Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins

NOX enzymes and the biology of reactive oxygen

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Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate

Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T.-C., Hinks, J. A., Tonks, N. K., & Barford, D. (2003) · Nature · doi:10.1038/nature01680 · Cited by 951

Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors

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Insulin-stimulated Hydrogen Peroxide Reversibly Inhibits Protein-tyrosine Phosphatase 1B in Vivo and Enhances the Early Insulin Action Cascade

Mahadev, K., Zilbering, A., Zhu, L., & Goldstein, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100109200 · Cited by 509

Proteomics Analysis of Cellular Response to Oxidative Stress

Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106585200 · Cited by 393

Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine

Chang, T.-S., Jeong, W., Woo, H. A., Lee, S. M., Park, S., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409482200 · Cited by 388

How mitochondria produce reactive oxygen species

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

Novel cell death program leads to neutrophil extracellular traps

Fuchs, T. A., Abed, U., Goosmann, C., Hurwitz, R., Schulze, I., Wahn, V., Weinrauch, Y., Brinkmann, V., & Zychlinsky, A. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200606027 · Cited by 3,197

Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production

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H 2 O 2 , a Necessary Evil for Cell Signaling

Rhee, S. G. (2006) · Science · doi:10.1126/science.1130481 · Cited by 2,160

Redox-based regulation of signal transduction: principles, pitfalls, and promises

Janssen-Heininger, Y. M. W., Mossman, B. T., Heintz, N. H., Forman, H. J., Kalyanaraman, B., Finkel, T., Stamler, J. S., Rhee, S. G., & van der Vliet, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.011 · Cited by 784

Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited

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Role of oxygen gradients in shaping redox relationships between the human intestine and its microbiota

Espey, M. G. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.554 · Cited by 396

Redox Control of Endothelial Function and Dysfunction: Molecular Mechanisms and Therapeutic Opportunities

Thomas, S. R., Witting, P. K., & Drummond, G. R. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2027 · Cited by 383

Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects

Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352

Redox regulation of protein kinases

Corcoran, A., & Cotter, T. G. (2013) · The FEBS Journal · doi:10.1111/febs.12224 · Cited by 306

Reactive Oxygen Species: Physiological and Physiopathological Effects on Synaptic Plasticity: Supplementary Issue: Brain Plasticity and Repair

Beckhauser, T. F., Francis-Oliveira, J., & De Pasquale, R. (2016) · Journal of Experimental Neuroscience · doi:10.4137/jen.s39887 · Cited by 301

Redox signaling and cancer: The role of “labile” iron

Galaris, D., Skiada, V., & Barbouti, A. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.02.038 · Cited by 284

T cells and reactive oxygen species

Belikov, A. V., Schraven, B., & Simeoni, L. (2015) · Journal of Biomedical Science · doi:10.1186/s12929-015-0194-3 · Cited by 264

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Forman, H. J., Fukuto, J. M., Miller, T., Zhang, H., Rinna, A., & Levy, S. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.06.011 · Cited by 226

Stressin’ Sestrins take an aging fight

Budanov, A. V., Lee, J. H., & Karin, M. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000097 · Cited by 208

Glutathione Peroxidase-1 Regulates Mitochondrial Function to Modulate Redox-dependent Cellular Responses

Handy, D. E., Lubos, E., Yang, Y., Galbraith, J. D., Kelly, N., Zhang, Y.-Y., Leopold, J. A., & Loscalzo, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900392200 · Cited by 187

Influence of vitamin C and vitamin E on redox signaling: implications for exercise adaptations

Cobley, J. N., McHardy, H., Morton, J. P., Nikolaidis, M. G., & Close, G. L. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.03.018 · Cited by 118

Reactive oxygen species and uncoupling protein 2 in pancreatic β ‐cell function

Pi, J., & Collins, S. (2010) · Diabetes, Obesity and Metabolism · doi:10.1111/j.1463-1326.2010.01269.x · Cited by 91

Antioxidants in Personalized Nutrition and Exercise

Margaritelis, N. V., Paschalis, V., Theodorou, A. A., Kyparos, A., & Nikolaidis, M. G. (2018) · Advances in Nutrition · doi:10.1093/advances/nmy052 · Cited by 84

Malaria inflammation by xanthine oxidase-produced reactive oxygen species

Ty, M. C., Zuniga, M., Götz, A., Kayal, S., Sahu, P. K., Mohanty, A., Mohanty, S., Wassmer, S. C., & Rodriguez, A. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201809903 · Cited by 73

Protein oxidation: role in signalling and detection by mass spectrometry

Spickett, C. M., & Pitt, A. R. (2012) · Amino Acids · doi:10.1007/s00726-010-0585-4 · Cited by 65

Rescue of anaemia and autoimmune responses in SOD1-deficient mice by transgenic expression of human SOD1 in erythrocytes

Iuchi, Y., Okada, F., Takamiya, R., Kibe, N., Tsunoda, S., Nakajima, O., Toyoda, K., Nagae, R., Suematsu, M., Soga, T., et al. (2009) · Biochemical Journal · doi:10.1042/bj20090176 · Cited by 45

Protective Role of Mitochondrial Peroxiredoxin III against UVB-Induced Apoptosis of Epidermal Keratinocytes

Baek, J. Y., Park, S., Park, J., Jang, J. Y., Wang, S. B., Kim, S. R., Woo, H. A., Lim, K. M., & Chang, T.-S. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.01.027 · Cited by 43

Measuring Mitochondrial Protein Thiol Redox State

Requejo, R., Chouchani, E. T., Hurd, T. R., Menger, K. E., Hampton, M. B., & Murphy, M. P. (2010) · Methods in Enzymology · doi:10.1016/s0076-6879(10)74008-8 · Cited by 31

Reactive Oxygen Species Are Required for 5-HT-Induced Transactivation of Neuronal Platelet-Derived Growth Factor and TrkB Receptors, but Not for ERK1/2 Activation

Kruk, J. S., Vasefi, M. S., Heikkila, J. J., & Beazely, M. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077027 · Cited by 31