, M. (2015) · Biological Reviews · doi:10.1111/brv.12103 · Cited by 56 · see citing works
Dual regulation of SLC25A39 by AFG3L2 and iron controls mitochondrial glutathione homeostasis
Shi, X., DeCiucis, M., Grabinska, K. A., Kanyo, J., Liu, A., Lam, T. T., & Shen, H. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.008 · Cited by 54 · 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
Song, N.-Y., Lee, Y.-H., Na, H.-K., Baek, J.-H., & Surh, Y.-J. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.02.001 · Cited by 36 · see citing works
Fiorilla, I., Martinotti, S., Todesco, A. M., Bonsignore, G., Cavaletto, M., Patrone, M., Ranzato, E., & Audrito, V. (2023) · Cells · doi:10.3390/cells12162048 · Cited by 34 · see citing works
Triplet-Energy Quenching Functions of Antioxidant Molecules
Angelé-Martínez, C., Goncalves, L. C. P., Premi, S., Augusto, F. A., Palmatier, M. A., Amar, S. K., & Brash, D. E. (2022) · Antioxidants · doi:10.3390/antiox11020357 · Cited by 21 · see citing works
García-Barbazán, I., Torres-Cano, A., García-Rodas, R., Sachse, M., Luque, D., Megías, D., & Zaragoza, O. (2024) · mBio · doi:10.1128/mbio.02549-23 · Cited by 14 · see citing works
Mitochondrial Function and Neurodegenerative Diseases
Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2 · see citing works
- Authors
- D'Autréaux, B., & Toledano, M. B.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2007-10
- Volume
- 8
- Issue
- 10
- Pages
- 813-824
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2102472842
- Cited by
- 3,642
- References
- 133
- Citations by year
- 2026: 155 · 2025: 214 · 2024: 248 · 2023: 266 · 2022: 264 · 2021: 299 · 2020: 184 · 2019: 238 · 2018: 217 · 2017: 213 · 2016: 224 · 2015: 188 · 2014: 204 · 2013: 184 · 2012: 166
- FWCI
- 6.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- reactive oxygen species, ROS signalling, ROS homeostasis, oxidative stress, aging, prokaryotes, mammals
- MeSH terms
- Animals, Homeostasis, Humans, 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