Redox regulation of cell survival
Open accessAbstract
Reactive oxygen species (ROS) and reactive nitrogen species (RNS) play important roles in regulation of cell survival. In general, moderate levels of ROS/RNS may function as signals to promote cell proliferation and survival, whereas severe increase of ROS/RNS can induce cell death. Under physiologic conditions, the balance between generation and elimination of ROS/RNS maintains the proper function of redox-sensitive signaling proteins. Normally, the redox homeostasis ensures that the cells respond properly to endogenous and exogenous stimuli. However, when the redox homeostasis is disturbed, oxidative stress may lead to aberrant cell death and contribute to disease development. This review focuses on the roles of key transcription factors, signal-transduction pathways, and cell-death regulators in affecting cell survival, and how the redox systems regulate the functions of these molecules. The current understanding of how disturbance in redox homeostasis may affect cell death and contribute to the development of diseases such as cancer and degenerative disorders is reviewed. We also discuss how the basic knowledge on redox regulation of cell survival can be used to develop strategies for the treatment or prevention of those diseases.Antioxid. Redox Signal. 10, 1343–1374. Redox Biology and Regulatory Mechanisms Redox homeostasis: ROS production and elimination Oxidative stress and its consequences Redox-mediated mechanisms in regulation of cellular processes Transcriptional regulation Direct oxidative modification Regulation of redox-sensitive interacting proteins Regulation of redox-sensitive modifying enzymes Regulation of protein turnover Redox Regulation of Signaling Proteins Affecting Cell Death and Survival Redox regulation of cell survival at the transcription level NF-κB Role of NF-κB in cell survival Redox regulation of NF-κB Redox regulation of nuclear NF-κB Cytoplasmic regulation of NF-κB AP-1 Role of AP-1 in cell survival Redox regulation of AP-1 Nrf2 Role of Nrf2 in cell survival Redox regulation of Nrf2 HIF Role of HIF in cell survival Redox regulation of HIF Redox regulation of cell survival at the signal-transduction level Mitogen-activated protein kinase Role of MAPK for cell survival under oxidative stress Redox regulation of MAPK PI3K/Akt pathway Role of PI3K/Akt in cell survival Redox regulation of PI3K/Akt Redox regulation of cell survival at the cell death–execution level Caspases Role of caspases in cell death and survival Redox regulation of caspases Bcl-2 Role of Bcl-2 in cell survival Redox regulation of Bcl-2 Cytochrome c Role of cytochrome c in cell survival Redox regulation of cytochrome c Integration of redox-sensitive signaling pathways in the regulation of cell survival Crosstalk between signaling pathways Role of p53 P53 serves as an antioxidant to maintain redox homeostasis and normal cell survival Role of p53 in cell death Redox regulation of p53 Role of Redox Regulation of Cell Survival in Pathogenesis of Diseases Aberrant prolonged cell survival leads to cancer Oncogene activation Ras c-Myc Bcr-Abl Loss of functional p53 Aberrant expression of antioxidant enzymes Superoxide dismutase (SOD) Glutathione peroxidase (GPX) and peroxiredoxin (Prx) Diseases with excessive cell death: aging and degenerative disorders Therapeutic Strategies Based on Redox Regulation of Cell Survival Manipulating redox homeostasis Pro-oxidants as a therapeutic strategy for cancer Antioxidants for prevention of degenerative diseases Modulating redox-sensitive signaling molecules Concluding Remarks
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
SOD is composed of three isoforms: SOD1 (Cu/Zn-SOD, the predominant •O2− scavenger, localized in the cytoplasm), SOD2 (Mn-SOD, in the mitochondrial intermembrane space, nucleus, and lysosomes) and SOD3 (Cu/Zn-SOD, localized in the mitochondrion and extracellular matrix).
“It is composed of three isoforms, SOD1 (Cu/Zn-SOD is the predominant •O2− scavenger and is localized in the cytoplasm), SOD2 (Mn-SOD, in the mitochondrial intermembrane space, nucleus, and lysosomes) and SOD3 (Cu/Zn-SOD, is localized in the mitochondrion and extracellular matrix) [100].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [100]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
3 retracted
Kasuno, K., Takabuchi, S., Fukuda, K., Kizaka‐Kondoh, S., Yodoi, J., Adachi, T., Semenza, G. L., & Hirota, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308197200 · Cited by 223 · see citing works
RetractedEl‐Remessy, A. B., Bartoli, M., Platt, D. H., Fulton, D. J., & Caldwell, R. B. (2004) · Journal of Cell Science · doi:10.1242/jcs.01612 · Cited by 147 · see citing works
RetractedModulation of Intracellular Signaling Pathways to Induce Apoptosis in Prostate Cancer Cells
Guo, J., Zhu, T., Xiao, Z. J., & Chen, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702938200 · Cited by 9 · see citing works
RetractedHanahan, D., & Weinberg, R. A. (2000) · Cell · doi:10.1016/s0092-8674(00)81683-9 · Cited by 29,219 · see citing works
Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269 · see citing works
Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works
Free radicals, metals and antioxidants in oxidative stress-induced cancer
Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680 · see citing works
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216 · see citing works
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535 · see citing works
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,178 · cited 1× · see citing works
“Although the increase in ROS production induced by Ras can transform some immortalized nontumorigenic cells to malignant cells, Ras transformation also provoked premature senescence in primary cells in the Em-N-Ras transgenic mouse model (275).”
Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,153 · see citing works
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506 · see citing works
Itoh, K., Chiba, T., Takahashi, S., Ishii, T., Igarashi, K., Katoh, Y., Oyake, T., Hayashi, N., Satoh, K., Hatayama, I., et al. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6943 · Cited by 3,999 · see citing works
Kim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905 · see citing works
Hayden, M. S., & Ghosh, S. (2004) · Genes & Development · doi:10.1101/gad.1228704 · Cited by 3,842 · see citing works
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works
Effects of a combination of beta carotene and vitamin A on lung cancer and cardiovascular disease
Omenn, G. S., Goodman, G. E., Thornquist, M. D., Balmes, J., Cullen, M. R., Glass, A., Keogh, J. P., Meyskens, F. L., Valanis, B., Williams, J. H., et al. (1996) · New England Journal of Medicine · doi:10.1056/nejm199605023341802 · Cited by 3,638 · 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
Targeting the KEAP1-NRF2 system to prevent kidney disease progression
Nezu, M., Suzuki, N., & Yamamoto, M. (2017) · American Journal of Nephrology · doi:10.1159/000475890 · Cited by 3,447 · see citing works
Bcl-2 functions in an antioxidant pathway to prevent apoptosis
Hockenbery, D. M., Oltvai, Z. N., Yin, X., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,420 · see citing works
The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation
Angel, P. E., & Karin, M. (1991) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(91)90011-9 · Cited by 3,390 · see citing works
Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,369 · see citing works
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · see citing works
AP-1 as a regulator of cell life and death
Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961 · cited 2× · see citing works
“The intracellular levels of c-jun and c-fos are controlled mainly by their transcription rates, which are tightly regulated by a variety of stimuli (278).”
The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases
Ogryzko, V. V., Schiltz, R. L., Russanova, V., Howard, B. H., & Nakatani, Y. (1996) · Cell · doi:10.1016/s0092-8674(00)82001-2 · Cited by 2,952 · see citing works
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734 · see citing works
NF-κB at the crossroads of life and death
Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709 · 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
Production of large amounts of hydrogen peroxide by human tumor cells.
Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,504 · see citing works
Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473 · see citing works
The Regulation of AP-1 Activity by Mitogen-activated Protein Kinases
Karin, M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16483 · Cited by 2,432 · see citing works
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377 · see citing works
Johnstone, R. W., Ruefli, A. A., & Lowe, S. W. (2002) · Cell · doi:10.1016/s0092-8674(02)00625-6 · Cited by 2,236 · see citing works
Introduction to NF-κB: players, pathways, perspectives
Gilmore, T. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209954 · Cited by 2,227 · 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
Mitochondrial 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 · see citing works
Protein S-nitrosylation: Purview and parameters
Hess, D. T., Matsumoto, A., Kim, S.-O., Marshall, H. E., & Stamler, J. S. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1569 · Cited by 2,153 · see citing works
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
Szabó, C., Ischiropoulos, H., & Radi, R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2222 · Cited by 2,134 · see citing works
TIGAR, a p53-Inducible Regulator of Glycolysis and Apoptosis
Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C., Nakano, K., Bartrons, R., Gottlieb, E., & Vousden, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.05.036 · Cited by 2,019 · see citing works
Crucial role of p53-dependent cellular senescence in suppression of Pten-deficient tumorigenesis
Chen, Z., Trotman, L. C., Shaffer, D., Lin, H.-K., Dotan, Z. A., Niki, M., Koutcher, J. A., Scher, H. I., Ludwig, T., Gerald, W., et al. (2005) · Nature · doi:10.1038/nature03918 · Cited by 1,993 · see citing works
ROS stress in cancer cells and therapeutic implications.
Pelicano, H., Carney, D., & Huang, P. (2004) · Drug resistance updates · doi:10.1016/j.drup.2004.01.004 · Cited by 1,992 · see citing works
Self-citationAmplification of a gene encoding a p53-associated protein in human sarcomas
Oliner, J. D., Kinzler, K. W., Meltzer, P. S., George, D. L., & Vogelstein, B. (1992) · Nature · doi:10.1038/358080a0 · Cited by 1,949 · 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
Sheehan, D., Meade‐Murphy, G., Foley, V., & DOWD, C. A. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3600001 · Cited by 1,840 · see citing works
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792 · 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
The p66shc adaptor protein controls oxidative stress response and life span in mammals
Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712 · see citing works
Biochemistry and pathology of radical-mediated protein oxidation
Dean, R. T., Fu, S., Stocker, R., & Davies, M. J. (1997) · Biochemical Journal · doi:10.1042/bj3240001 · Cited by 1,678 · see citing works
p53 Regulates Mitochondrial Respiration
Matoba, S., Kang, J.-G., Patino, W. D., Wragg, A., Boehm, M., Gavrilova, O., Hurley, P. J., Bunz, F., & Hwang, P. M. (2006) · Science · doi:10.1126/science.1126863 · Cited by 1,650 · see citing works
Fantin, V. R., St-Pierre, J., & Leder, P. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.04.023 · Cited by 1,635 · see citing works
The PI3K‒PDK1 connection: more than just a road to PKB
Vanhaesebroeck, B., & Alessi, D. R. (2000) · Biochemical Journal · doi:10.1042/bj3460561 · Cited by 1,632 · see citing works
Novack, D. V., Sorenson, C. M., Shutter, J. R., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80065-m · Cited by 1,628 · 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
Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550 · cited 1× · see citing works
“Under normoxia, FIH-1 hydroxylates an N-terminal asparagines residue and renders HIF inactive by preventing the binding between HIF and its coactivators (175).”
The JNK signal transduction pathway
Weston, C. R. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(01)00258-1 · Cited by 1,545 · see citing works
Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase
Deng, H., Hentati, A., Tainer, J. A., Iqbal, Z., Cayabyab, A., Hung, W.-Y., Getzoff, E. D., Hu, P., Herzfeldt, B., Roos, R. P., et al. (1993) · Science · doi:10.1126/science.8351519 · Cited by 1,479 · see citing works
Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., & Yamamoto, M. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.21.16023 · Cited by 1,460 · see citing works
p53 mutant mice that display early ageing-associated phenotypes
Tyner, S. D., Venkatachalam, S., Choi, J., Jones, S., Ghebranious, N., Igelmann, H., Lu, X., Soron, G., Cooper, B., Brayton, C., et al. (2002) · Nature · doi:10.1038/415045a · Cited by 1,459 · cited 2× · see citing works
“Despite only having one wildtype allele, the mice showed a premature aging phenotype, but seemed not prone to cancer development (307).”
The Haber–Weiss reaction and mechanisms of toxicity
Kehrer, J. P. (2000) · Toxicology · doi:10.1016/s0300-483x(00)00231-6 · Cited by 1,418 · see citing works
Rac1b and reactive oxygen species mediate MMP-3-induced EMT and genomic instability
Radisky, D. C., Levy, D. D., Littlepage, L. E., Liu, H., Nelson, C. M., Fata, J. E., Leake, D., Godden, E. L., Albertson, D. G., Angela Nieto, M., et al. (2005) · Nature · doi:10.1038/nature03688 · Cited by 1,284 · see citing works
Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors
Kagan, V. E., Tyurin, V. A., Jiang, J., Tyurina, Y. Y., Ritov, V. B., Amoscato, A. A., Osipov, A. N., Belikova, N. A., Kapralov, A. A., Kini, V., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio727 · Cited by 1,256 · see citing works
Omenn, G. S., Goodman, G. E., Thornquist, M. D., Balmes, J., Cullen, M. R., Glass, A., Keogh, J. P., Meyskens, F. L., Valanis, B., Williams, J. H., et al. (1996) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/88.21.1550 · Cited by 1,255 · see citing works
Base-excision repair of oxidative DNA damage
David, S. S., O'Shea, V. L., & Kundu, S. (2007) · Nature · doi:10.1038/nature05978 · Cited by 1,238 · see citing works
Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival
Cullinan, S. B., Zhang, D. D., Hannink, M., Arvisais, E. W., Kaufman, R. J., & Diehl, J. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7198-7209.2003 · Cited by 1,233 · see citing works
Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
Yang, D. D., Kuan, C.-Y., Whitmarsh, A. J., Rinócn, M., Zheng, T. S., Davis, R. J., RAKIC, P. T., & Flavell, R. A. (1997) · Nature · doi:10.1038/39899 · Cited by 1,230 · see citing works
ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
Tobiume, K., Matsuzawa, A., Takahashi, T., Nishitoh, H., Morita, K., Takeda, K., Minowa, O., Miyazono, K., Noda, T., & Ichijo, H. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve046 · Cited by 1,213 · see citing works
Lipid hydroperoxide generation, turnover, and effector action in biological systems
Girotti, A. W. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32182-9 · Cited by 1,204 · see citing works
Huang, E. L., Arany, Z. P., Livingston, D. M., & Bunn, H. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.50.32253 · Cited by 1,190 · see citing works
Giorgio, M., Migliaccio, E., Orsini, F., Paolucci, D., Moroni, M., Contursi, C., Pelliccia, G., Luzi, L., Minucci, S., Marcaccio, M., et al. (2005) · Cell · doi:10.1016/j.cell.2005.05.011 · Cited by 1,176 · see citing works
Redox Regulation of Cellular Signalling
Kamata, H., & Hirata, H. (1999) · Cellular Signalling · doi:10.1016/s0898-6568(98)00037-0 · Cited by 1,150 · 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
REDOX REGULATION OF CELLULAR ACTIVATION
Nakamura, H., Nakamura, K., & Yodoi, J. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.351 · Cited by 1,106 · see citing works
Regulation of JNK signaling by GSTp
Adler, V., Yin, Z., Fuchs, S. Y., Benezra, M., Rosario, L., Tew, K. D., Pincus, M. R., Sardana, M., Henderson, C. J., Wolf, C. R., et al. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1321 · Cited by 1,105 · see citing works
Trachootham, D., Zhou, Y., Zhang, H., Demizu, Y., Chen, Z., Pelicano, H., Chiao, P. J., Achanta, G., Arlinghaus, R. B., Liu, J., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.009 · Cited by 1,080 · see citing works
Molecular Mechanisms Activating the Nrf2-Keap1 Pathway of Antioxidant Gene Regulation
Kobayashi, M., & Yamamoto, M. P. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.385 · Cited by 1,075 · see citing works
Huang, H.-C., Nguyen, T., & Pickett, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206911200 · Cited by 1,070 · see citing works
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,061 · see citing works
Trends in oxidative aging theories
Muller, F. L., Lustgarten, M. S., Jang, Y., Richardson, A., & Van Remmen, H. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.03.034 · Cited by 1,053 · 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
Reactions of oxyl radicals with DNA
Breen, A. P., & Murphy, J. A. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00209-3 · Cited by 1,038 · see citing works
Gao, X., Wu, G., Gu, X., Fu, L., & Mei, C. (2013) · Kidney & Blood Pressure Research · doi:10.1159/000355743 · Cited by 1,036 · see citing works
The JNK signal transduction pathway
Weston, C. R., & Davis, R. J. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.02.001 · Cited by 1,021 · see citing works
Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969 · see citing works
Beckman, K. B., & Ames, B. N. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.19633 · Cited by 959 · see citing works
Reactive Oxygen Species: A Breath of Life or Death?
Fruehauf, J. P., & Meyskens, F. L. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2082 · Cited by 908 · see citing works
Kim, Y.-M., Talanian, R. V., & Billiar, T. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.31138 · Cited by 887 · see citing works
c-Myc Can Induce DNA Damage, Increase Reactive Oxygen Species, and Mitigate p53 Function
Vafa, O., Wade, M., Kern, S., Beeche, M., Pandita, T. K., Hampton, G. M., & Wahl, G. M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00520-8 · Cited by 876 · 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
Superoxide dismutase as a target for the selective killing of cancer cells
Huang, P., Li, F., Oldham, E. A., Keating, M. J., & Plunkett, W. K. (2000) · Nature · doi:10.1038/35030140 · Cited by 842 · see citing works
Self-citationLu, H., Forbes, R. A., & Verma, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202487200 · Cited by 839 · see citing works
Protein carbonylation, cellular dysfunction, and disease progression
Dalle‐Donne, I., Aldini, G., Carini, M., Colombo, R., Rossi, R., & Milzani, A. (2006) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2006.tb00407.x · Cited by 836 · see citing works
Mitochondrial permeability transition and oxidative stress
Kowaltowski, A. J., Castilho, R. F., & Vercesi, A. E. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02316-x · Cited by 832 · see citing works
Matthews, J. R., Wakasugi, N., Virelizier, J., Yodoi, J., & Hay, R. T. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.15.3821 · Cited by 831 · see citing works
Zhong, H., Suyang, H., Erdjument‐Bromage, H., Tempst, P., & Ghosh, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80222-6 · Cited by 828 · see citing works
Reactive Oxygen Species-Induced Activation of the MAP Kinase Signaling Pathways
McCubrey, J. A., LaHair, M. M., & Franklin, R. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1775 · Cited by 804 · see citing works
Bhaskar, P. T., & Hay, N. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.020 · Cited by 798 · see citing works
Lee, J., Calkins, M. J., Chan, K., Kan, Y. W., & Johnson, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211558200 · Cited by 783 · see citing works
The role of hypoxia inducible factor 1 (HIF-1) in hypoxia induced apoptosis: Figure 1
Greijer, A. E., & van der Wall, E. (2004) · Journal of Clinical Pathology · doi:10.1136/jcp.2003.015032 · Cited by 781 · see citing works
Madrid, L. V., Mayo, M. W., Reuther, J. Y., & Baldwin, A. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101103200 · Cited by 777 · see citing works
Suh, J. H., Shenvi, S. V., Dixon, B. M., Liu, H., Jaiswal, A. K., Liu, R.-M., & Hagen, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400282101 · Cited by 774 · see citing works
An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen
Chan, K., Han, X.-D., & Kan, Y. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081082098 · Cited by 766 · see citing works
Vermeulen, L., Wilde, G. D., Damme, P. V., Berghe, W. V., & Haegeman, G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg139 · Cited by 760 · see citing works
Unraveling peroxynitrite formation in biological systems
Radi, R., Peluffo, G., Alvarez, M. N., Naviliat, M., & Cayota, A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00373-7 · Cited by 735 · 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
Induction of gadd45β by NF-κB downregulates pro-apoptotic JNK signalling
De Smaele, E., Zazzeroni, F., Papa, S., Nguyen, D. U., Jin, R., Jones, J., Cong, R., & Franzoso, G. (2001) · Nature · doi:10.1038/35104560 · Cited by 732 · see citing works
Thioredoxin and Related Molecules–From Biology to Health and Disease
Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724 · see citing works
Akt Phosphorylates and Negatively Regulates Apoptosis Signal-Regulating Kinase 1
Kim, A. H., Khursigara, G., Sun, X., Franke, T. F., & Chao, M. V. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.3.893-901.2001 · Cited by 710 · see citing works
Redistribution of Intracellular Oxygen in Hypoxia by Nitric Oxide: Effect on HIF1α
Hagen, T., Taylor, C. T., Lam, F., & Moncada, S. (2003) · Science · doi:10.1126/science.1088805 · Cited by 704 · see citing works
Conversion of Bcl-2 from Protector to Killer by Interaction with Nuclear Orphan Receptor Nur77/TR3
Lin, B., Kolluri, S. K., Lin, F., Liu, W., Han, Y.-H., Cao, X., Dawson, M. I., Reed, J. C., & Zhang, X.-K. (2004) · Cell · doi:10.1016/s0092-8674(04)00162-x · Cited by 672 · see citing works
Elchuri, S., Oberley, T. D., Qi, W., Eisenstein, R. S., Jackson Roberts, L., Van Remmen, H., Epstein, C. J., & Huang, T.-T. (2005) · Oncogene · doi:10.1038/sj.onc.1208207 · Cited by 667 · see citing works
Dual regulation of caspase activity by hydrogen peroxide: implications for apoptosis
Hampton, M. B., & Orrenius, S. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01068-5 · Cited by 663 · see citing works
Kwak, M.-K., Wakabayashi, N., Itoh, K., Motohashi, H., Yamamoto, M. P., & Kensler, T. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211898200 · Cited by 661 · see citing works
Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro.
Toledano, M. B., & Leonard, W. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4328 · Cited by 657 · see citing works
In vivo ubiquitination and proteasome-mediated degradation of p53(1).
Maki, C. G., Huibregtse, J. M., & Howley, P. M. (1996) · PubMed · Cited by 645 · see citing works
Shen, H.-M., & Liu, Z.-G. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.10.056 · Cited by 629 · 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
JunD Reduces Tumor Angiogenesis by Protecting Cells from Oxidative Stress
Gerald, D., Berra, E., Frapart, Y. M., Chan, D. A., Giaccia, A. J., Mansuy, D., Pouysségur, J., Yaniv, M., & Mechta-Grigoriou, F. (2004) · Cell · doi:10.1016/j.cell.2004.08.025 · Cited by 588 · see citing works
Kabe, Y., Ando, K., Hirao, S., Yoshida, M., & Handa, H. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.395 · Cited by 585 · see citing works
Defective T Cell Differentiation in the Absence of Jnk1
Dong, C., Yang, D. D., Wysk, M., Whitmarsh, A. J., Davis, R. J., & Flavell, R. A. (1998) · Science · doi:10.1126/science.282.5396.2092 · Cited by 579 · see citing works
Radjendirane, V., & Jaiswal, A. K. (1998) · Oncogene · doi:10.1038/sj.onc.1202237 · Cited by 566 · see citing works
Caspases in cell survival, proliferation and differentiation
Lamkanfi, M., Festjens, N., Declercq, W., Berghe, T. V., & Vandenabeele, P. (2006) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402047 · Cited by 564 · see citing works
Daley, G. Q., & Baltimore, D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.23.9312 · Cited by 563 · see citing works
Yamaguchi, T., Sano, K., Takakura, K., Saito, I., Shinohara, Y., Asano, T., & Yasuhara, H. (1998) · Stroke · doi:10.1161/01.str.29.1.12 · Cited by 558 · see citing works
Liu, H., Nishitoh, H., Ichijo, H., & Kyriakis, J. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2198-2208.2000 · Cited by 545 · see citing works
Targeting programmed cell death in neurodegenerative diseases
Vila, M., & Przedborski, S. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1100 · Cited by 545 · see citing works
c-Jun is essential for normal mouse development and hepatogenesis
Hilberg, F., Aguzzi, A., Howells, N., & Wagner, E. F. (1993) · Nature · doi:10.1038/365179a0 · Cited by 539 · see citing works
Transcriptional regulation of bcl-2 by nuclear factor κB and its significance in prostate cancer
Catz, S. D., & Johnson, J. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204926 · Cited by 538 · see citing works
Reactive oxygen species in oncogenic transformation
Behrend, L., Henderson, G., & Zwacka, R. M. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311441 · Cited by 531 · see citing works
Vascular protection: superoxide dismutase isoforms in the vessel wall.
Faraci, F., & Didion, S. (2004) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000133604.20182.cf · Cited by 528 · see citing works
Coping with stress: multiple ways to activate p53
Horn, H. F., & Vousden, K. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210263 · Cited by 522 · see citing works
Knebel, A., Rahmsdorf, H. J., Ullrich, A., & Herrlich, P. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00916.x · Cited by 514 · see citing works
Rahman, I., Marwick, J., & Kirkham, P. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.05.042 · Cited by 507 · see citing works
Dose-dependent oncogene-induced senescence in vivo and its evasion during mammary tumorigenesis
Sarkisian, C. J., Keister, B. A., Stairs, D. B., Boxer, R. B., Moody, S. E., & Chodosh, L. A. (2007) · Nature Cell Biology · doi:10.1038/ncb1567 · Cited by 490 · see citing works
Kokoszka, J. E., Coskun, P. E., Esposito, L., & Wallace, D. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051627098 · Cited by 488 · see citing works
Oxidative stress and aberrant signaling in aging and cognitive decline
Dröge, W., & Schipper, H. M. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00294.x · Cited by 479 · see citing works
Multiple pathways of cytochrome c release from mitochondria in apoptosis
Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.03.016 · Cited by 466 · see citing works
Delayed ageing through damage protection by the Arf/p53 pathway
Matheu, A., Maraver, A., Klatt, P., Flores, I., Garcia-Cao, I., Borras, C., Flores, J. M., Viña, J., Blasco, M. A., & Serrano, M. (2007) · Nature · doi:10.1038/nature05949 · Cited by 466 · see citing works
Epidermal Growth Factor Receptor-dependent Akt Activation by Oxidative Stress Enhances Cell Survival
Wang, X., McCullough, K. D., Franke, T. F., & Holbrook, N. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14624 · Cited by 461 · see citing works
Mitochondrial Generation of Reactive Oxygen Species and its Role in Aerobic Life
Inoue, M., Sato, E. F., Nishikawa, M., Park, A.-M., Kira, Y., Imada, I., & Utsumi, K. (2003) · Current Medicinal Chemistry · doi:10.2174/0929867033456477 · Cited by 459 · see citing works
Reynaert, N. L., van der Vliet, A., Guala, A. S., McGovern, T., Hristova, M., Pantano, C., Heintz, N. H., Heim, J., Ho, Y.-S., Matthews, D. E., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603290103 · Cited by 442 · see citing works
Regulation of HIF-1α Stability through S-Nitrosylation
Li, F., Sonveaux, P., Rabbani, Z. N., Liu, S., Yan, B., Huang, Q., Vujašković, Ž., Dewhirst, M. W., & Li, C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.024 · Cited by 439 · see citing works
Mitochondrial nitric oxide synthase
Ghafourifar, P., & Cadenas, E. (2005) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2005.02.005 · Cited by 429 · see citing works
Requirement for Caspase-8 in NF-κB Activation by Antigen Receptor
Su, H. C., Bidère, N., Zheng, L., Cubre, A., Sakai, K., Dale, J. K., Salmena, L., Hakem, R., Straus, S. E., & Lenardo, M. J. (2005) · Science · doi:10.1126/science.1104765 · Cited by 427 · see citing works
Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors
Haddad, J. J. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(02)00053-0 · Cited by 427 · see citing works
Induction of apoptosis by the transcription factor c‐Jun
Bossy‐Wetzel, E., Bakiri, L., & Yaniv, M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1695 · Cited by 427 · see citing works
Transient excess of MYC activity can elicit genomic instability and tumorigenesis
Felsher, D. W., & Bishop, J. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3940 · Cited by 420 · see citing works
Thrombin Activates the Hypoxia-Inducible Factor-1 Signaling Pathway in Vascular Smooth Muscle Cells
Görlach, A., Diebold, I., Schini‐Kerth, V. B., Berchner‐Pfannschmidt, U., Roth, U., Brandes, R. P., Kietzmann, T., & Busse, R. (2001) · Circulation Research · doi:10.1161/hh1301.092678 · Cited by 416 · see citing works
Nitric Oxide Impairs Normoxic Degradation of HIF-1α by Inhibition of Prolyl Hydroxylases
Metzen, E., Zhou, J., Jelkmann, W., Fandrey, J., & Brüne, B. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0791 · Cited by 414 · see citing works
Redox modulation of p53 conformation and sequence-specific DNA binding in vitro.
Hainaut, P. L., & Milner, J. (1993) · PubMed · Cited by 408 · see citing works
Mitochondrial point mutations do not limit the natural lifespan of mice
Vermulst, M., Bielas, J. H., Kujoth, G. C., Ladiges, W. C., Rabinovitch, P. S., Prolla, T. A., & Loeb, L. A. (2007) · Nature Genetics · doi:10.1038/ng1988 · Cited by 404 · see citing works
Bubici, C., Papa, S., Dean, K., & Franzoso, G. (2006) · Oncogene · doi:10.1038/sj.onc.1209936 · Cited by 399 · see citing works
Colotta, F., Polentarutti, N., Sironi, M., & Mantovani, A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36956-x · Cited by 396 · see citing works
Antioxidant enzyme levels in cancer.
Oberley, T. D., & Oberley, L. W. (1997) · PubMed · Cited by 393 · see citing works
Pineda‐Molina, E., Klatt, P., Vázquez, J., Marina, A., de Lacoba, M. G., Pérez‐Sala, D., & Lamas, S. (2001) · Biochemistry · doi:10.1021/bi011459o · Cited by 389 · see citing works
Nitric oxide represses inhibitory κB kinase through S-nitrosylation
Reynaert, N. L., Ckless, K., Korn, S. H., Vos, N., Guala, A. S., Wouters, E. F. �., van der Vliet, A., & Janssen-Heininger, Y. M. W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400588101 · Cited by 388 · see citing works
Oxygen, a source of life and stress
Brahimi-Horn, M. C., & Pouysségur, J. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.06.018 · Cited by 383 · see citing works
Pelicano, H., Xu, R., Du, M., Feng, L., Sasaki, R., Carew, J. S., Hu, Y., Ramdas, L., Hu, L., Keating, M. J., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200512100 · Cited by 382 · see citing works
Self-citationInhibition of NF-κB by S-Nitrosylation
Marshall, H. E., & Stamler, J. S. (2001) · Biochemistry · doi:10.1021/bi002239y · Cited by 380 · see citing works
Apoptosis by cisplatin requires p53 mediated p38α MAPK activation through ROS generation
Bragado, P., Armesilla, A., Silva, A., & Porras, A. (2007) · Apoptosis · doi:10.1007/s10495-007-0082-8 · Cited by 377 · see citing works
Rhee, S. G., Yang, K.-S., Kang, S. W., Woo, H. A., & Chang, T.-S. (2005) · Antioxidants & Redox Signaling · doi:10.1089/ars.2005.7.619 · Cited by 376 · see citing works
Nrf2: A Potential Molecular Target for Cancer Chemoprevention by Natural Compounds
Jeong, W., Jun, M., & Kong, A. T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.99 · Cited by 371 · see citing works
NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response?
Schopfer, F. J. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.006 · Cited by 369 · see citing works
Role of Oxidant Species in Aging
Stadtman, E. R. (2004) · Current Medicinal Chemistry · doi:10.2174/0929867043365341 · Cited by 368 · cited 1× · see citing works
“Reversible oxidation of the sulfhydryl group includes intramolecular or intermolecular protein cross-linkages and glutathionylation (287).”
Reactive oxygen species mediate crosstalk between NF-κB and JNK
Nakano, H., Nakajima, A., Sakon-Komazawa, S., Piao, J.-H., Xue, X., & Okumura, K. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401830 · Cited by 367 · see citing works
Shaping Genetic Alterations in Human Cancer: The p53 Mutation Paradigm
Soussi, T., & Wiman, K. G. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.10.001 · Cited by 366 · see citing works
Motohashi, H., Katsuoka, F., Engel, J. D., & Yamamoto, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305902101 · Cited by 363 · see citing works
Glutathione peroxidases and redox-regulated transcription factors
Brigelius‐Flohé, R. (2006) · Biological Chemistry · doi:10.1515/bc.2006.166 · Cited by 361 · see citing works
Reactive oxygen species and the mitochondrial signaling pathway of cell death.
Bras, M. L., Clément, M.-V., Pervaiz, S., & Brenner, C. (2005) · PubMed · doi:10.14670/hh-20.205 · Cited by 359 · see citing works
Gotoh, Y., & Cooper, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.28.17477 · Cited by 355 · see citing works
(2003) · PubMed · Cited by 350 · see citing works
p53 Suppresses the Nrf2-dependent Transcription of Antioxidant Response Genes
Faraonio, R., Vergara, P., Marzo, D. D., Pierantoni, G. M., Napolitano, M., Russo, T., & Cimino, F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605707200 · Cited by 350 · see citing works
Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.06.007 · Cited by 349 · see citing works
Signalling hypoxia by HIF hydroxylases
Schofield, C. J., & Ratcliffe, P. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.111 · Cited by 343 · see citing works
Chinery, R., Brockman, J. A., Peeler, M. O., Shyr, Y., Beauchamp, R. D., & Coffey, R. J. (1997) · Nature Medicine · doi:10.1038/nm1197-1233 · Cited by 334 · see citing works
The BCR/ABL Tyrosine Kinase Induces Production of Reactive Oxygen Species in Hematopoietic Cells
Sattler, M., Verma, S., Shrikhande, G., Byrne, C. H., Pride, Y. B., Winkler, T., Greenfield, E. A., Salgia, R., & Griffin, J. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002094200 · Cited by 323 · see citing works
Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention
Hayes, J. D. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00695-4 · Cited by 323 · see citing works
Phosphoinositide 3‐kinase‐dependent activation of Rac
Welch, H. C. E., Coadwell, W. J., Stephens, L., & Hawkins, P. T. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00454-x · Cited by 320 · see citing works
Essential role of RelA Ser311 phosphorylation by ζPKC in NF‐κB transcriptional activation
Duran, A., Díaz-Meco, M. T., & Moscat, J. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg370 · Cited by 319 · see citing works
Breitschopf, K., Haendeler, J., Malchow, P., Zeiher, A. M., & Dimmeler, S. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1886-1896.2000 · Cited by 319 · see citing works
Hsp72 functions as a natural inhibitory protein of c‐Jun N‐terminal kinase
Park, H.-S., Lee, J., Huh, S., Seo, J., & Choi, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.446 · Cited by 317 · see citing works
Mottet, D., Dumont, V., Deccache, Y., Demazy, C., Ninane, N., Raes, M. J., & Michiels, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300763200 · Cited by 316 · see citing works
Rescue of cells from apoptosis by inhibition of active GSH extrusion
Ghibelli, L., Fanelli, C., Rotilio, G., Lafavia, E., Coppola, S., Colussi, C., Civitareale, P., & Ciriolo, M. R. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.6.479 · Cited by 314 · see citing works
Wang, T., Arifoglu, P., Ronai, Z. A., & Tew, K. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101355200 · Cited by 313 · see citing works
Functions and Mechanisms of Redox Regulation of Cysteine-Based Phosphatases
Salmeen, A. E., & Barford, D. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.560 · Cited by 312 · see citing works
The phosphatidyl inositol 3-kinase signaling network: implications for human breast cancer
Dillon, R. L., White, D. E., & Muller, W. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210202 · Cited by 311 · see citing works
Aylon, Y., & Oren, M. (2007) · Cell · doi:10.1016/j.cell.2007.08.005 · Cited by 311 · see citing works
Translational Control and the Unfolded Protein Response
Wek, R. C., & Cavener, D. R. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1764 · Cited by 305 · see citing works
Bensaad, K., & Vousden, K. H. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.04.004 · Cited by 305 · see citing works
Glutaredoxin Exerts an Antiapoptotic Effect by Regulating the Redox State of Akt*
Murata, H., Ihara, Y., Nakamura, H., Yodoi, J., Sumikawa, K., & Kondo, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310171200 · Cited by 304 · see citing works
Redox-Sensitive Kinases of the Nuclear Factor-κB Signaling Pathway
Pantano, C., Reynaert, N., van der Vliet, A., & Janssen-Heininger, Y. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1791 · Cited by 302 · see citing works
Shaulian, E., Schreiber, M., Piu, F., Beeche, M., Wagner, E. F., & Karin, M. (2000) · Cell · doi:10.1016/s0092-8674(00)00193-8 · Cited by 297 · see citing works
Redox regulation of cell signalling
Lander, H. M., MILBANK, A. J., Tauras, J. M., Hajjar, D. P., Hempstead, B. L., Schwartz, G. D., Kraemer, R. T., Mirza, U. A., Chait, B. T., Campbell, S. L., et al. (1996) · Nature · doi:10.1038/381380a0 · Cited by 297 · see citing works
Novel Role for JNK as a Stress-activated Bcl2 Kinase
Deng, X., Xiao, L., Lang, W., Gao, F., Ruvolo, P. P., & May, W. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100279200 · Cited by 296 · see citing works
Reactive oxygen species in the control of hypoxia-inducible factor-mediated gene expression
Kietzmann, T., & Görlach, A. (2005) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2005.03.010 · Cited by 295 · see citing works
Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in response to oxidative stress
Morita, K., Saitoh, M., Tobiume, K., Matsuura, H., Enomoto, S., Nishitoh, H., & Ichijo, H. (2001) · The EMBO Journal · doi:10.1093/emboj/20.21.6028 · Cited by 293 · see citing works
Nuclear Factor-κB in Development, Prevention, and Therapy of Cancer
Waes, C. V. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2221 · Cited by 293 · see citing works
Holmgren, A., & Åslund, F. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52031-7 · Cited by 292 · see citing works
Tanaka, H., Matsumura, I., Ezoe, S., Satoh, Y., Sakamaki, T., Albanese, C., Machii, T., Pestell, R. G., & Kanakura, Y. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00522-1 · Cited by 289 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach?
Trachootham, D., Alexandre, J., & Huang, P. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2803 · Cited by 5,452 · see citing works
Self-citationNRF2 and the Hallmarks of Cancer
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
Anoikis molecular pathways and its role in cancer progression
Paoli, P., Giannoni, E., & Chiarugi, P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.026 · Cited by 1,160 · see citing works
Molecular mechanisms of ROS production and oxidative stress in diabetes
Newsholme, P., Cruzat, V. F., Keane, K. N., Carlessi, R., & de Bittencourt, P. I. H. (2016) · Biochemical Journal · doi:10.1042/bcj20160503c · Cited by 878 · see citing works
Regulation of μ-opioid receptors: desensitization, phosphorylation, internalization, and tolerance
Williams, J. T., Ingram, S. L., Henderson, G., Chavkin, C., von Zastrow, M., Schulz, S., Koch, T., Evans, C. J., & Christie, M. J. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.005942 · Cited by 802 · see citing works
Neutrophils to the ROScue: Mechanisms of NADPH oxidase activation and bacterial resistance
Nguyen, G. T., Green, E. R., & Mecsas, J. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00373 · Cited by 741 · see citing works
Taking a good look at free radicals in the aging process
Hekimi, S., Lapointe, J., & Wen, Y. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.06.008 · Cited by 606 · see citing works
Genetics and biology of pancreatic ductal adenocarcinoma
Ying, H., Dey, P., Yao, W., Kimmelman, A. C., Draetta, G. F., Maitra, A., & DePinho, R. A. (2016) · Genes & Development · doi:10.1101/gad.275776.115 · Cited by 527 · see citing works
Redox-Directed Cancer Therapeutics: Molecular Mechanisms and Opportunities
Wondrak, G. T. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2541 · Cited by 462 · see citing works
The role of androgens and estrogens on healthy aging and longevity
Horstman, A. M., Dillon, E. L., Urban, R. J., & Sheffield-Moore, M. (2012) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/gls068 · Cited by 396 · see citing works
NRF2 Promotes Tumor Maintenance by Modulating mRNA Translation in Pancreatic Cancer
Chio, I. I. C., Jafarnejad, S. M., Ponz-Sarvise, M., Park, Y., Rivera, K., Palm, W., Wilson, J., Sangar, V., Hao, Y., Öhlund, D., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.056 · Cited by 378 · see citing works
“Although oxidative stress may disrupt biological functions, redox reactions in a cell are often tightly regulated and play essential physiological roles (Trachootham et al., 2008).”
Oxidative stress and calcium dysregulation by palmitate in type 2 diabetes
Ly, L. D., Xu, S., Choi, S.-K., Ha, C.-M., Thoudam, T., Cha, S.-K., Wiederkehr, A., Wollheim, C. B., Lee, I.-K., & Park, K.-S. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.157 · Cited by 378 · see citing works
Oxidative DNA damage is epigenetic by regulating gene transcription via base excision repair
Fleming, A. M., Ding, Y., & Burrows, C. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1619809114 · Cited by 364 · see citing works
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works
Biochemical basis and metabolic interplay of redox regulation
Zhang, L., Wang, X., Cueto, R., Effi, C., Zhang, Y., Tan, H., Qin, X., Ji, Y., Yang, X., & Wang, H. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101284 · Cited by 308 · see citing works
The Role of Oxidative Stress in Skeletal Muscle Myogenesis and Muscle Disease
Lian, D., Chen, M.-M., Wu, H., Deng, S., & Hu, X. (2022) · Antioxidants · doi:10.3390/antiox11040755 · Cited by 232 · see citing works
4-Hydroxynonenal in the Pathogenesis and Progression of Human Diseases
Shoeb, M., Ansari, N., Srivastava, S., & Ramana, K. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113209990181 · Cited by 230 · see citing works
Redox interplay between mitochondria and peroxisomes
Lismont, C., Nordgren, M., Van Veldhoven, P. P., & Fransen, M. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00035 · Cited by 214 · 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
Yoshida, S., Miyagawa, S., Fukushima, S., Kawamura, T., Kashiyama, N., Ohashi, F., Toyofuku, T., Toda, K., & Sawa, Y. (2018) · Molecular Therapy · doi:10.1016/j.ymthe.2018.08.012 · Cited by 178 · see citing works
Oxidative and antioxidative mechanisms in oral cancer and precancer: A review
Choudhari, S. K., Chaudhary, M., Gadbail, A. R., Sharma, A., & Tekade, S. (2014) · Oral Oncology · doi:10.1016/j.oraloncology.2013.09.011 · Cited by 177 · see citing works
VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress
Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170 · see citing works
Matsa, E., Burridge, P. W., Yu, K.-H., Ahrens, J. H., Termglinchan, V., Wu, H., Liu, C., Shukla, P., Sayed, N., Churko, J. M., et al. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.07.006 · Cited by 164 · see citing works
Hu, H., Zhong, D., Li, W., Lin, X., He, J., Sun, Y., Wu, Y., Shi, M., Chen, X., Xu, F., et al. (2022) · Nano Today · doi:10.1016/j.nantod.2021.101368 · Cited by 165 · see citing works
A model of the mitochondrial basis of bipolar disorder
Morris, G., Walder, K., McGee, S. L., Dean, O. M., Tye, S. J., Maes, M., & Berk, M. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.01.014 · Cited by 162 · see citing works
Ncf1 polymorphism reveals oxidative regulation of autoimmune chronic inflammation
Holmdahl, R., Sareila, O., Olsson, L. M., Bäckdahl, L., & Wing, K. (2016) · Immunological Reviews · doi:10.1111/imr.12378 · Cited by 131 · see citing works
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works
Ju, H.-Q., Gocho, T., Aguilar, M., Wu, M., Zhuang, Z.-N., Fu, J., Yanaga, K., Huang, P., & Chiao, P. J. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0420 · Cited by 137 · see citing works
Self-citationPrecision Redox: The Key for Antioxidant Pharmacology
Meng, J., Lv, Z., Zhang, Y., Wang, Y., Qiao, X., Sun, C., Chen, Y., Guo, M., Han, W., Ye, A., et al. (2021) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8212 · Cited by 122 · see citing works
Li, X., Zhu, F., Jiang, J., Sun, C., Wang, X., Shen, M., Tian, R., Shi, C., Xu, M., Peng, F., et al. (2015) · Cancer Letters · doi:10.1016/j.canlet.2014.11.026 · Cited by 116 · see citing works
Nrf2 activation by tauroursodeoxycholic acid in experimental models of Parkinson's disease
Moreira, S., Fonseca, I., Nunes, M. J., Rosa, A., Lemos, L., Rodrigues, E., Carvalho, A. N., Outeiro, T. F., Rodrigues, C. M. P., Gama, M. J., et al. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.05.009 · Cited by 112 · see citing works
Kim, S., You, D. H., Han, T., & Choi, E.-M. (2014) · Journal of Photochemistry and Photobiology B: Biology · doi:10.1016/j.jphotobiol.2014.10.012 · Cited by 49 · see citing works
Gole, H. K. A., Tharp, D. L., & Bowles, D. K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105337 · Cited by 36 · see citing works
Chaisiriwong, L., Wanitphakdeedecha, R., Sitthinamsuwan, P., Sampattavanich, S., Chatsiricharoenkul, S., Manuskiatti, W., & Panich, U. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/5934024 · Cited by 20 · see citing works
- Authors
- Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P.
- Affiliations
- Thammasat University (TH)
- The University of Texas MD Anderson Cancer Center (US)
- Corresponding author
- Huang, Peng
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2008-08
- Volume
- 10
- Issue
- 8
- Pages
- 1343-1374
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC2932530
- OpenAlex
- W2062845561
- Cited by
- 1,781
- References
- 354
- Citations by year
- 2026: 50 · 2025: 83 · 2024: 79 · 2023: 115 · 2022: 112 · 2021: 134 · 2020: 112 · 2019: 101 · 2018: 130 · 2017: 153 · 2016: 148 · 2015: 115 · 2014: 129 · 2013: 102 · 2012: 73
- FWCI
- 3.71
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (CA085563, R01CA109041, CA109041, R01CA085563, R01CA100428, CA100428)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- redox regulation, cell survival, reactive oxygen species, reactive nitrogen species, redox homeostasis, oxidative stress, cell death, NF-κB, AP-1, Nrf2, hypoxia-inducible factor, MAPK signaling, PI3K/Akt signaling, caspases, Bcl-2, cytochrome c, mitochondrial apoptosis, transcriptional regulation, protein oxidation
- MeSH terms
- Animals, Cell Survival, Homeostasis, Humans, Models, Biological, Oxidation-Reduction, Signal Transduction, Reactive Oxygen Species, Reactive Nitrogen 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