ROS function in redox signaling and oxidative stress

Schieber, Michael; Chandel, Navdeep S.

doi:10.1016/j.cub.2014.03.034

Cited by 6,931Redox biology and oxidative stressAntioxidant Activity and Oxidative StressNitric Oxide and Endothelin Effects

ROS function in redox signaling and oxidative stress

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Schieber, Michael, Chandel, Navdeep S.·2014·Current Biology

DOI 10.1016/j.cub.2014.03.034PMC PMC4055301

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Abstract

Oxidative stress refers to elevated intracellular levels of reactive oxygen species (ROS) that cause damage to lipids, proteins and DNA. Oxidative stress has been linked to a myriad of pathologies. However, elevated ROS also act as signaling molecules in the maintenance of physiological functions--a process termed redox biology. In this review we discuss the two faces of ROS--redox biology and oxidative stress--and their contribution to both physiological and pathological conditions. Redox biology involves a small increase in ROS levels that activates signaling pathways to initiate biological processes, while oxidative stress denotes high levels of ROS that result in damage to DNA, protein or lipids. Thus, the response to ROS displays hormesis, given that the opposite effect is observed at low levels compared with that seen at high levels. Here, we argue that redox biology, rather than oxidative stress, underlies physiological and pathological conditions.

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The negative effects of air pollution are primarily mediated by the production of reactive oxygen species.
“The negative effects of air pollution are primarily mediated by the production of reactive oxygen species (ROS)14.”
From Air Pollution and Skin Diseases (2025) · cites this paper as [14]
The Introduction says ROS can cause pathology by damaging lipids, proteins, and DNA. It does not link ROS production to air pollution or establish that ROS primarily mediate air pollution’s negative effects (searched: air pollution, pollutants, particulate matter). (LLM, conf=0.82)
Experimental — accuracy not yet measured
Activated macrophages and microglia release ROS that disrupt cell membranes, cellular DNA, and protein synthesis.
“Activated macrophages and microglia release ROS that disrupt cell membranes, cellular DNA, and protein synthesis (101).”
From Chronic stress, neuroinflammation, and depression: an overview of pathophysiological mechanisms and emerging anti-inflammatories (2023) · cites this paper as [101]
The Introduction says ROS can damage lipids, proteins, and DNA, and the ‘Regulation of inflammation’ section links macrophage activity to ROS generation and notes that elevated ROS in immune cells can contribute to tissue damage. The paper does not establish that activated macrophages release ROS that cause the specified damage; it does not address microglia or disruption of protein synthesis. The relevant passages have no page numbers in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measured
When ROS generation surpasses the skin's antioxidant defenses, it results in oxidative stress, which can impair lipids, proteins, and DNA, disrupting cellular organelles and tissue functions.
“When ROS generation surpasses the skin’s antioxidant defenses, it results in oxidative stress, a condition that can impair lipids, proteins, and DNA, thereby, disrupting various cellular organelles and tissue functions (Fig. 2)14.”
From Air Pollution and Skin Diseases (2025) · cites this paper as [14]
The Introduction says oxidative stress involves ROS damage to lipids, proteins, and DNA, and the regulation-of-aging section describes damaged mitochondria impairing cellular function. The cited passages do not establish the claim’s skin-specific threshold—ROS generation surpassing the skin’s antioxidant defenses—or the resulting disruption of skin tissue function. (LLM, conf=0.84)
Experimental — accuracy not yet measured
ROS accumulation causes oxidative stress that can damage lipids, proteins, and ribonucleic acids.
“ROS accumulation causes oxidative stress that can damage lipids, proteins, and ribonucleic acids10.”
From Key points for the development of antioxidant cocktails to prevent cellular stress and damage caused by reactive oxygen species (ROS) during manned space missions (2021) · cites this paper as [10]
The Abstract and Introduction say elevated ROS can cause oxidative stress that damages lipids, proteins, and DNA. The claim matches the first two targets but substitutes ribonucleic acids (RNA) for DNA; the cited passages do not support that substitution. (LLM, conf=0.90)
Experimental — accuracy not yet measured
Compared with normal cells, cancer cells usually face greater oxidative stress due to faster metabolism and faulty mitochondria.
“cancer cells experience more oxidative stress compared with normal cells owing to an elevated metabolic rate and defective mitochondria12”
From Targeting cancer vulnerabilities with high-dose vitamin C (2019) · cites this paper as [12]

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Chen, C., Liu, Y., Liu, R., Ikenoue, T., Guan, K.-L., Liu, Y., & Zheng, P. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20081297 · Cited by 682 · see citing works
Mitochondrial Complex III ROS Regulate Adipocyte Differentiation
Tormos, K. V., Ansó, E., Hamanaka, R. B., Eisenbart, J. D., Joseph, J., Kalyanaraman, B., & Chandel, N. S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.007 · Cited by 662 · see citing works
Self-citation
Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., & Rhee, S. G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407396101 · Cited by 631 · see citing works
A Mitochondrial Superoxide Signal Triggers Increased Longevity in Caenorhabditis elegans
Yang, W., & Hekimi, S. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000556 · Cited by 630 · see citing works
Redox regulation of PI 3‐kinase signalling via inactivation of PTEN
Leslie, N. R., Bennett, D., Lindsay, Y. E., Stewart, H., Gray, A., & Downes, C. P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg513 · Cited by 614 · see citing works
Inactivation of Peroxiredoxin I by Phosphorylation Allows Localized H2O2 Accumulation for Cell Signaling
Woo, H. A., Yim, S. H., Shin, D. H., Kang, D., Yu, D., & Rhee, S. G. (2010) · Cell · doi:10.1016/j.cell.2010.01.009 · Cited by 613 · see citing works
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
Disruption of Nrf2 enhances susceptibility to severe airway inflammation and asthma in mice
Rangasamy, T., Guo, J., Mitzner, W. A., Roman, J., Singh, A., Fryer, A. D., Yamamoto, M., Kensler, T. W., Tuder, R. M., Georas, S. N., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050538 · Cited by 580 · see citing works
Absence of autophagy results in reactive oxygen species-dependent amplification of RLR signaling
Tal, M. C., Sasai, M., Lee, H. K., Yordy, B., Shadel, G. S., & Iwasaki, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807694106 · Cited by 573 · see citing works
The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
Bell, E. L., Klimova, T. A., Eisenbart, J., Moraes, C. T., Murphy, M. P., Budinger, G. R. S., & Chandel, N. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609074 · Cited by 568 · see citing works
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Role of Oxidants in NF-κB Activation and TNF-α Gene Transcription Induced by Hypoxia and Endotoxin
Chandel, N. S., Trzyna, W., McClintock, D. S., & Schumacker, P. T. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.2.1013 · Cited by 536 · see citing works
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HIF-Dependent Antitumorigenic Effect of Antioxidants In Vivo
Gao, P., Zhang, H., Dinavahi, R., Li, F., Xiang, Y., Raman, V., Bhujwalla, Z. M., Felsher, D. W., Cheng, L., Pevsner, J., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.08.004 · Cited by 523 · see citing works
Deletion of the mitochondrial superoxide dismutase sod-2 extends lifespan in Caenorhabditis elegans
Van Raamsdonk, J. M., & Hekimi, S. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000361 · Cited by 511 · see citing works
Inhibition of Respiration Extends C. elegans Life Span via Reactive Oxygen Species that Increase HIF-1 Activity
Lee, S., Hwang, A. B., & Kenyon, C. J. (2010) · Current Biology · doi:10.1016/j.cub.2010.10.057 · Cited by 495 · see citing works
Bmi1 regulates mitochondrial function and the DNA damage response pathway
Liu, J., Cao, L., Chen, J., Song, S., Lee, I. H., Quijano, C., Liu, H., Keyvanfar, K., Chen, H., Cao, L.-Y., et al. (2009) · Nature · doi:10.1038/nature08040 · Cited by 474 · see citing works
SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production
Bell, E. L., Emerling, B. M., Ricoult, S. J. H., & Guarente, L. (2011) · Oncogene · doi:10.1038/onc.2011.37 · Cited by 440 · see citing works
ATM activates the pentose phosphate pathway promoting anti‐oxidant defence and DNA repair
Cosentino, C., Grieco, D., & Costanzo, V. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.330 · Cited by 436 · see citing works
Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal
Zarse, K., Schmeisser, S., Groth, M., Priebe, S., Beuster, G., Kuhlow, D., Guthke, R., Platzer, M., Kahn, C. R., & Ristow, M. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.02.013 · Cited by 430 · see citing works
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
Low oxygen concentration extends the lifespan of cultured human diploid cells
Packer, L., & FUEHR, K. (1977) · Nature · doi:10.1038/267423a0 · Cited by 393 · see citing works
Perinuclear Mitochondrial Clustering Creates an Oxidant-Rich Nuclear Domain Required for Hypoxia-Induced Transcription
Al‐Mehdi, A., Pastukh, V. M., Swiger, B. M., Reed, D., Patel, M., Bardwell, G. C., Pastukh, V. V., ALEXEYEV, M. F., & Gillespie, M. N. (2012) · Science Signaling · doi:10.1126/scisignal.2002712 · Cited by 386 · see citing works
The overexpression of major antioxidant enzymes does not extend the lifespan of mice
Pérez, V. I., Van Remmen, H., Bokov, A., Epstein, C. J., Vijg, J., & Richardson, A. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2008.00449.x · Cited by 353 · see citing works
Evolutionary conservation of the clk-1 -dependent mechanism of longevity: loss of mclk1 increases cellular fitness and lifespan in mice
Liu, X., Jiang, N., Hughes, B., Bigras, E., Shoubridge, E., & Hekimi, S. (2005) · Genes & Development · doi:10.1101/gad.1352905 · Cited by 345 · see citing works
Prdx1 inhibits tumorigenesis via regulating PTEN/AKT activity
Cao, J., Schulte, J., Knight, A., Leslie, N. R., Zagożdżon, A., Bronson, R. T., Manevich, Y., Beeson, C. C., & Neumann, C. A. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.101 · Cited by 344 · see citing works
Mitochondrial Thiols in Antioxidant Protection and Redox Signaling: Distinct Roles for Glutathionylation and Other Thiol Modifications
Murphy, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4289 · Cited by 338 · see citing works
Mechanisms that Regulate Stem Cell Aging and Life Span
Signer, R. A. J., & Morrison, S. J. (2013) · Cell Stem Cell · doi:10.1016/j.stem.2013.01.001 · Cited by 320 · see citing works
Mitochondrial reactive oxygen species promote epidermal differentiation and hair follicle development
Hamanaka, R. B., Glasauer, A., Hoover, P., Yang, S., Blatt, H., Mullen, A. R., Getsios, S., Gottardi, C. J., DeBerardinis, R. J., Lavker, R. M., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2003638 · Cited by 315 · see citing works
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Regulation of Yeast Chronological Life Span by TORC1 via Adaptive Mitochondrial ROS Signaling
Pan, Y., Schroeder, E. A., Ocampo, A., Barrientos, A., & Shadel, G. S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.018 · Cited by 313 · see citing works
The Proto-oncometabolite Fumarate Binds Glutathione to Amplify ROS-Dependent Signaling
Sullivan, L. B., Martinez-Garcia, E., Nguyen, H., Mullen, A. R., Dufour, E., Sudarshan, S., Licht, J. D., Deberardinis, R. J., & Chandel, N. S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.003 · Cited by 304 · see citing works
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Measuring EGSH and H2O2 with roGFP2-based redox probes
Morgan, B., Sobotta, M. C., & Dick, T. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.035 · Cited by 295 · see citing works
The Permeability Transition Pore Controls Cardiac Mitochondrial Maturation and Myocyte Differentiation
Hom, J., Quintanilla, R. A., Hoffman, D. L., Bentley, K. L. D. M., Molkentin, J. D., Sheu, S., & Porter, G. A., Jr. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.08.008 · Cited by 293 · see citing works
AKT1 and AKT2 maintain hematopoietic stem cell function by regulating reactive oxygen species
Juntilla, M. M., Patil, V. D., Calamito, M., Joshi, R. P., Birnbaum, M. J., & Koretzky, G. A. (2010) · Blood · doi:10.1182/blood-2009-09-241000 · Cited by 284 · see citing works
Caloric restriction or catalase inactivation extends yeast chronological lifespan by inducing H 2 O 2 and superoxide dismutase activity
Mesquita, A., Weinberger, M., Silva, A., Sampaio‐Marques, B., Almeida, B., Leão, C., Costa, V., Rodrigues, F. J. S., Burhans, W. C., & Ludovico, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004432107 · Cited by 268 · see citing works
Unravelling the tumor-suppressive functions of FOXO proteins
Dansen, T. B., & Burgering, B. M. T. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.07.004 · Cited by 267 · see citing works
Mitochondrial Reactive Oxygen Species Control T Cell Activation by Regulating IL-2 and IL-4 Expression: Mechanism of Ciprofloxacin-Mediated Immunosuppression
Kamiński, M. M., Sauer, S. W., Klemke, C., Süss, D., Okun, J. G., Krammer, P. H., & Gülow, K. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0901662 · Cited by 253 · see citing works
Mitochondrial H2O2 Regulates the Angiogenic Phenotype via PTEN Oxidation
Connor, K. M., Subbaram, S., Regan, K. J., Nelson, K. K., Mazurkiewicz, J. E., Bartholomew, P. J., Aplin, A. E., Tai, Y.-T., Aguirre-Ghiso, J., Flores, S. C., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410690200 · Cited by 251 · see citing works
ROS Are Required for Mouse Spermatogonial Stem Cell Self-Renewal
Morimoto, H., Iwata, K., Ogonuki, N., Inoue, K., Ogura, A., Kanatsu‐Shinohara, M., Morimoto, T., Yabe‐Nishimura, C., & Shinohara, T. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.04.001 · Cited by 246 · see citing works
Mitochondrial localization of TIGAR under hypoxia stimulates HK2 and lowers ROS and cell death
Cheung, E. C., Ludwig, R. L., & Vousden, K. H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206530109 · Cited by 244 · see citing works
Somatic Progenitor Cell Vulnerability to Mitochondrial DNA Mutagenesis Underlies Progeroid Phenotypes in Polg Mutator Mice
Ahlqvist, K. J., Hämäläinen, R. H., Yatsuga, S., Uutela, M., Terzioglu, M., Götz, A., Forsström, S., Salvén, P., Angers‐Loustau, A., Kopra, O., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.11.012 · Cited by 240 · see citing works
Mitochondrial reactive oxygen species trigger hypoxia-inducible factor-dependent extension of the replicative life span during hypoxia
Bell, E. L., Klimova, T. A., Eisenbart, J., Schumacker, P. T., & Chandel, N. S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02265-06 · Cited by 237 · see citing works
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Role of sirtuins in lifespan regulation is linked to methylation of nicotinamide
Schmeisser, K., Mansfeld, J., Kuhlow, D., Weimer, S., Priebe, S., Heiland, I., Birringer, M., Groth, M., Segref, A., Kanfi, Y., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1352 · Cited by 236 · see citing works
Selective killing of K-ras mutant cancer cells by small molecule inducers of oxidative stress
Shaw, A. T., Winslow, M. M., Magendantz, M., Ouyang, C., Dowdle, J. A., Subramanian, A., Lewis, T. A., Maglathin, R. L., Tolliday, N. J., & Jacks, T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105941108 · Cited by 229 · see citing works
Prdm16 promotes stem cell maintenance in multiple tissues, partly by regulating oxidative stress
Chuikov, S., Levi, B. P., Smith, M. L., & Morrison, S. J. (2010) · Nature Cell Biology · doi:10.1038/ncb2101 · Cited by 224 · see citing works
Enhancing Nrf2 Pathway by Disruption of Keap1 in Myeloid Leukocytes Protects against Sepsis
Kong, X., Thimmulappa, R. K., Craciun, F. L., Harvey, C. J., Singh, A., Kombairaju, P., Reddy, S. P., Remick, D. G., & Biswal, S. S. (2011) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201102-0271oc · Cited by 223 · see citing works
Targeting SOD1 reduces experimental non–small-cell lung cancer
Glasauer, A., Sena, L. A., Diebold, L. P., Mazar, A. P., & Chandel, N. S. (2013) · Journal of Clinical Investigation · doi:10.1172/jci71714 · Cited by 212 · see citing works
Self-citation
The strength of receptor signaling is centrally controlled through a cooperative loop between Ca2+ and an oxidant signal
Singh, D. K., Kumar, D., Siddiqui, Z., Basu, S. K., Kumar, V., & Rao, K. V. S. (2005) · Cell · doi:10.1016/j.cell.2005.02.036 · Cited by 206 · see citing works
Mice Deficient in Both Mn Superoxide Dismutase and Glutathione Peroxidase-1 Have Increased Oxidative Damage and a Greater Incidence of Pathology but No Reduction in Longevity
Zhang, Y., Ikeno, Y., Qi, W., Chaudhuri, A., Li, Y., Bokov, A., Thorpe, S. R., Baynes, J., Epstein, C. J., Richardson, A. G., et al. (2009) · The Journals of Gerontology Series A · doi:10.1093/gerona/glp132 · Cited by 206 · see citing works
Negative feedback control of HIF-1 through REDD1-regulated ROS suppresses tumorigenesis
Horak, P., Crawford, A. R., Vadysirisack, D. D., Nash, Z. M., DeYoung, M. P., Sgroi, D. C., & Ellisen, L. W. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907705107 · Cited by 201 · see citing works
Mitochondrial Stress Engages E2F1 Apoptotic Signaling to Cause Deafness
Raimundo, N., Song, L., Shutt, T. E., McKay, S. E., Cotney, J. L., Guan, M., Gilliland, T., Hohuan, D., Santos‐Sacchi, J., & Shadel, G. S. (2012) · Cell · doi:10.1016/j.cell.2011.12.027 · Cited by 189 · see citing works
Reactive Oxygen Species and Aging in Caenorhabditis elegans : Causal or Casual Relationship?
Raamsdonk, J. M. V., & Hekimi, S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3215 · Cited by 184 · see citing works
PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease
Wishart, M. J., & Dixon, J. E. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(02)02412-1 · Cited by 182 · see citing works
Prolonged Production of Reactive Oxygen Species in Response to B Cell Receptor Stimulation Promotes B Cell Activation and Proliferation
Wheeler, M. L., & DeFranco, A. L. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201433 · Cited by 171 · see citing works
From Sulfenylation to Sulfhydration: What a Thiolate Needs to Tolerate
Finkel, T. (2012) · Science Signaling · doi:10.1126/scisignal.2002943 · Cited by 161 · see citing works
The ATM–BID pathway regulates quiescence and survival of haematopoietic stem cells
Maryanovich, M., Oberkovitz, G., Niv, H., Vorobiyov, L., Zaltsman, Y., Brenner, O. J., Lapidot, T., Jung, S., & Gross, A. (2012) · Nature Cell Biology · doi:10.1038/ncb2468 · Cited by 152 · see citing works
Mammalian SH2-Containing Protein Tyrosine Phosphatases
Adachi, M., Fischer, E. H., Ihle, J., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81077-6 · Cited by 149 · see citing works
Novel Role for Mitochondria: Protein Kinase Cθ-Dependent Oxidative Signaling Organelles in Activation-Induced T-Cell Death
Kamiński, M. M., Kießling, M. K., Süss, D., Krammer, P. H., & Gülow, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02295-06 · Cited by 139 · see citing works
Effect of antioxidants on primary alloantigen-induced T cell activation and proliferation
Chaudhri, G., Clark, I. A., Hunt, N. H., Cowden, W. B., & Ceredig, R. (1986) · The Journal of Immunology · doi:10.4049/jimmunol.137.8.2646 · Cited by 138 · cited 1× · see citing works
“Initial evidence for redox signaling in this process stemmed from the observations that treatment of primary T cells with pharmacological antioxidants inhibited proliferation and production of the cytokine interleukin-2 (IL-2) following T-cell receptor stimulation in vitro [91].”
Background
Mitochondrial Genome Instability and ROS Enhance Intestinal Tumorigenesis in APC Mice
Woo, D. K., Green, P. D., Santos, J. H., D’Souza, A. D., Walther, Z., Martin, W. D., Christian, B. E., Chandel, N. S., & Shadel, G. S. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.10.003 · Cited by 138 · see citing works
Self-citation
Elevated Mitochondrial Reactive Oxygen Species Generation Affects the Immune Response via Hypoxia-Inducible Factor-1α in Long-Lived Mclk1 +/− Mouse Mutants
Wang, D., Malo, D., & Hekimi, S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902352 · Cited by 123 · see citing works
Exploiting Thiol Modifications
Kiley, P. J., & Storz, G. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020400 · Cited by 111 · see citing works
Antitumorigenesis of antioxidants in a transgenic Rac1 model of Kaposi's sarcoma
Ma, Q., Cavallin, L. E., Yan, B., Zhu, S., Duran, E. M., Wang, H., Hale, L. P., Dong, C., Cesarman, E., Mesri, E. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812688106 · Cited by 105 · see citing works
Reversal of the Mitochondrial Phenotype and Slow Development of Oxidative Biomarkers of Aging in Long-lived Mclk1+/− Mice
Lapointe, J., Stepanyan, Z., Bigras, E., & Hekimi, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.006569 · Cited by 91 · see citing works
Effect of the NADPH Oxidase Inhibitor Apocynin on Septic Lung Injury in Guinea Pigs
Wang, W., Suzuki, Y., Tanigaki, T., et al. (1994) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.150.5.7952574 · Cited by 86 · see citing works
N-acetylcysteine for sepsis and systemic inflammatory response in adults
Szakmány, T., Hauser, B., & Radermacher, P. (2012) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd006616.pub2 · Cited by 82 · see citing works
Regulation of Mitochondrial Antiviral Signaling Pathways
Moore, C. B., & Ting, J. P. ‐. (2008) · Immunity · doi:10.1016/j.immuni.2008.05.005 · Cited by 82 · see citing works
Changes in mitochondrial reactive oxygen species synthesis during differentiation of skeletal muscle cells
Malińska, D., Kudin, A. P., Bejtka, M., & Kunz, W. S. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.06.015 · Cited by 73 · see citing works
Mitochondria as Oxidative Signaling Organelles in T-cell Activation: Physiological Role and Pathological Implications
Kamiński, M. M., Röth, D., Krammer, P. H., & Gülow, K. (2013) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-013-0235-0 · Cited by 72 · see citing works
Reducing Mitochondrial ROS Improves Disease-related Pathology in a Mouse Model of Ataxia-telangiectasia
D’Souza, A. D., Parish, I. A., Krause, D. S., Kaech, S. M., & Shadel, G. S. (2012) · Molecular Therapy · doi:10.1038/mt.2012.203 · Cited by 71 · see citing works
Rethinking the regulation of cellular metabolism
Thompson, C. B. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2012.76.010496 · Cited by 66 · see citing works
Antioxidant Treatment Reduces Expansion and Contraction of Antigen-Specific CD8+T Cells during Primary but Not Secondary Viral Infection
Laniewski, N. G., & Grayson, J. M. (2004) · Journal of Virology · doi:10.1128/jvi.78.20.11246-11257.2004 · Cited by 55 · see citing works
Reactive oxygen species delay control of lymphocytic choriomeningitis virus
Lang, P. A., Xu, H. C., Grusdat, M., McIlwain, D. R., Pandyra, A. A., Harris, I. S., Shaabani, N., Honke, N., Maney, S. K., Lang, E., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2012.167 · Cited by 51 · see citing works
Expression of multiple copies of mitochondrially targeted catalase or genomic Mn superoxide dismutase transgenes does not extend the life span of Drosophila melanogaster
Mockett, R. J., Sohal, B. H., & Sohal, R. S. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.029 · Cited by 48 · see citing works

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ROS Are Good
Mittler, R. (2017) · Trends in Plant Science · doi:10.1016/j.tplants.2016.08.002 · Cited by 3,499 · see citing works
Pathophysiology of type 2 diabetes mellitus
Galicia-Garcia, U., Benito-Vicente, A., Jebari, S., Larrea-Sebal, A., Siddiqi, H., Uribe, K. B., Ostolaza, H., & Martín, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176275 · Cited by 3,360 · see citing works
The multifaceted contributions of mitochondria to cellular metabolism
Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935 · see citing works
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
Sies, H., Belousov, V. V., Chandel, N. S., Davies, M. J., Jones, D. P., Mann, G. E., Murphy, M. P., Yamamoto, M., & Winterbourn, C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00456-z · Cited by 1,735 · see citing works
Self-citation
Supporting aspartate biosynthesis is an essential function of respiration in proliferating cells
Sullivan, L. B., Gui, D. Y., Hosios, A. M., Bush, L. N., Freinkman, E., & Vander Heiden, M. G. (2015) · Cell · doi:10.1016/j.cell.2015.07.017 · Cited by 1,173 · see citing works
Application of glutathione depletion in cancer therapy: Enhanced ROS-based therapy, ferroptosis, and chemotherapy
Niu, B., Liao, K., Zhou, Y., Wen, T., Quan, G., Pan, X., & Wu, C. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121110 · Cited by 1,168 · see citing works
ROS, Cell Senescence, and Novel Molecular Mechanisms in Aging and Age‐Related Diseases
Davalli, P., Mitic, T., Caporali, A., Lauriola, A., & D’Arca, D. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3565127 · Cited by 1,059 · see citing works
Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives
Hajam, Y. A., Rani, R., Ganie, S. Y., Sheikh, T. A., Javaid, D., Qadri, S. S., Pramodh, S., Alsulimani, A., Alkhanani, M. F., Harakeh, S., et al. (2022) · Cells · doi:10.3390/cells11030552 · Cited by 915 · see citing works
Mitochondrial stress induced by continuous stimulation under hypoxia rapidly drives T cell exhaustion
Scharping, N. E., Rivadeneira, D. B., Menk, A. V., Vignali, P. D. A., Ford, B. R., Rittenhouse, N. L., Peralta, R., Wang, Y., Wang, Y., DePeaux, K., et al. (2021) · Nature Immunology · doi:10.1038/s41590-020-00834-9 · Cited by 897 · see citing works
Oxidative stress: The core pathogenesis and mechanism of Alzheimer’s disease
Bai, R., Guo, J., Ye, X.-Y., Xie, Y., & Xie, T. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101619 · Cited by 813 · see citing works
Mitonuclear communication in homeostasis and stress
Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787 · see citing works
Neutrophils to the ROScue: Mechanisms of NADPH oxidase activation and bacterial resistance
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Authors: Schieber, M., & Chandel, N. S.
Affiliations: Northwestern University (US)
Corresponding author: Chandel, Navdeep S.
ORCID: Schieber, Michael
Chandel, Navdeep S.
Venue: Current Biology
Publisher: Elsevier BV
Published: 2014-05
Volume: 24
Issue: 10
Pages: R453-R462
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/j.cub.2014.03.034
PMC: PMC4055301
OpenAlex: W1976599392
Cited by: 6,931
References: 150
Citations by year: 2026: 613 · 2025: 810 · 2024: 782 · 2023: 676 · 2022: 815 · 2021: 789 · 2020: 693 · 2019: 619 · 2018: 468 · 2017: 309 · 2016: 198 · 2015: 124 · 2014: 27 · 2013: 1
FWCI: 20.65
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 383 d)
Locations: Current Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
National Heart, Lung, and Blood Institute (P01HL071643, T32-HL76139, T32HL076139)
National Cancer Institute (R01CA123067)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Keywords: reactive oxygen species, redox signaling, oxidative stress, redox biology, hormesis, lipid peroxidation, protein oxidation, DNA damage, signaling pathways
MeSH terms: Animals, DNA Damage, Humans, Oxidation-Reduction, Signal Transduction, Reactive Oxygen Species, Oxidative Stress, Cell Proliferation, Mice, Carcinogenesis

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