Reactive Oxygen Species in Metabolic and Inflammatory Signaling

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works

How mitochondria produce reactive oxygen species

Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works

Autophagy in the Pathogenesis of Disease

Levine, B., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2007.12.018 · Cited by 7,069 · see citing works

The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology

Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works

Chronic inflammation in fat plays a crucial role in the development of obesity-related insulin resistance

Xu, H., Barnes, G. T., Yang, Q., Tan, G., Yang, D., Chou, C. J., Sole, J., Nichols, A., Ross, J. S., Tartaglia, L. A., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200319451 · Cited by 6,760 · see citing works

Heart Disease and Stroke Statistics—2016 Update: A Report From the American Heart Association

Mozaffarian, D., Benjamin, E. J., Go, A. S., Arnett, D. K., Blaha, M. J., Cushman, M., Das, S. R., de Ferranti, S., Després, J.-P., Fullerton, H. J., et al. (2016) · Circulation · doi:10.1161/cir.0000000000000350 · Cited by 6,596 · see citing works

Lipid Peroxidation: Production, Metabolism, and Signaling Mechanisms of Malondialdehyde and 4-Hydroxy-2-Nonenal

Ayala, A., Muñoz, M., & Argüelles, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/360438 · Cited by 6,561 · see citing works

Beyond Cholesterol

Epstein, F. H., Steinberg, D. I., Parthasarathy, S., Carew, T. E., Khoo, J. C., & Witztum, J. L. (1989) · New England Journal of Medicine · doi:10.1056/nejm198904063201407 · Cited by 6,425 · see citing works

A role for mitochondria in nlrp3 inflammasome activation

Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602 · see citing works

Increased oxidative stress in obesity and its impact on metabolic syndrome

Furukawa, S., Fujita, T., Shimabukuro, M., Iwaki, M., Yamada, Y., Nakajima, Y., Nakayama, O., Makishima, M., Matsuda, M., & Shimomura, I. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21625 · Cited by 5,508 · see citing works

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · 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

Atherosclerosis

Lusis, A. J. (2000) · Nature · doi:10.1038/35025203 · Cited by 4,880 · see citing works

Cardiovascular Morbidity and Mortality Associated With the Metabolic Syndrome

Isomaa, B., Almgren, P., Tuomi, T., Forsén, B., Lahti, K., Nissén, M., Taskinen, M.-R., & Groop, L. (2001) · Diabetes Care · doi:10.2337/diacare.24.4.683 · Cited by 4,760 · see citing works

AMPK: a nutrient and energy sensor that maintains energy homeostasis

Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3311 · Cited by 4,602 · see citing works

Autophagy and Viruses: Adversaries or Allies?

Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,441 · see citing works

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,216 · see citing works

Succinate is an inflammatory signal that induces IL-1β through HIF-1α

Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176 · see citing works

HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia

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

Risk factors for ischaemic and intracerebral haemorrhagic stroke in 22 countries (the INTERSTROKE study): a case-control study

O'Donnell, M. J., Xavier, D., Liu, L., Zhang, H., Chin, S. L., Rao-Melacini, P., Rangarajan, S., Islam, S., Pais, P., McQueen, M. J., et al. (2010) · The Lancet · doi:10.1016/s0140-6736(10)60834-3 · Cited by 3,448 · see citing works

The AMPK signalling pathway coordinates cell growth, autophagy and metabolism

Mihaylova, M. M., & Shaw, R. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2329 · Cited by 2,923 · see citing works

Mechanisms linking obesity with cardiovascular disease

Van Gaal, L. F., Mertens, I. L., & De Block, C. E. (2006) · Nature · doi:10.1038/nature05487 · Cited by 2,814 · see citing works

Endoplasmic reticulum stress and the inflammatory basis of metabolic disease

Hotamisligil, G. S. (2010) · Cell · doi:10.1016/j.cell.2010.02.034 · Cited by 2,802 · see citing works

Mechanism and Regulation of NLRP3 Inflammasome Activation

He, Y., Hara, H., & Núñez, G. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.002 · Cited by 2,759 · see citing works

Thioredoxin-interacting protein links oxidative stress to inflammasome activation

Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708 · see citing works

Signal transduction by reactive oxygen species

Finkel, T. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102095 · Cited by 2,322 · see citing works

Succinate Dehydrogenase Supports Metabolic Repurposing of Mitochondria to Drive Inflammatory Macrophages

Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291 · see citing works

Mortality in Randomized Trials of Antioxidant Supplements for Primary and Secondary Prevention: Systematic Review and Meta-analysis

Bjelakovic, G., Nikolova, D., Gluud, L. L., Simonetti, R. G., & Gluud, C. (2007) · JAMA · doi:10.1001/jama.297.8.842 · Cited by 2,275 · see citing works

K+ Efflux Is the Common Trigger of NLRP3 Inflammasome Activation by Bacterial Toxins and Particulate Matter

Muñoz-Planillo, R., Kuffa, P., Martínez-Colón, G. J., Smith, B. L., Rajendiran, T. M., & Núñez, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.016 · Cited by 2,167 · see citing works

Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4

Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101 · see citing works

HIF-1α is essential for myeloid cell-mediated inflammation

Cramer, T., Yamanishi, Y., Clausen, B. E., Förster, I., Pawlinski, R., Mackman, N., Haase, V. H., Jaenisch, R., Corr, M., Nizet, V., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00154-5 · Cited by 2,046 · see citing works

Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases

Fukai, T., & Ushio‐Fukai, M. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3999 · Cited by 2,009 · see citing works

NF-κB, Inflammation, and Metabolic Disease

Baker, R. G., Hayden, M. S., & Ghosh, S. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2010.12.008 · Cited by 1,952 · see citing works

IKK-β links inflammation to obesity-induced insulin resistance

Arkan, M. C., Hevener, A. L., Greten, F. R., Maeda, S., Li, Z.-W., Long, J. M., Wynshaw-Boris, A., Poli, G., Olefsky, J., & Karin, M. (2005) · Nature Medicine · doi:10.1038/nm1185 · Cited by 1,773 · 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

Tlr signalling augments macrophage bactericidal activity through mitochondrial ros

West, A. P., Brodsky, I. E., Rahner, C., Woo, D. K., Erdjument-Bromage, H., Tempst, P., Walsh, M. C., Choi, Y., Shadel, G. S., & Ghosh, S. (2011) · Nature · doi:10.1038/nature09973 · Cited by 1,659 · see citing works

Beyond oxidative stress: an immunologist's guide to reactive oxygen species

Nathan, C., & Cunningham-Bussel, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3423 · Cited by 1,619 · see citing works

High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C--dependent activation of NAD(P)H oxidase in cultured vascular cells

Inoguchi, T., Li, P., Umeda, F., Yu, H. Y., Kakimoto, M., Imamura, M., Aoki, T., Etoh, T., Hashimoto, T., Naruse, M., et al. (2000) · Diabetes · doi:10.2337/diabetes.49.11.1939 · Cited by 1,577 · see citing works

Calcium and ROS: A mutual interplay

Görlach, A., Bertram, K., Hudecova, S., & Krizanova, O. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.010 · Cited by 1,546 · see citing works

NF-κB activation by reactive oxygen species: Fifteen years later

Gloire, G., Legrand-Poels, S., & Piette, J. G. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.04.011 · Cited by 1,540 · see citing works

Advanced Glycation End Products and Diabetic Complications

Singh, V. P., Bali, A., Singh, N., & Jaggi, A. S. (2014) · The Korean Journal of Physiology & Pharmacology · doi:10.4196/kjpp.2014.18.1.1 · Cited by 1,518 · see citing works

Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors

Vásquez-Vivar, J., Kalyanaraman, B., Martásek, P., Hogg, N., Masters, B. S. S., Karoui, H., Tordo, P., & Pritchard, K. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9220 · Cited by 1,484 · see citing works

Mitochondrial Dynamics Controls T Cell Fate through Metabolic Programming

Buck, M. D., O’Sullivan, D., Geltink, R. I. K., Curtis, J. D., Chang, C., Sanin, D. E., Qiu, J., Kretz, O., Braas, D., van der Windt, G. J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.035 · Cited by 1,444 · see citing works

Reactive Oxygen Species (Ros-Induced) Ros Release

Zorov, D. B., Filburn, C. R., Klotz, L.-O., Zweier, J. L., & Sollott, S. J. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.7.1001 · Cited by 1,412 · see citing works

Molecular mechanisms regulating NLRP3 inflammasome activation

Jo, E.-K., Kim, J. K., Shin, D.-M., & Sasakawa, C. (2016) · Cellular & Molecular Immunology · doi:10.1038/cmi.2015.95 · Cited by 1,378 · see citing works

Selective Mitochondrial Autophagy, or Mitophagy, as a Targeted Defense Against Oxidative Stress, Mitochondrial Dysfunction, and Aging

Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,342 · see citing works

Mitochondrial Dynamics and Metabolic Regulation

Wai, T., & Langer, T. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.12.001 · Cited by 1,304 · see citing works

Endoplasmic Reticulum Stress and Oxidative Stress in Cell Fate Decision and Human Disease

Cao, S. S., & Kaufman, R. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5851 · Cited by 1,304 · see citing works

Regulation of autophagy by ROS: physiology and pathology

Scherz-Shouval, R., & Elazar, Z. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.007 · Cited by 1,263 · see citing works

Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology

Yu, T., Robotham, J. L., & Yoon, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511154103 · Cited by 1,246 · see citing works

Protein degradation by the ubiquitin-proteasome pathway in normal and disease states

Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234 · see citing works

Inhibition of Pyruvate Kinase M2 by Reactive Oxygen Species Contributes to Cellular Antioxidant Responses

Anastasiou, D., Poulogiannis, G., Asara, J. M., Boxer, M. B., Jiang, J., Shen, M., Bellinger, G., Sasaki, A. T., Locasale, J. W., Auld, D. S., et al. (2011) · Science · doi:10.1126/science.1211485 · Cited by 1,196 · see citing works

Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis

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

Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes

Robertson, R. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400019200 · Cited by 1,078 · see citing works

Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE

Wautier, M., Chappey, O., Corda, S., Stern, D. M., Schmidt, A. M., & Wautier, J. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.5.e685 · Cited by 1,076 · see citing works

Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells

Marui, N., Offermann, M. K., Swerlick, R., Kunsch, C., Rosen, C. A., Ahmad, M., Alexander, R. W., & Medford, R. M. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116778 · Cited by 1,072 · see citing works

Antioxidant responses and cellular adjustments to oxidative stress

Espinosa-Diez, C., Miguel, V., Mennerich, D., Kietzmann, T., Sánchez-Pérez, P., Cadenas, S., & Lamas, S. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.008 · Cited by 1,046 · see citing works

Recent insights into the cellular biology of atherosclerosis

Tabas, I., García-Cardeña, G., & Owens, G. K. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201412052 · Cited by 1,016 · see citing works

Biochemistry of mammalian peroxisomes revisited

Wanders, R. J. A., & Waterham, H. R. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133329 · Cited by 995 · see citing works

Autophagy at the crossroads of catabolism and anabolism

Kaur, J., & Debnath, J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4024 · Cited by 993 · see citing works

Mitochondrial Glutathione, a Key Survival Antioxidant

Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · see citing works

Oxidative Stress and Its Role in the Pathogenesis of Ischaemic Stroke

Allen, C., & Bayraktutan, U. (2009) · International Journal of Stroke · doi:10.1111/j.1747-4949.2009.00387.x · Cited by 969 · see citing works

ROS, mitochondria and the regulation of autophagy

Scherz-Shouval, R., & Elazar, Z. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.009 · Cited by 954 · see citing works

NADPH oxidases: An overview from structure to innate immunity-associated pathologies

Panday, A., Sahoo, M. K., Osorio, D., & Batra, S. (2015) · Cellular & Molecular Immunology · doi:10.1038/cmi.2014.89 · Cited by 944 · see citing works

Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Lee, B., Lee, M. J., Park, S., Oh, D., Elsasser, S., Chen, P., Gartner, C. A., Dimova, N. V., Hanna, J. W., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 943 · see citing works

Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling

Forman, H. J., & Torres, M. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206007 · Cited by 891 · see citing works

The proteasome: overview of structure and functions

TANAKA, K. (2009) · Proceedings of the Japan Academy, Series B · doi:10.2183/pjab.85.12 · Cited by 862 · see citing works

Mechanisms of Mitochondrial Fission and FusionPreprint

van der Bliek, A. M., Shen, Q., & Kawajiri, S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011072 · Cited by 861 · see citing works

Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS)

Bulua, A. C., Simon, A., Maddipati, R., Pelletier, M., Park, H., Kim, K.-Y., Sack, M. N., Kastner, D. L., & Siegel, R. M. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20102049 · Cited by 860 · see citing works

Degradation of oxidized proteins by the 20S proteasome

Davies, K. J. A. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01250-0 · Cited by 849 · see citing works

IRE1α Induces Thioredoxin-Interacting Protein to Activate the NLRP3 Inflammasome and Promote Programmed Cell Death under Irremediable ER Stress

Lerner, A. G., Upton, J.-P., Praveen, P. V. K., Ghosh, R., Nakagawa, Y., Igbaria, A., Shen, S., Nguyen, V. Q., Backes, B. J., Heiman, M., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.007 · Cited by 841 · see citing works

Peroxisomes and oxidative stress

Schrader, M., & Fahimi, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.09.006 · Cited by 838 · see citing works

Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells

Du, X., Matsumura, T., Edelstein, D., Rossetti, L., Zsengellér, Z. K., Szabó, C., & Brownlee, M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18127 · Cited by 832 · see citing works

Paraoxonase and Atherosclerosis

Durrington, P. N., Mackness, B., & Mackness, M. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.21.4.473 · Cited by 821 · see citing works

Obesity, Insulin Resistance, Diabetes, and Cardiovascular Risk in Children

Steinberger, J., & Daniels, S. R. (2003) · Circulation · doi:10.1161/01.cir.0000060923.07573.f2 · Cited by 806 · see citing works

Superoxide is the major reactive oxygen species regulating autophagy

Chen, Y., Azad, M. B., & Gibson, S. B. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.49 · Cited by 796 · see citing works

Mitochondrial Fission Inhibitors Suppress Endothelin-1-Induced Artery Constriction

Chen, C., Gao, J., Liu, M., Li, S., Xuan, X., Zhang, X., Zhang, X.-Y., Wei, Y., Zhen, C., Jin, J., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479536 · Cited by 782 · see citing works

High Glucose Increases Nitric Oxide Synthase Expression and Superoxide Anion Generation in Human Aortic Endothelial Cells

Cosentino, F., Hishikawa, K., Katušić, Z. S., & Lüscher, T. F. (1997) · Circulation · doi:10.1161/01.cir.96.1.25 · Cited by 762 · see citing works

The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria

Kußmaul, L., & Hirst, J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510977103 · Cited by 720 · see citing works

Mitochondrial reactive oxygen species: A double edged sword in ischemia/reperfusion vs preconditioning

Kalogeris, T. J., Bao, Y., & Korthuis, R. J. (2014) · Redox Biology · doi:10.1016/j.redox.2014.05.006 · Cited by 719 · see citing works

ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS

Alexander, A., Cai, S.-L., Kim, J., Nanez, A., Sahin, M., MacLean, K. H., Inoki, K., Guan, K.-L., Shen, J., Person, M. D., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913860107 · Cited by 717 · see citing works

Mitochondrial α-Ketoglutarate Dehydrogenase Complex Generates Reactive Oxygen Species

Starkov, A. A., Fiskum, G. M., Chinopoulos, C., Lorenzo, B. J., Browne, S. E., Patel, M. S., & Beal, M. F. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1899-04.2004 · Cited by 692 · see citing works

Mammalian Autophagy: How Does It Work?

Bento, C. F., Renna, M., Ghislat, G., Puri, C., Ashkenazi, A., Vicinanza, M., Menzies, F. M., & Rubinsztein, D. C. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014556 · Cited by 692 · see citing works

Oxidized Phospholipids on Lipoprotein(a) Elicit Arterial Wall Inflammation and an Inflammatory Monocyte Response in Humans

van der Valk, F. M., Bekkering, S., Kroon, J., Yeang, C., den Bossche, J. V., van Buul, J. D., Ravandi, A., Nederveen, A. J., Verberne, H. J., Scipione, C. A., et al. (2016) · Circulation · doi:10.1161/circulationaha.116.020838 · Cited by 684 · see citing works

Antioxidants reduce endoplasmic reticulum stress and improve protein secretion

Malhotra, J. D., Miao, H. Z., Zhang, K., Wolfson, A., Pennathur, S., Pipe, S. W., & Kaufman, R. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809677105 · Cited by 672 · see citing works

Mitochondrial Complex II Can Generate Reactive Oxygen Species at High Rates in Both the Forward and Reverse Reactions

Quinlan, C. L., Orr, A. L., Perevoshchikova, I. V., Treberg, J. R., Ackrell, B. A., & Brand, M. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.374629 · Cited by 670 · see citing works

Role of peroxisomes in ros/rns-metabolism: Implications for human disease

Fransen, M., Nordgren, M., Wang, B., & Apanasets, O. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.12.001 · Cited by 644 · see citing works

Molecular Mechanisms of Ischemia–Reperfusion Injury in Brain: Pivotal Role of the Mitochondrial Membrane Potential in Reactive Oxygen Species Generation

Sanderson, T. H., Reynolds, C. A., Kumar, R., Przyklenk, K., & Hüttemann, M. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8344-z · Cited by 641 · see citing works

Cutting Edge: Direct Interaction of TLR4 with NAD(P)H Oxidase 4 Isozyme Is Essential for Lipopolysaccharide-Induced Production of Reactive Oxygen Species and Activation of NF-κB

Park, H. S., Jung, H. Y., Park, E. Y., Kim, J., Lee, W. J., & Bae, Y. S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.6.3589 · Cited by 635 · see citing works

NADPH Oxidases in Cardiovascular Health and Disease

Cave, A. C., Brewer, A. C., Narayanapanicker, A., Ray, R., Grieve, D. J., Walker, S., & Shah, A. M. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.691 · Cited by 630 · see citing works

Macrophage Autophagy Plays a Protective Role in Advanced Atherosclerosis

Liao, X., Sluimer, J. C., Wang, Y., Subramanian, M., Brown, K., Pattison, J. S., Robbins, J., Martinez, J., & Tabas, I. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.022 · Cited by 627 · see citing works

Glucose Challenge Stimulates Reactive Oxygen Species (ROS) Generation by Leucocytes

Mohanty, P., Hamouda, W., Garg, R., Aljada, A., Ghanim, H., & Dandona, P. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.85.8.6854 · Cited by 621 · see citing works

Activation of Chaperone-mediated Autophagy during Oxidative Stress

Kiffin, R., Christian, C., Knecht, E., & Cuervo, A. M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0477 · Cited by 611 · see citing works

Hypoxia and mitochondrial oxidative metabolism

Solaini, G., Baracca, A., Lenaz, G., & Sgarbi, G. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.011 · Cited by 608 · see citing works

Redox Regulation of NF-κB Activation: Distinct Redox Regulation Between the Cytoplasm and the Nucleus

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

Endothelial dysfunction in diabetes mellitus: Molecular mechanisms and clinical implications

Tabit, C. E., Chung, W. B., Hamburg, N. M., & Vita, J. A. (2010) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-010-9134-4 · Cited by 584 · see citing works

Role of Reactive Oxygen Species in the Progression of Type 2 Diabetes and Atherosclerosis

Kaneto, H., Katakami, N., Matsuhisa, M., & Matsuoka, T. (2010) · Mediators of Inflammation · doi:10.1155/2010/453892 · Cited by 578 · see citing works

Glutathione and mitochondria

Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00151 · Cited by 572 · see citing works

Altered mitochondrial dynamics contributes to endothelial dysfunction in diabetes mellitus

Shenouda, S. M., Widlansky, M. E., Chen, K., Xu, G., Holbrook, M., Tabit, C. E., Hamburg, N. M., Frame, A. A., Caiano, T. L., Kluge, M. A., et al. (2011) · Circulation · doi:10.1161/circulationaha.110.014506 · Cited by 570 · see citing works

Mitochondrial Reactive Oxygen Species Induces NLRP3-Dependent Lysosomal Damage and Inflammasome Activation

Heid, M. E., Keyel, P. A., Kamga, C., Shiva, S., Watkins, S. C., & Salter, R. D. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301490 · Cited by 570 · see citing works

Pathophysiologic mechanisms of acute ischemic stroke: An overview with emphasis on therapeutic significance beyond thrombolysis

Deb, P., Sharma, S., & Hassan, K. M. (2010) · Pathophysiology · doi:10.1016/j.pathophys.2009.12.001 · Cited by 567 · see citing works

Human copper-zinc superoxide dismutase transgenic mice are highly resistant to reperfusion injury after focal cerebral ischemia.

Yang, G., Chan, P. H., Chen, J., Carlson, E. J., Chen, S. F., Weinstein, P. R., Epstein, C. J., & Kamii, H. (1994) · Stroke · doi:10.1161/01.str.25.1.165 · Cited by 567 · see citing works

Mechanisms that regulate production of reactive oxygen species by cytochrome P450

Zangar, R. C. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.01.018 · Cited by 555 · see citing works

Uncoupling proteins and the control of mitochondrial reactive oxygen species production

Mailloux, R. J., & Harper, M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.022 · Cited by 534 · see citing works

Hyperglycemia-Induced Reactive Oxygen Species Increase Expression of the Receptor for Advanced Glycation End Products (RAGE) and RAGE Ligands

Yao, D., & Brownlee, M. (2009) · Diabetes · doi:10.2337/db09-0801 · Cited by 526 · see citing works

Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma

Mattiasson, G., Shamloo, M., Gido, G., Mathi, K., Tomasevic, G., Yi, S., Warden, C. H., Castilho, R. F., Melcher, T., Gonzalez-Zulueta, M., et al. (2003) · Nature Medicine · doi:10.1038/nm903 · Cited by 515 · see citing works

TCA Cycle and Mitochondrial Membrane Potential Are Necessary for Diverse Biological Functions

Martínez‐Reyes, I., Diebold, L. P., Kong, H., Schieber, M., Huang, H., Hensley, C. T., Mehta, M., Wang, T., Santos, J. H., Woychik, R. P., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.12.002 · Cited by 512 · see citing works

Oxidized Low Density Lipoprotein (ox-LDL) Binding to ox-LDL Receptor-1 in Endothelial Cells Induces the Activation of NF-κB through an Increased Production of Intracellular Reactive Oxygen Species

Cominacini, L., Pasini, A. F., Garbin, U., Davoli, A., Tosetti, M. L., Campagnola, M., Rigoni, A. M., Pastorino, A. M., Cascio, V. L., & Sawamura, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.12633 · Cited by 511 · see citing works

Upregulation of Nox4 by Hypertrophic Stimuli Promotes Apoptosis and Mitochondrial Dysfunction in Cardiac Myocytes

Ago, T., Kuroda, J., Pain, J., Fu, C., Li, H., & Sadoshima, J. (2010) · Circulation Research · doi:10.1161/circresaha.109.213116 · Cited by 506 · see citing works

IL-1β Processing in Host Defense: Beyond the Inflammasomes

Netea, M. G., Simon, A., van de Veerdonk, F. L., Kullberg, B. J., van der Meer, J. W. M., & Joosten, L. A. B. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000661 · Cited by 496 · see citing works

Hydrogen Peroxide Activates NF-κB through Tyrosine Phosphorylation of IκBα and Serine Phosphorylation of p65

Takada, Y., Mukhopadhyay, A., Kundu, G. C., Mahabeleshwar, G. H., Singh, S., & Aggarwal, B. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212389200 · Cited by 495 · see citing works

p47phox is required for atherosclerotic lesion progression in ApoE–/– mice

Barry-Lane, P. A., Patterson, C., van der Merwe, M., Hu, Z., Holland, S. M., Yeh, E. T. H., & Runge, M. S. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200111927 · Cited by 489 · see citing works

Hypoxia-inducible factor 1: Regulator of mitochondrial metabolism and mediator of ischemic preconditioning

Semenza, G. L. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.08.006 · Cited by 484 · see citing works

Mitochondrial Integrity and Function in Atherogenesis

Ballinger, S. W., Patterson, C., Knight-Lozano, C. A., Burow, D. L., Conklin, C. A., Hu, Z., Reuf, J., Horaist, C., Lebovitz, R. M., Hunter, G. C., et al. (2002) · Circulation · doi:10.1161/01.cir.0000023921.93743.89 · Cited by 478 · see citing works

Endoplasmic reticulum stress as a therapeutic target in cardiovascular disease.

Minamino, T., Komuro, I., & Kitakaze, M. (2010) · Circulation Research · doi:10.1161/circresaha.110.227819 · Cited by 469 · see citing works

Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner

Frank, M., Duvezin-Caubet, S., Koob, S., Occhipinti, A., Jagasia, R., Petcherski, A., Ruonala, M. O., Priault, M., Salin, B., & Reichert, A. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.08.007 · Cited by 468 · see citing works

NF-κB Activation Represses Tumor Necrosis Factor-α-induced Autophagy

Djavaheri‐Mergny, M., Amelotti, M., Mathieu, J., Besançon, F., Bauvy, C., Souquère, S., Pierron, G., & Codogno, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602097200 · Cited by 467 · see citing works

Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes

Rodrı́guez-Manzaneque, M. T., Tamarit, J., Bellı́, G., Ros, J., & Herrero, E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-10-0517 · Cited by 464 · see citing works

Mitochondrial fission mediates high glucose-induced cell death through elevated production of reactive oxygen species

Yu, T., Sheu, S.-S., Robotham, J. L., & Yoon, Y. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn104 · Cited by 462 · see citing works

Post-Stroke Inhibition of Induced NADPH Oxidase Type 4 Prevents Oxidative Stress and Neurodegeneration

Kleinschnitz, C., Grund, H., Wingler, K., Armitage, M. E., Jones, E., Mittal, M., Barit, D., Schwarz, T., Geis, C., Kraft, P., et al. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000479 · Cited by 447 · see citing works

Comparative resistance of the 20S and 26S proteasome to oxidative stress

REINHECKEL, T., SITTE, N., ULLRICH, O., KUCKELKORN, U., DAVIES, K. J. A., & GRUNE, T. (1998) · Biochemical Journal · doi:10.1042/bj3350637 · Cited by 447 · see citing works

Mitochondrial electron-transport-chain inhibitors of complexes I and II induce autophagic cell death mediated by reactive oxygen species

Chen, Y., McMillan‐Ward, E., Kong, J., Israels, S. J., & Gibson, S. B. (2007) · Journal of Cell Science · doi:10.1242/jcs.011163 · Cited by 444 · see citing works

Exposure to hydrogen peroxide induces oxidation and activation of AMP-activated protein kinase

Zmijewski, J. W., Banerjee, S., Bae, H., Friggeri, A., Lazarowski, E. R., & Abraham, E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143685 · Cited by 441 · see citing works

Ubiquitin Conjugation Is Not Required for the Degradation of Oxidized Proteins by Proteasome

Shringarpure, R., Grune, T., Mehlhase, J., & Davies, K. J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206279200 · Cited by 438 · see citing works

NAD(P)H Oxidase Nox-4 Mediates 7-Ketocholesterol-Induced Endoplasmic Reticulum Stress and Apoptosis in Human Aortic Smooth Muscle Cells

Pédruzzi, E., Guichard, C., Ollivier, V., Driss, F., Fay, M., Prunet, C., Marie, J., Pouzet, C., Samadi, M. H., Elbim, C., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10703-10717.2004 · Cited by 435 · see citing works

Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress

Tretter, L., & Adam-Vizi, V. (2005) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2005.1764 · Cited by 434 · see citing works

The transcription factor HIF-1α plays a critical role in the growth factor-dependent regulation of both aerobic and anaerobic glycolysis

Lum, J. J., Bui, T., Gruber, M., Gordan, J. D., DeBerardinis, R. J., Covello, K. L., Simon, M. C., & Thompson, C. B. (2007) · Genes & Development · doi:10.1101/gad.1529107 · Cited by 429 · see citing works

ATM functions at the peroxisome to induce pexophagy in response to ROS

Zhang, J., Tripathi, D. N., Ji, J., Alexander, A., Kim, J., Powell, R. T., Dere, R., Tait-Mulder, J., Lee, J., Paull, T. T., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3230 · Cited by 426 · see citing works

Why Have Antioxidants Failed in Clinical Trials?

Steinhubl, S. R. (2008) · The American Journal of Cardiology · doi:10.1016/j.amjcard.2008.02.003 · Cited by 424 · see citing works

Macrophages Generate Reactive Oxygen Species in Response to Minimally Oxidized Low-Density Lipoprotein

Bae, Y. S., Lee, J. H., Choi, S. H., Kim, S. A., Almazan, F., Witztum, J. L., & Miller, Y. I. (2008) · Circulation Research · doi:10.1161/circresaha.108.181040 · Cited by 423 · see citing works

Inhibition of Krebs Cycle Enzymes by Hydrogen Peroxide: A Key Role of α-Ketoglutarate Dehydrogenase in Limiting NADH Production under Oxidative Stress

Tretter, L., & Ádám‐Vizi, V. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-24-08972.2000 · Cited by 422 · see citing works

Mitochondrial oxidative stress causes mitochondrial fragmentation via differential modulation of mitochondrial fission–fusion proteins

Wu, S., Zhou, F., Zhang, Z., & Xing, D. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08010.x · Cited by 420 · see citing works

Endoplasmic Reticulum stress activates the inflammasome via NLRP3-caspase-2 driven mitochondrial damage

Bronner, D. N., Abuaita, B. H., Chen, X., Fitzgerald, K., Núñez, G., He, Y., Yin, X.-M., & O'Riordan, M. (2015) · Immunity · doi:10.1016/j.immuni.2015.08.008 · Cited by 407 · see citing works

The role of oxidized phospholipids in atherosclerosis

Berliner, J. A., Leitinger, N., & Tsimikas, S. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800074-jlr200 · Cited by 404 · see citing works

Glutaredoxin 2 Catalyzes the Reversible Oxidation and Glutathionylation of Mitochondrial Membrane Thiol Proteins

Beer, S. M., Taylor, E. R., Brown, S. E., Dahm, C. C., Costa, N. J., Runswick, M. J., & Murphy, M. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408011200 · Cited by 404 · see citing works

NF-κB controls energy homeostasis and metabolic adaptation by upregulating mitochondrial respiration

Mauro, C., Leow, S. C., Ansó, E., Rocha, S., Thotakura, A. K., Tornatore, L., Moretti, M., Smaele, E. D., Beg, A. A., Tergaonkar, V., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2324 · Cited by 393 · see citing works

Impact of mitochondrial ROS production in the pathogenesis of diabetes mellitus and its complications.

Nishikawa, T., & Araki, E. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.1458 · Cited by 391 · see citing works

Inducible Nitric-oxide Synthase Generates Superoxide from the Reductase Domain

Xia, Y., Roman, L. J., Masters, B. S. S., & Zweier, J. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22635 · Cited by 388 · see citing works

NF-κB Regulates Phagocytic NADPH Oxidase by Inducing the Expression of gp91

Anrather, J., Racchumi, G., & Iadecola, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m506172200 · Cited by 387 · see citing works

NADPH Oxidase Plays a Central Role in Blood-Brain Barrier Damage in Experimental Stroke

Kahles, T., Luedike, P., Endres, M., Galla, H., Steinmetz, H., Busse, R., Neumann‐Haefelin, T., & Brandes, R. P. (2007) · Stroke · doi:10.1161/strokeaha.107.489765 · Cited by 386 · see citing works

NADPH Oxidase 1 Plays a Key Role in Diabetes Mellitus–Accelerated Atherosclerosis

Gray, S. P., Di Marco, E., Okabe, J., Szyndralewiez, C., Heitz, F., Montezano, A. C., de Haan, J. B., Koulis, C., El-Osta, A., Andrews, K. L., et al. (2013) · Circulation · doi:10.1161/circulationaha.112.132159 · Cited by 386 · see citing works

Hypoxia triggers AMPK activation through reactive oxygen species-mediated activation of calcium release-activated calcium channels

Mungai, P. T., Waypa, G. B., Jairaman, A., Prakriya, M., Dokic, D., Ball, M. K., & Schumacker, P. T. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05124-11 · Cited by 385 · see citing works

Bone Morphogenic Protein 4 Produced in Endothelial Cells by Oscillatory Shear Stress Induces Monocyte Adhesion by Stimulating Reactive Oxygen Species Production From a Nox1-Based NADPH Oxidase

Sorescu, G. P., Song, H. W., Tressel, S. L., Hwang, J., Dikalov, S., Smith, D. A., Boyd, N. L., Platt, M. O., Lassegue, B. P., Griendling, K. K., et al. (2004) · Circulation Research · doi:10.1161/01.res.0000145728.22878.45 · Cited by 379 · see citing works

Metabolic syndrome and cardiovascular disease

Qiao, Q., Gao, W., Zhang, L., Nyamdorj, R., & Tuomilehto, J. O. (2007) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/000456307780480963 · Cited by 375 · see citing works

Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors

Rechsteiner, M., & Hill, C. P. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.11.003 · Cited by 372 · see citing works

Metformin suppresses diabetes-accelerated atherosclerosis via the inhibition of drp1-mediated mitochondrial fission

Wang, Q., Zhang, M., Torres, G., Wu, S., Ouyang, C., Xie, Z., & Zou, M.-H. (2017) · Diabetes · doi:10.2337/db16-0915 · Cited by 370 · see citing works

Superoxide generation by complex III: From mechanistic rationales to functional consequences

Bleier, L., & Dröse, S. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.002 · Cited by 369 · see citing works

Mitochondrial fission promotes the continued clearance of apoptotic cells by macrophages

Wang, Y., Subramanian, M., Yurdagul, A., Barbosa-Lorenzi, V. C., Cai, B., de Juan-Sanz, J., Ryan, T. A., Nomura, M., Maxfield, F. R., & Tabas, I. (2017) · Cell · doi:10.1016/j.cell.2017.08.041 · Cited by 364 · see citing works

eNOS, metabolic syndrome and cardiovascular disease

Huang, P. L. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.03.005 · Cited by 357 · see citing works

Oxidative Modification and Inactivation of the Proteasome during Coronary Occlusion/Reperfusion

Bulteau, A., Lundberg, K. C., Humphries, K. M., Sadek, H. A., Szweda, P. A., Friguet, B., & Szweda, L. I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100142200 · Cited by 354 · see citing works

Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system

Berndt, C., Lillig, C. H., & Holmgren, A. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01162.2006 · Cited by 350 · see citing works

Ischemic stroke injury is reduced in mice lacking a functional NADPH oxidase

Walder, C. E., Green, S. P., Darbonne, W. C., Mathias, J., Rae, J., Dinauer, M. C., Curnutte, J. T., & Thomas, G. R. (1997) · Stroke · doi:10.1161/01.str.28.11.2252 · Cited by 349 · see citing works

Increased mitochondrial H 2 O 2 production promotes endothelial NF-κB activation in aged rat arteries

Ungvari, Z. I., Orosz, Z. Z., Labinskyy, N., Rivera, A., Xiangmin, Z., Smith, K. E., & Csiszár, A. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01346.2006 · Cited by 347 · see citing works

Reduced Apoptosis and Plaque Necrosis in Advanced Atherosclerotic Lesions of Apoe−/− and Ldlr−/− Mice Lacking CHOP

Thorp, E. B., Li, G., Seimon, T. A., Kuriakose, G., Ron, D., & Tabas, I. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.003 · Cited by 342 · see citing works

Protein Synthesis upon Acute Nutrient Restriction Relies on Proteasome Function

Vabulas, R. M., & Hartl, F. U. (2005) · Science · doi:10.1126/science.1121925 · Cited by 339 · see citing works

A soluble form of the Mer receptor tyrosine kinase inhibits macrophage clearance of apoptotic cells and platelet aggregation

Sather, S., Kenyon, K. D., Lefkowitz, J. B., Liang, X., Varnum, B. C., Henson, P. M., & Graham, D. K. (2006) · Blood · doi:10.1182/blood-2006-05-021634 · Cited by 333 · see citing works

Degradation of Oxidized Proteins in K562 Human Hematopoietic Cells by Proteasome

Grune, T., Reinheckel, T., & Davies, K. J. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.26.15504 · Cited by 328 · see citing works

The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes

Pickering, A. M., Koop, A. L., Teoh, C., Ermak, G., Grune, T., & Davies, K. J. A. (2010) · Biochemical Journal · doi:10.1042/bj20100878 · Cited by 319 · see citing works

Oxidant Stress Impairs In Vivo Reendothelialization Capacity of Endothelial Progenitor Cells From Patients With Type 2 Diabetes Mellitus

Sorrentino, S. A., Bahlmann, F. H., Besler, C., Müller, M. F., Schulz, S., Kirchhoff, N., Doerries, C., Horváth, T., Limbourg, A., Limbourg, F. P., et al. (2007) · Circulation · doi:10.1161/circulationaha.106.684381 · Cited by 318 · see citing works

Aldosterone mediates angiotensin II‐induced interstitial cardiac fibrosis via a Nox2‐containing NADPH oxidase

Johar, S., Cave, A. C., Narayanapanicker, A., Grieve, D., & Shah, A. M. (2006) · The FASEB Journal · doi:10.1096/fj.05-4642fje · Cited by 314 · see citing works

The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex I

Quinlan, C. L., Goncalves, R. L. S., Hey-Mogensen, M., Yadava, N., Bunik, V. I., & Brand, M. D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545301 · Cited by 310 · see citing works

Manganese Superoxide Dismutase Mediates the Early Release of Mitochondrial Cytochrome C and Subsequent DNA Fragmentation after Permanent Focal Cerebral Ischemia in Mice

Fujimura, M., Morita‐Fujimura, Y., 川瀬, 誠., Copin, J., Calagui, B., Epstein, C. J., & Chan, P. H. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-09-03414.1999 · Cited by 309 · see citing works

NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis

Li, G., Scull, C. M., Özcan, L., & Tabas, I. A. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201006121 · Cited by 306 · see citing works

Direct evidence of a role for Nox2 in superoxide production, reduced nitric oxide bioavailability, and early atherosclerotic plaque formation in ApoE^−/−mice

Judkins, C. P., Diep, H., Broughton, B. R. S., Mast, A. E., Hooker, E. U., Miller, A. A., Selemidis, S., Dusting, G. J., Sobey, C. G., & Drummond, G. R. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00799.2009 · Cited by 299 · see citing works

Shedding of the Mer Tyrosine Kinase Receptor Is Mediated by ADAM17 Protein through a Pathway Involving Reactive Oxygen Species, Protein Kinase Cδ, and p38 Mitogen-activated Protein Kinase (MAPK)

Thorp, E., Vaisar, T., Subramanian, M., Mautner, L., Blobel, C., & Tabas, I. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.263020 · Cited by 298 · see citing works

Oscillatory Shear Stress Stimulates Endothelial Production of O2- from p47 -dependent NAD(P)H Oxidases, Leading to Monocyte Adhesion

Hwang, J., Saha, A., Boo, Y. C., Sorescu, G. P., McNally, J. S., Holland, S. M., Dikalov, S., Giddens, D. P., Griendling, K. K., Harrison, D. G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305150200 · Cited by 296 · see citing works

Glucose and NADPH oxidase drive neuronal superoxide formation in stroke

Suh, S. W., Shin, B. S., Ma, H., Hoecke, M. V., Brennan, A. M., Yenari, M. A., & Swanson, R. A. (2008) · Annals of Neurology · doi:10.1002/ana.21511 · Cited by 292 · see citing works

Inhibition of NADPH Oxidase is Neuroprotective after Ischemia—Reperfusion

Chen, H., Song, Y. S., & Chan, P. H. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.47 · Cited by 286 · see citing works

High-Glucose Stimulation Increases Reactive Oxygen Species Production Through the Calcium and Mitogen-Activated Protein Kinase-Mediated Activation of Mitochondrial Fission

Yu, T., Jhun, B. S., & Yoon, Y. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3284 · Cited by 286 · see citing works

Mitophagy Plays an Essential Role in Reducing Mitochondrial Production of Reactive Oxygen Species and Mutation of Mitochondrial DNA by Maintaining Mitochondrial Quantity and Quality in Yeast

Kurihara, Y., Kanki, T., Aoki, Y., Hirota, Y., Saigusa, T., Uchiumi, T., & Kang, D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.280156 · Cited by 279 · see citing works

Macropinocytosis Is the Endocytic Pathway That Mediates Macrophage Foam Cell Formation with Native Low Density Lipoprotein

Kruth, H. S., Jones, N. L., Huang, W., Zhao, B., Ishii, I., Chang, J., Combs, C. A., Malide, D. A., & Zhang, W.-Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407167200 · Cited by 276 · see citing works

Reactive oxygen species and peroxisomes: Struggling for balance

Bonekamp, N. A., Völkl, A., Fahimi, H. D., & Schrader, M. (2009) · BioFactors · doi:10.1002/biof.48 · Cited by 271 · see citing works

LPS-induced autophagy is mediated by oxidative signaling in cardiomyocytes and is associated with cytoprotection

Yuan, H., Perry, C. N., Huang, C., Iwai‐Kanai, E., Carreira, R., Glembotski, C. C., & Gottlieb, R. A. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01051.2008 · Cited by 265 · see citing works

Macrophage Mitochondrial Oxidative Stress Promotes Atherosclerosis and Nuclear Factor-κB–Mediated Inflammation in Macrophages

Wang, Y., Wang, G. Z., Rabinovitch, P. S., & Tabas, I. A. (2013) · Circulation Research · doi:10.1161/circresaha.114.302153 · Cited by 264 · see citing works

Crucial role of the amino-terminal tyrosine residue 42 and the carboxyl-terminal PEST domain of IκBα in NF-κB activation by an oxidative stress

Schoonbroodt, S., Ferreira, V., Best-Belpomme, M., Boelaert, J. R., Legrand-Poels, S., Korner, M., & Piette, J. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.8.4292 · Cited by 263 · see citing works

Thioredoxin and TRAF Family Proteins Regulate Reactive Oxygen Species-Dependent Activation of ASK1 through Reciprocal Modulation of the N-Terminal Homophilic Interaction of ASK1

Fujino, G., Noguchi, T., Matsuzawa, A., Yamauchi, S., Saitoh, M., Takeda, K., & Ichijo, H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00227-07 · Cited by 262 · see citing works

A tuberous sclerosis complex signalling node at the peroxisome regulates mTORC1 and autophagy in response to ROS

Zhang, J., Kim, J., Alexander, A., Cai, S., Tripathi, D. N., Dere, R., Tee, A. R., Tait-Mulder, J., Di Nardo, A., Han, J. M., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2822 · Cited by 258 · see citing works

Regulation of the 26 S Proteasome Complex During Oxidative Stress

Wang, X., Yen, J. L., Kaiser, P., & Huang, L. (2010) · Science Signaling · doi:10.1126/scisignal.2001232 · Cited by 256 · see citing works

Gene Silencing of the Mitochondrial Adaptor p66 Shc Suppresses Vascular Hyperglycemic Memory in Diabetes

Paneni, F., Mocharla, P. S., Akhmedov, A. T., Costantino, S., Osto, E., Volpe, M., Lüscher, T. F., & Cosentino, F. (2012) · Circulation Research · doi:10.1161/circresaha.112.266593 · Cited by 256 · see citing works

Minimally modified low density lipoprotein-induced inflammatory responses in endothelial cells are mediated by cyclic adenosine monophosphate.

Parhami, F., Fang, Z. T., Fogelman, A. M., Andalibi, A., Territo, M., & Berliner, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116590 · Cited by 256 · see citing works

Sodium Selenite Induces Superoxide-Mediated Mitochondrial Damage and Subsequent Autophagic Cell Death in Malignant Glioma Cells

Kim, E. H., Sohn, S., Kwon, H. J., Kim, S. U., Kim, M.-J., Lee, S.-J., & Choi, K. S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4217 · Cited by 251 · see citing works

Manganese Superoxide Dismutase Deficiency Exacerbates Cerebral Infarction After Focal Cerebral Ischemia/Reperfusion in Mice

Kim, G. W., Kondo, T., Noshita, N., & Chan, P. H. (2002) · Stroke · doi:10.1161/hs0302.103745 · Cited by 251 · see citing works

AMP-activated protein kinase, stress responses and cardiovascular diseases

Wang, S., Song, P., & Zou, M. (2012) · Clinical Science · doi:10.1042/cs20110625 · Cited by 243 · see citing works

Tumor Necrosis Factor-α Induces Endothelial Dysfunction in Lepr db Mice

Gao, X., Belmadani, S., Picchi, A., Xu, X., Potter, B. J., Tewari‐Singh, N., Capobianco, S., Chilian, W. M., & Zhang, C. (2007) · Circulation · doi:10.1161/circulationaha.106.650671 · Cited by 241 · see citing works

Protective Role of Uncoupling Protein 2 in Atherosclerosis

Blanc, J., Alves‐Guerra, M., Esposito, B., Rousset, S., Gourdy, P., Ricquier, D., Tedgui, A., Miroux, B., & Mallat, Z. (2003) · Circulation · doi:10.1161/01.cir.0000051722.66074.60 · Cited by 239 · see citing works

Reactive oxygen species trigger Parkin/PINK1 pathway–dependent mitophagy by inducing mitochondrial recruitment of Parkin

Xiao, B., Goh, J. Y., Xiao, L., Xian, H., Lim, K., & Liou, Y. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.787739 · Cited by 238 · see citing works

Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

Tavender, T. J., Springate, J. J., & Bulleid, N. J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.273 · Cited by 237 · see citing works

Mechanisms of Vascular Smooth Muscle NADPH Oxidase 1 (Nox1) Contribution to Injury-Induced Neointimal Formation

Lee, M. Y., Martín, A. S., Mehta, P. K., Dikalova, A., Garrido, A. M., Datla, S. R., Lyons, E., Krause, K., Bánfi, B., Lambeth, J. D., et al. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.108.181925 · Cited by 234 · see citing works

Activity of Ubiquitin-dependent Pathway in Response to Oxidative Stress

Shang, F., Gong, X., & Taylor, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.37.23086 · Cited by 231 · see citing works

Retardation of Atherosclerosis by Overexpression of Catalase or Both Cu/Zn-Superoxide Dismutase and Catalase in Mice Lacking Apolipoprotein E

Yang, H., Roberts, L. J., Shi, M., Zhou, L. C., Ballard, B. R., Richardson, A. G., & Guo, Z. M. (2004) · Circulation Research · doi:10.1161/01.res.0000149564.49410.0d · Cited by 230 · see citing works

Nox2 and Rac1 Regulate H2O2-Dependent Recruitment of TRAF6 to Endosomal Interleukin-1 Receptor Complexes

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

Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones

Ullrich, O., Reinheckel, T., Sitte, N., Hass, R., Grune, T., & Davies, K. J. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6223 · Cited by 229 · see citing works

A Role for Oxidized Phospholipids in Atherosclerosis

Berliner, J. A., & Watson, A. D. (2005) · New England Journal of Medicine · doi:10.1056/nejmp058118 · Cited by 229 · see citing works

Mitochondrial fragmentation and superoxide anion production in coronary endothelial cells from a mouse model of type 1 diabetes

Makino, A., Scott, B. T., & Dillmann, W. H. (2010) · Diabetologia · doi:10.1007/s00125-010-1770-4 · Cited by 223 · see citing works

Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-Induced Endothelial Cell Activation

Li, X., Fang, P., Li, Y., Kuo, Y., Andrews, A. J., Nanayakkara, G., Johnson, C., Fu, H., Shan, H., Du, F., et al. (2016) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.115.306964 · Cited by 220 · see citing works

NOX4 NADPH Oxidase-Dependent Mitochondrial Oxidative Stress in Aging-Associated Cardiovascular Disease

Vendrov, A. E., Vendrov, K. C., Smith, A., Yuan, J., Sumida, A., Robidoux, J., Runge, M. S., & Madamanchi, N. R. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6221 · Cited by 219 · see citing works

Ferroptosis: mechanisms, biology and role in disease

Jiang, X., Stockwell, B. R., & Conrad, M. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00324-8 · Cited by 7,698 · see citing works

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

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

Role of oxidative stress in the pathogenesis of nonalcoholic fatty liver disease

Chen, Z., Tian, R., She, Z., Cai, J., & Li, H. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.025 · Cited by 1,303 · see citing works

Role of Reactive Oxygen Species in Cancer Progression: Molecular Mechanisms and Recent Advancements

Aggarwal, V., Tuli, H. S., Varol, A., Thakral, F., Yerer, M. B., Sak, K., Varol, M., Jain, A., Khan, M. A., & Sethi, G. (2019) · Biomolecules · doi:10.3390/biom9110735 · Cited by 1,235 · see citing works

Reactive Oxygen Species: Drivers of Physiological and Pathological Processes

Checa, J., & Aran, J. M. (2020) · Journal of Inflammation Research · doi:10.2147/jir.s275595 · Cited by 1,022 · see citing works

The mechanism of HMGB1 secretion and release

Chen, R., Kang, R., & Tang, D. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00736-w · Cited by 878 · see citing works

Mechanisms of Oxidative Stress in Metabolic Syndrome

Masenga, S. K., Kabwe, L. S., Chakulya, M., & Kirabo, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097898 · Cited by 786 · see citing works

The role of metabolism in chondrocyte dysfunction and the progression of osteoarthritis.

Zheng, L.-L., Zhang, Z.-J., Sheng, P., & Mobasheri, A. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101249 · Cited by 717 · see citing works

New insights into oxidative stress and inflammation during diabetes mellitus-accelerated atherosclerosis

Yuan, T., Yang, T., Chen, H., Fu, D., Hu, Y., Wang, J., Yuan, Q., Yu, H., Xu, W., & Xie, X. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.025 · Cited by 750 · see citing works

PARP and PARG inhibitors in cancer treatmentPreprint

Slade, D. (2020) · Genes & Development · doi:10.1101/gad.334516.119 · Cited by 666 · see citing works

Research progress of glutathione peroxidase family (GPX) in redoxidation

Pei, J., Pan, X., Wei, G., & Hua, Y. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1147414 · Cited by 650 · see citing works

Targeting Oxidative Stress and Mitochondrial Dysfunction in the Treatment of Impaired Wound Healing: A Systematic Review

Sanchez, M. C. C., Lancel, S., Boulanger, É., & Nevière, R. (2018) · Antioxidants · doi:10.3390/antiox7080098 · Cited by 584 · see citing works

Dietary patterns and biomarkers of oxidative stress and inflammation: A systematic review of observational and intervention studies

Aleksandrova, K., Koelman, L., & Rodrigues, C. E. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101869 · Cited by 526 · see citing works

Antioxidant enzymes regulation in plants in reference to reactive oxygen species (ROS) and reactive nitrogen species (RNS)

Kapoor, D., Singh, S., Kumar, V., Romero, R., Prasad, R., & Singh, J. (2019) · Plant Gene · doi:10.1016/j.plgene.2019.100182 · Cited by 512 · see citing works

Oxidative Stress: Pathogenetic Role in Diabetes Mellitus and Its Complications and Therapeutic Approaches to Correction

Darenskaya, M. A., Колесникова, Л. И., & Kolesnikov, S. I. (2021) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-021-05191-7 · Cited by 488 · see citing works

The diversified role of mitochondria in ferroptosis in cancer

Liu, Y., Lu, S.-P., Wu, L., Yang, L., Wang, J., & Wang, J. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06045-y · Cited by 473 · see citing works

Cellular Mechanisms of Aortic Aneurysm Formation

Quintana, R. A., & Taylor, W. R. (2019) · Circulation Research · doi:10.1161/circresaha.118.313187 · Cited by 438 · see citing works

Mitochondrial Reactive Oxygen Species and Their Contribution in Chronic Kidney Disease Progression Through Oxidative Stress

Tirichen, H., Yaigoub, H., Xu, W., Wu, C., Li, R., & Li, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.627837 · Cited by 431 · see citing works

The Role of the Pentose Phosphate Pathway in Diabetes and Cancer

Ge, T., Yang, J., Zhou, S., Wang, Y., Li, Y., & Tong, X. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00365 · Cited by 413 · see citing works

Xanthine oxidoreductase: One enzyme for multiple physiological tasks

Bortolotti, M., Polito, L., Battelli, M. G., & Bolognesi, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101882 · Cited by 405 · see citing works

The interplay of ROS and the PI3K/Akt pathway in autophagy regulation

Kma, L., & Baruah, T. J. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2104 · Cited by 401 · see citing works

The Role of NADPH Oxidases and Oxidative Stress in Neurodegenerative Disorders

Tarafdar, A., & Pula, G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19123824 · Cited by 373 · see citing works

Thiazole Ring—A Biologically Active Scaffold

Petrou, A., Fesatidou, M., & Geronikaki, A. A. (2021) · Molecules · doi:10.3390/molecules26113166 · Cited by 358 · see citing works

Toxicity of metal-based nanoparticles: Challenges in the nano era

Zhang, N., Xiong, G., & Liu, Z. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.1001572 · Cited by 355 · see citing works

Molecular Mechanisms That Link Oxidative Stress, Inflammation, and Fibrosis in the Liver

Ramos‐Tovar, E., & Muriel, P. (2020) · Antioxidants · doi:10.3390/antiox9121279 · Cited by 348 · see citing works

Nonalcoholic fatty liver disease (NAFLD) from pathogenesis to treatment concepts in humans

Pafili, K., & Roden, M. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101122 · Cited by 330 · see citing works

Mitochondrial complex I ROS production and redox signaling in hypoxia

Okoye, C. N., Koren, S. A., & Wojtovich, A. P. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102926 · Cited by 328 · see citing works

NRF2 as a regulator of cell metabolism and inflammation in cancer

He, F., Antonucci, L., & Karin, M. (2020) · Carcinogenesis · doi:10.1093/carcin/bgaa039 · Cited by 318 · 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

Catalytic activity tunable ceria nanoparticles prevent chemotherapy-induced acute kidney injury without interference with chemotherapeutics

Weng, Q., Sun, H., Fang, C., Xia, F., Liao, H., Lee, J., Wang, J., Xie, A., Ren, J., Guo, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21714-2 · Cited by 303 · see citing works

Mechanistic Pathogenesis of Endothelial Dysfunction in Diabetic Nephropathy and Retinopathy

Yang, J., & Liu, Z. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.816400 · Cited by 298 · see citing works

Fe-Curcumin Nanozyme-Mediated Reactive Oxygen Species Scavenging and Anti-Inflammation for Acute Lung Injury

Yuan, R., Li, Y., Han, S., Chen, X., Chen, J., He, J., Gao, H., Yang, Y., Yang, S., & Yang, Y. P. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00866 · Cited by 288 · see citing works

Cardiomyopathy in obesity, insulin resistance and diabetes

Nakamura, M., & Sadoshima, J. (2019) · The Journal of Physiology · doi:10.1113/jp276747 · Cited by 287 · see citing works

ROS systems are a new integrated network for sensing homeostasis and alarming stresses in organelle metabolic processes

Sun, Y., Lu, Y., Saredy, J., Wang, X., Drummer, C., Shao, Y., Saaoud, F., Xu, K., Liu, M., Yang, W. Y., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101696 · Cited by 283 · see citing works

Oxidative stress and the role of redox signalling in chronic kidney disease

Kishi, S., Nagasu, H., Kidokoro, K., & Kashihara, N. (2023) · Nature Reviews Nephrology · doi:10.1038/s41581-023-00775-0 · Cited by 283 · see citing works

Mitochondrial metabolism regulates macrophage biology

Wang, Y., Li, N., Zhang, X., & Horng, T. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100904 · Cited by 278 · see citing works

Reactive oxygen species-based nanomaterials for the treatment of myocardial ischemia reperfusion injuries

Zhao, T., Wu, W., Sui, L., Huang, Q., Nan, Y., Liu, J., & Ai, K. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.06.006 · Cited by 270 · see citing works

Effects of Dietary Patterns on Biomarkers of Inflammation and Immune Responses: A Systematic Review and Meta-Analysis of Randomized Controlled Trials

Koelman, L., Rodrigues, C. E., & Aleksandrova, K. (2021) · Advances in Nutrition · doi:10.1093/advances/nmab086 · Cited by 267 · see citing works

Microvesicles: ROS scavengers and ROS producers

Bodega, G., Alique, M., Puebla, L., Carracedo, J., & Ramı́rez, R. (2019) · Journal of Extracellular Vesicles · doi:10.1080/20013078.2019.1626654 · Cited by 257 · see citing works

Oxidative Stress and Mitochondrial Dysfunction in Chronic Kidney Disease

Ho, H.-J., & Shirakawa, H. (2022) · Cells · doi:10.3390/cells12010088 · Cited by 255 · see citing works

Oxidative stress as a key modulator of cell fate decision in osteoarthritis and osteoporosis: a narrative review

Riegger, J., Schoppa, A., Ruths, L., Haffner‐Luntzer, M., & Ignatius, A. A. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00489-y · Cited by 255 · see citing works

Cannabidiol (CBD) as a Promising Anti-Cancer Drug

Seltzer, E. S., Watters, A. K., MacKenzie, D., Granat, L. M., & Zhang, D. (2020) · Cancers · doi:10.3390/cancers12113203 · Cited by 252 · see citing works

FOXO3a from the Nucleus to the Mitochondria: A Round Trip in Cellular Stress Response

Fasano, C., Disciglio, V., Bertora, S., Signorile, M. L., & Simone, C. (2019) · Cells · doi:10.3390/cells8091110 · Cited by 237 · see citing works

Biomedical Applications of Reactive Oxygen Species Generation by Metal Nanoparticles

Canaparo, R., Foglietta, F., Limongi, T., & Serpe, L. (2020) · Materials · doi:10.3390/ma14010053 · Cited by 229 · see citing works

Stem Cell‐Derived Nanovesicles Embedded in Dual‐Layered Hydrogel for Programmed ROS Regulation and Comprehensive Tissue Regeneration in Burn Wound Healing

Zhao, M., Kang, M., Wang, J., Yang, R., Zhong, X., Xie, Q., Zhou, S., Zhang, Z., Zheng, J., Zhang, Y., et al. (2024) · Advanced Materials · doi:10.1002/adma.202401369 · Cited by 227 · see citing works

Size-dependent effects of polystyrene nanoplastics on autophagy response in human umbilical vein endothelial cells

Lu, Y.-Y., Li, H., Ren, H.-Y., Zhang, X., Huang, F.-Y., Zhang, D., Huang, Q., & Zhang, X. (2021) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2021.126770 · Cited by 221 · see citing works

Aucubin alleviates oxidative stress and inflammation via Nrf2-mediated signaling activity in experimental traumatic brain injury

Wang, H., Zhou, X., Wu, L., Liu, G., Xu, W., Zhang, X., Gao, Y., Tao, T., Zhou, Y., Lu, Y., et al. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01863-9 · Cited by 216 · see citing works

Antioxidant Activity, Metabolism, and Bioavailability of Polyphenols in the Diet of Animals

Bešlo, D., Golubić, N., Rastija, V., Agić, D., Karnaš, M., Šubarić, D., & Lučić, B. (2023) · Antioxidants · doi:10.3390/antiox12061141 · Cited by 215 · see citing works

Complex IV – The regulatory center of mitochondrial oxidative phosphorylation

Kadenbach, B. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.10.004 · Cited by 212 · see citing works

Redox Imbalance in Inflammation: The Interplay of Oxidative and Reductive Stress

Bellanti, F., Coda, A. R. D., Trecca, M. I., Buglio, A. L., Serviddio, G., & Vendemiale, G. (2025) · Antioxidants · doi:10.3390/antiox14060656 · Cited by 212 · see citing works

Immune cell - produced ROS and their impact on tumor growth and metastasis

Kennel, K. B., & Greten, F. R. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101891 · Cited by 209 · see citing works

Mechanisms of Arterial Stiffening

Lacolley, P. J., Regnault, V., & Laurent, S. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.313129 · Cited by 203 · see citing works

Uric acid and inflammation in kidney disease

Jung, S. W., Kim, S.-M., Kim, Y., Lee, S. H., & Moon, J.-Y. (2020) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00272.2019 · Cited by 196 · see citing works

Antioxidant peptides, the guardian of life from oxidative stress

Zhu, Y., Wang, K., Jia, X., Fu, C., Yu, H., & Wang, Y. (2023) · Medicinal Research Reviews · doi:10.1002/med.21986 · Cited by 192 · see citing works

The Release of Peripheral Immune Inflammatory Cytokines Promote an Inflammatory Cascade in PCOS Patients via Altering the Follicular Microenvironment

Liu, Y., Liu, H., Li, Z., Fan, H., Yan, X., Liu, X., Xuan, J., Feng, D., & Wei, X. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.685724 · Cited by 190 · see citing works

Taurine as a Natural Antioxidant: From Direct Antioxidant Effects to Protective Action in Various Toxicological Models

Surai, P. F., Earle-Payne, K., & Kidd, M. T. (2021) · Antioxidants · doi:10.3390/antiox10121876 · Cited by 185 · 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

Targeting oxidative stress as a preventive and therapeutic approach for cardiovascular disease

Yan, Q., Liu, S., Sun, Y., Chen, C., Yang, S., Lin, M., Long, J., Yao, J., Lin, Y.-T., Yi, F., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04361-7 · Cited by 184 · see citing works

ROS signaling cascades: dual regulations for osteoclast and osteoblast

Tao, H., Ge, G., Liang, X., Zhang, W., Sun, H., Li, M., & Geng, D. (2020) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmaa098 · Cited by 182 · see citing works

Oxidative stress in cancer: from tumor and microenvironment remodeling to therapeutic frontiers

Liang, X., Weng, J., You, Z., Wang, Y., Wen, J., Xia, Z., Huang, S., Luo, P., & Cheng, Q. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02375-x · Cited by 182 · see citing works

Carotenoids and Markers of Oxidative Stress in Human Observational Studies and Intervention Trials: Implications for Chronic Diseases

Bohn, T. (2019) · Antioxidants · doi:10.3390/antiox8060179 · Cited by 181 · see citing works

Protective Effects and Target Network Analysis of Ginsenoside Rg1 in Cerebral Ischemia and Reperfusion Injury: A Comprehensive Overview of Experimental Studies

Xie, W., Zhou, P., Sun, Y., Meng, X., Dai, Z., Sun, G., & Sun, X. (2018) · Cells · doi:10.3390/cells7120270 · Cited by 179 · see citing works

Adiponectin peptide alleviates oxidative stress and NLRP3 inflammasome activation after cerebral ischemia-reperfusion injury by regulating AMPK/GSK-3β

Liu, H., Wu, X., Luo, J., Zhao, L., Li, X., Guo, H., Bai, H., Cui, W., Guo, W., Feng, D., et al. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113302 · Cited by 178 · see citing works

Mechanisms of Non-Alcoholic Fatty Liver Disease in the Metabolic Syndrome. A Narrative Review

Rinaldi, L., Pafundi, P. C., Galiero, R., Caturano, A., Morone, M. V., Silvestri, C., Giordano, M., Salvatore, T., & Sasso, F. C. (2021) · Antioxidants · doi:10.3390/antiox10020270 · Cited by 178 · see citing works

Hydrogen, a Novel Therapeutic Molecule, Regulates Oxidative Stress, Inflammation, and Apoptosis

Tian, Y., Zhang, Y., Wang, Y. C., Chen, Y., Fan, W., Zhou, J., Qiao, J., & Wei, Y. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.789507 · Cited by 176 · see citing works

Mechanisms of Acupuncture in the Regulation of Oxidative Stress in Treating Ischemic Stroke

Su, X.-T., Wang, L., Ma, S., Cao, Y., Yang, N., Lin, L., Fisher, M., Yang, J., & Liu, C. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7875396 · Cited by 174 · see citing works

Antioxidative nanomaterials and biomedical applications

Liu, Y., & Shi, J. (2019) · Nano Today · doi:10.1016/j.nantod.2019.05.008 · Cited by 173 · see citing works

Reactive Oxygen Species Scavenging Nanomedicine for the Treatment of Ischemic Heart Disease

Zhang, Z., Dalan, R., Hu, Z., Wang, J., Chew, N., Poh, K. K., Tan, R., Soong, T. W., Dai, Y., Ye, L., et al. (2022) · Advanced Materials · doi:10.1002/adma.202202169 · Cited by 174 · see citing works

Mitochondrial Oxidative Stress and “Mito-Inflammation”: Actors in the Diseases

Patergnani, S., Bouhamida, E., Leo, S., Pinton, P., & Rimessi, A. (2021) · Biomedicines · doi:10.3390/biomedicines9020216 · Cited by 172 · see citing works

Breaking the Intracellular Redox Balance with Diselenium Nanoparticles for Maximizing Chemotherapy Efficacy on Patient-Derived Xenograft Models

Wei, D., Yu, Y., Zhang, X., Wang, Y., Chen, H., Zhao, Y., Wang, F., Rong, G., Wang, W., Kang, X., et al. (2020) · ACS Nano · doi:10.1021/acsnano.0c06190 · Cited by 170 · see citing works

Roles of reactive oxygen species in inflammation and cancer

Yu, Y., Liu, S., Yang, L., Song, P., Liu, Z., Liu, X., Yan, X., & Dong, Q. (2024) · MedComm · doi:10.1002/mco2.519 · Cited by 170 · see citing works

ROS Scavenging Biopolymers for Anti‐Inflammatory Diseases: Classification and Formulation

Zhang, J., Fu, Y., Yang, P., Liu, X., Li, Y., & Gu, Z. (2020) · Advanced Materials Interfaces · doi:10.1002/admi.202000632 · Cited by 169 · see citing works

Targeting Mitochondrial-Derived Reactive Oxygen Species in T Cell-Mediated Autoimmune Diseases

Chávez, M. D., & Tse, H. M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.703972 · Cited by 169 · see citing works

The interplay of autophagy and oxidative stress in the pathogenesis and therapy of retinal degenerative diseases

Chang, K., Liu, P., Chang, C., Lin, Y., Chen, Y., & Shu, C. (2022) · Cell & Bioscience · doi:10.1186/s13578-021-00736-9 · Cited by 168 · see citing works

Stimuli-responsive polysaccharide-based smart hydrogels for diabetic wound healing: Design aspects, preparation methods and regulatory perspectives

Kolipaka, T., Pandey, G., Abraham, N., Srinivasarao, D. A., Raghuvanshi, R. S., Rajinikanth, P. S., Tickoo, V., & Srivastava, S. (2023) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2023.121537 · Cited by 168 · see citing works

Unveiling the Role of Inflammation and Oxidative Stress on Age-Related Cardiovascular Diseases

de Almeida, A. J. P. O., Rezende, M. S. D. A., Dantas, S. H., Silva, S. D. L., de Oliveira, J. C. P. L., de Azevedo, F. D. L. A. A., Alves, R. M. F. R., de Menezes, G. M. S., dos Santos, P. F., Gonçalves, T. A. F., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/1954398 · Cited by 167 · see citing works

Mitochondria, oxidative stress and nonalcoholic fatty liver disease: A complex relationship

Karkucińska‐Więckowska, A., Simões, I. C. M., Kalinowski, P., Lebiedzińska, M., Zieniewicz, K., Milkiewicz, P., Górska‐Ponikowska, M., Pinton, P., Malik, A. N., Krawczyk, M. J., et al. (2021) · European Journal of Clinical Investigation · doi:10.1111/eci.13622 · Cited by 165 · see citing works

Research advances in bioactive components and health benefits of jujube (Ziziphus jujuba Mill.) fruit

Yang, L., Bao, T., Mo, J., Ni, J., & Chen, W. (2021) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2000594 · Cited by 163 · see citing works

ROS signaling in innate immunity via oxidative protein modifications

Manoharan, R. R., Prasad, A., Pospı́šil, P., & Kzhyshkowska, J. G. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1359600 · Cited by 163 · see citing works

Biological synthesis of metallic nanoparticles (MNPs) by plants and microbes: their cellular uptake, biocompatibility, and biomedical applications

Ahmad, F., Ashraf, N., Ashraf, T., Zhou, R., & Yin, D. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09675-5 · Cited by 162 · see citing works

Mitochondrial complex II and reactive oxygen species in disease and therapy

Vanova, K. H., Kraus, M., Neužil, J., & Rohlena, J. (2020) · Redox Report · doi:10.1080/13510002.2020.1752002 · Cited by 162 · see citing works

Supplementing Glycine and N-Acetylcysteine (GlyNAC) in Older Adults Improves Glutathione Deficiency, Oxidative Stress, Mitochondrial Dysfunction, Inflammation, Physical Function, and Aging Hallmarks: A Randomized Clinical Trial

Kumar, P., Liu, C., Suliburk, J. W., Hsu, J. W.-C., Muthupillai, R., Jahoor, F., Minard, C. G., Taffet, G. E., & Sekhar, R. V. (2022) · The Journals of Gerontology Series A · doi:10.1093/gerona/glac135 · Cited by 161 · see citing works

Endothelial Cell Metabolism in Atherosclerosis

Theodorou, K., & Boon, R. A. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00082 · Cited by 160 · see citing works

Large Extracellular Vesicles: Have We Found the Holy Grail of Inflammation?

Słomka, A., Urban, S. K., Kornek, M., Żekanowska, E., & Kornek, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02723 · Cited by 160 · see citing works

Dihydrolipoic Acid–Gold Nanoclusters Regulate Microglial Polarization and Have the Potential To Alter Neurogenesis

Xiao, L., Wei, F., Zhou, Y., Anderson, G. J., Frazer, D. M., Lim, Y. C., Liu, T., & Xiao, Y. (2019) · Nano Letters · doi:10.1021/acs.nanolett.9b04216 · Cited by 160 · see citing works

The Role of Oxidative Stress in Vitiligo: An Update on Its Pathogenesis and Therapeutic Implications

Chang, W., & Ko, C.-H. (2023) · Cells · doi:10.3390/cells12060936 · Cited by 150 · see citing works

Ionizing Radiation as a Source of Oxidative Stress—The Protective Role of Melatonin and Vitamin D

Nuszkiewicz, J., Woźniak, A., & Szewczyk-Golec, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165804 · Cited by 156 · see citing works

The Inhibitory Effect of Curcumin on Virus-Induced Cytokine Storm and Its Potential Use in the Associated Severe Pneumonia

Liu, Z., & Ying, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00479 · Cited by 156 · see citing works

Reactive Oxygen Species and Oxidative Stress in the Pathogenesis of MAFLD

Clare, K., Dillon, J. F., & Brennan, P. (2022) · Journal of Clinical and Translational Hepatology · doi:10.14218/jcth.2022.00067 · Cited by 156 · see citing works

Oxidative stress and regeneration

Jaganjac, M., Milković, L., Žarković, N., & Žarković, K. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.02.004 · Cited by 154 · see citing works

Targeting pyroptosis as a preventive and therapeutic approach for stroke

Long, J., Sun, Y., Liu, S., Yang, S., Chen, C., Zhang, Z., Chu, S., Yang, Y., Pei, G., Lin, M., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01440-y · Cited by 153 · see citing works

The Influence of Reactive Oxygen Species in the Immune System and Pathogenesis of Multiple Sclerosis

Tavassolifar, M. J., Vodjgani, M., Salehi, Z., & Izad, M. H. (2020) · Autoimmune Diseases · doi:10.1155/2020/5793817 · Cited by 152 · see citing works

Glyphosate damages blood-testis barrier via NOX1-triggered oxidative stress in rats: Long-term exposure as a potential risk for male reproductive health

Liu, J., Li, Z., Lu, L., Wang, Z.-Y., & Wang, L. (2021) · Environment International · doi:10.1016/j.envint.2021.107038 · Cited by 152 · see citing works

Extracellular superoxide dismutase, a molecular transducer of health benefits of exercise

Yan, Z., & Spaulding, H. R. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101508 · Cited by 150 · see citing works

Hyaluronic Acid‐Based Reactive Oxygen Species‐Responsive Multifunctional Injectable Hydrogel Platform Accelerating Diabetic Wound Healing

Shi, C., Zhang, Y., Wu, G., Zhu, Z., Zheng, H., Sun, X., Heng, Y., Pan, S., Xiu, H., Zhang, J., et al. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202302626 · Cited by 149 · see citing works

Oxidative stress: The nexus of obesity and cognitive dysfunction in diabetes

Li, H., Ren, J. L., Li, Y., Wu, Q., & Wei, J. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1134025 · Cited by 148 · see citing works

Triggers, cascades, and endpoints: connecting the dots of coral bleaching mechanisms

Helgoe, J., Davy, S. K., Weis, V. M., & Rodríguez‐Lanetty, M. (2024) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.13042 · Cited by 148 · see citing works

The Link between Chronic Stress and Accelerated Aging

Yegorov, Y. E., Poznyak, A. V., Nikiforov, N. G., Sobenin, I. A., & Orekhov, A. N. (2020) · Biomedicines · doi:10.3390/biomedicines8070198 · Cited by 147 · see citing works

Green Tea and Epigallocatechin Gallate (EGCG) for the Management of Nonalcoholic Fatty Liver Diseases (NAFLD): Insights into the Role of Oxidative Stress and Antioxidant Mechanism

Tang, G., Xu, Y., Zhang, C., Wang, N., Li, H., & Feng, Y. (2021) · Antioxidants · doi:10.3390/antiox10071076 · Cited by 145 · see citing works

Forrester et al., 2018.pdf

J. Forrester, S., Kikuchi, D., S. Hernandes, M., Xu, Q., & K. Griendling, K. (2019) · Figshare · doi:10.25376/hra.7971263

Reactive Oxygen Species (ROS) in Metabolic Disease—Don’t Shoot the Metabolic Messenger

Lindsay, R. T., & Rhodes, C. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062622 · Cited by 35 · see citing works

Effects of REDOX in Regulating and Treatment of Metabolic and Inflammatory Cardiovascular Diseases

Wang, K., Dong, Y., Liu, J., Qian, L., Wang, T., Gao, X., Wang, K., & Zhou, L. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/5860356 · Cited by 32 · see citing works

Editorial: The role of oxidative stress in metabolic and inflammatory diseases

Klisic, A. N., Ahmad, R., Haddad, D., Bonomini, F., & Sindhu, S. T. A. K. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1374584 · Cited by 16 · see citing works

Interplay Between Reactive Oxygen/Reactive Nitrogen Species and Metabolism in Vascular Biology and Disease

Ushio‐Fukai, M., Ash, D., Nagarkoti, S., de Chantemèle, E. J. B., Fulton, D. J., & Fukai, T. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8161 · Cited by 96 · see citing works