Redox signaling: An evolution from free radicals to aging

Superoxide Dismutase

McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952

Aging: a theory based on free radical and radiation chemistry

Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567

Lung cancer, cardiopulmonary mortality, and long-term exposure to fine particulate air pollution

Pope III, C. A. (2002) · JAMA · doi:10.1001/jama.287.9.1132 · Cited by 8,447

Nanotoxicology: An Emerging Discipline Evolving from Studies of Ultrafine Particles

Oberdörster, G., Oberdörster, E., & Oberdörster, J. (2005) · Environmental Health Perspectives · doi:10.1289/ehp.7339 · Cited by 7,891

Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF‐kappa B transcription factor and HIV‐1.

Schreck, R., RIEBER, P., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07761.x · Cited by 3,793

Untitled work

Fridovich (1978) · doi:10.1126/science.210504 · Cited by 3,329

Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent

Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931

Physiological Roles of Mitochondrial Reactive Oxygen Species

Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632

Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1

Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377

The reaction of NO with superoxide

Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121

Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants

Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947

Superoxide Dismutases

Fridovich, I. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001051 · Cited by 1,753

The cellular production of hydrogen peroxide

Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549

Cell transformation by the superoxide-generating oxidase Mox1

Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480

The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity

Rushmore, T. H., Morton, M. R., & Pickett, C. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99004-6 · Cited by 1,464

Nitric oxide activates guanylate cyclase and increases guanosine 3′:5′-cyclic monophosphate levels in various tissue preparations

Arnold, W. P., Mittal, C. K., Katsuki, S., & Murad, F. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.8.3203 · Cited by 1,459

Oxidants as Stimulators of Signal Transduction

Suzuki, Y. J., Forman, H. J., & Sevanian, A. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00275-4 · Cited by 1,370

Keap1-dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression

McMahon, M., Itoh, K., Yamamoto, M., & Hayes, J. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300931200 · Cited by 1,141

Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice

Ramos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102

Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids

Benedetti, A., Comporti, M., & Esterbauer, H. (1980) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(80)90209-x · Cited by 1,085

Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase 1 gene

Radjendirane, V., & Jaiswal, A. K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.25.14960 · Cited by 1,034

Oxygen poisoning and x-irradiation: a mechanism in common

Gerschman, R., Gilbert, D. L., Nye, S. W., Dwyer, P., & Fenn, W. O. (1954) · Science · doi:10.1126/science.119.3097.623 · Cited by 961 · cited 2×

The role of oxidative stress in ambient particulate matter-induced lung diseases and its implications in the toxicity of engineered nanoparticles

Li, N., Xia, T., & Nel, A. E. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.028 · Cited by 949

Specific and Reversible Inactivation of Protein Tyrosine Phosphatases by Hydrogen Peroxide: Evidence for a Sulfenic Acid Intermediate and Implications for Redox Regulation

Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945

Signaling Functions of Reactive Oxygen Species

Forman, H. J., Maiorino, M., & Ursini, F. (2010) · Biochemistry · doi:10.1021/bi9020378 · Cited by 827

Decline in transcriptional activity of Nrf2 causes age-related loss of glutathione synthesis, which is reversible with lipoic acid

Suh, J. H., Shenvi, S. V., Dixon, B. M., Liu, H., Jaiswal, A. K., Liu, R.-M., & Hagen, T. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400282101 · Cited by 774

How do nutritional antioxidants really work: Nucleophilic tone and para-hormesis versus free radical scavenging in vivo

Forman, H. J., Davies, K. J. A., & Ursini, F. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.045 · Cited by 707

Role of ubiquinone in the mitochondrial generation of hydrogen peroxide

Boveris, A., Cadenas, E., & Stoppani, A. O. M. (1976) · Biochemical Journal · doi:10.1042/bj1560435 · Cited by 655

Superoxide radicals as precursors of mitochondrial hydrogen peroxide

Loschen, G., Azzi, A., Richter, C., & Flohé, L. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80281-4 · Cited by 634

Cellular mechanisms of redox cell signalling: role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products

Levonen, A., Landar, A. L., Ramachandran, A., CEASER, E. K., Dickinson, D. A., Zanoni, G., Morrow, J. D., & Darley-Usmar, V. M. (2004) · Biochemical Journal · doi:10.1042/bj20031049 · Cited by 569

Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity

Bus, J. S., Aust, S. D., & Gibson, J. E. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80481-x · Cited by 539

The γ-Glutamyl Cycle: A Possible Transport System for Amino Acids

Orłowski, M., & Meister, A. (1970) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.67.3.1248 · Cited by 531

Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215

Barrett, W. C., DeGnore, J. P., König, S., Fales, H. M., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Biochemistry · doi:10.1021/bi990240v · Cited by 488

Decreased Zinc Affinity of Amyotrophic Lateral Sclerosis‐Associated Superoxide Dismutase Mutants Leads to Enhanced Catalysis of Tyrosine Nitration by Peroxynitrite

Crow, J. P., Sampson, J. B., Zhuang, Y., Thompson, J. A., & Beckman, J. S. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69051936.x · Cited by 487

Superoxide dismutase and pulmonary oxygen toxicity

Crapo, J., & Tierney, D. (1974) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1974.226.6.1401 · Cited by 461

Relaxation of bovine coronary artery and activation of coronary arterial guanylate cyclase by nitric oxide, nitroprusside and a carcinogenic nitrosoamine.

Gruetter, C. A., Barry, B. K., McNamara, D. B., Gruetter, D. Y., Kadowitz, P. J., & Ignarro, L. J. (1979) · PubMed · Cited by 444

Redox homeostasis: The Golden Mean of healthy living

Ursini, F., Maiorino, M., & Forman, H. J. (2016) · Redox Biology · doi:10.1016/j.redox.2016.01.010 · Cited by 438

Silica binding and toxicity in alveolar macrophages

Hamilton, R. F., Thakur, S. A., & Holian, A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.027 · Cited by 415

Ca2+- and phospholipid-independent activation of protein kinase C by selective oxidative modification of the regulatory domain.

Gopalakrishna, R., & Anderson, W. B. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.17.6758 · Cited by 407

Separation and characterization of the aldehydic products of lipid peroxidation stimulated by carbon tetrachloride or ADP-iron in isolated rat hepatocytes and rat liver microsomal suspensions

Poli, G., Mu, D., Cheeseman, K. H., Slater, T. F., Lang, J., & Esterbauer, H. (1985) · Biochemical Journal · doi:10.1042/bj2270629 · Cited by 360

On the Stability of Bovine Superoxide Dismutase

Forman, H. J., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44055-6 · Cited by 348

Endothelial Cells as Mediators of Vasodilation of Arteries

Furchgott, R. F., Cherry, P. D., Zawadzki, J. V., & Jothianandan, D. (1984) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-198406002-00008 · Cited by 322

Inhibition of prostaglandin biosynthesis by eicosapentaenoic acid

Culp, B. R., Titus, B. G., & Lands, W. E. M. (1979) · Prostaglandins and Medicine · doi:10.1016/0161-4630(79)90068-5 · Cited by 315

Quinone-induced oxidative stress elevates glutathione and induces gamma-glutamylcysteine synthetase activity in rat lung epithelial L2 cells

Shi, M. M., Kugelman, A., Iwamoto, T., Tian, L., & Forman, H. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47224-9 · Cited by 307

An overview of mechanisms of redox signaling

Forman, H. J., Ursini, F., & Maiorino, M. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.01.018 · Cited by 306

Requirements for hydroperoxide by the cyclooxygenase and peroxidase activities of prostaglandin H synthase

Kulmacz, R. J., & Lands, W. E. M. (1983) · Prostaglandins · doi:10.1016/0090-6980(83)90025-4 · Cited by 276

Oxidative Stress and Signal Transduction

Schulze‐Osthoff, K., Bauer, M. K. A., Vogt, M., & Wesselborg, S. (1997) · Springer eBooks · doi:10.1007/978-1-4615-5981-8 · Cited by 275

The lipid peroxidation end product 4‐hydroxy‐2,3‐nonenal up‐regulates transforming growth factor β1 expression in the macrophage lineage: a link between oxidative injury and fibrosclerosis 1

Leonarduzzi, G., Scavazza, A., Biasi, F., Chiarpotto, E., Camandola, S., Vogl, S., Dargel, R., & Poli, G. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.11.9285483 · Cited by 264

EFFECTS OF OXYGEN AT INCREASED PRESSURE

Bean, J. W. (1945) · Physiological Reviews · doi:10.1152/physrev.1945.25.1.1 · Cited by 264

EFFECTS OF OXYGEN AT INCREASED PRESSURE

Bean, J. W. (1945) · Physiological Reviews · doi:10.1152/physrev.1945.25.4.715-s · Cited by 254

Superoxide dismutase: A comparison of rate constants

Forman, H. J., & Fridovich, I. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(73)90636-x · Cited by 252

Up-Regulation of the Human γ-Glutamylcysteine Synthetase Regulatory Subunit Gene Involves Binding of Nrf-2 to an Electrophile Responsive Element

Moinova, H., & Mulcahy, R. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1109 · Cited by 245

Two adjacent AP-1-like binding sites form the electrophile-responsive element of the murine glutathione S-transferase Ya subunit gene.

Friling, R. S., Bergelson, S., & Daniel, V. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.2.668 · Cited by 229

The Role of a Mitochondrial Pathway in the Induction of Apoptosis by Chemicals Extracted from Diesel Exhaust Particles

Hiura, T. S., Li, N., Kaplan, R., Horwitz, M. A., Seagrave, J., & Nel, A. E. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.5.2703 · Cited by 205

Lipid oxidation products in cell signaling

Leonarduzzi, G., Arkan, M. C., Başağa, H., Chiarpotto, E., Sevanian, A., & Poli, G. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00216-1 · Cited by 204

Human glutamate cysteine ligase gene regulation through the electrophile response element

Dickinson, D. A., Levonen, A., Moellering, D. R., Arnold, E. K., Zhang, H., Darley-Usmar, V. M., & Forman, H. J. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.06.011 · Cited by 201

The chemical nature of vitamin C

Svirbely, J. L., & Szent‐Györgyi, A. (1932) · Biochemical Journal · doi:10.1042/bj0260865 · Cited by 196

Identification of a Putative Antioxidant Response Element in the 5′-Flanking Region of the Human γ-Glutamylcysteine Synthetase Heavy Subunit Gene

Mulcahy, R., & Gipp, J. J. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1493 · Cited by 189

The Lipid Peroxidation Product 4‐Hydroxy‐2,3‐Nonenal Increases AP‐1‐Binding Activity Through Caspase Activation in Neurons

Camandola, S., Poli, G., & Mattson, M. P. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0740159.x · Cited by 177

Curcumin alters EpRE and AP‐1 binding complexes and elevates glutamate‐cysteine ligase gene expression

Dickinson, D. A., Iles, K. E., Zhang, H., Blank, V., & Forman, H. J. (2003) · The FASEB Journal · doi:10.1096/fj.02-0566fje · Cited by 176

Detection of Free Radicals Generated during Enzymic Oxidations by the Initiation of Sulfite Oxidation

Fridovich, I., & Handler, P. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63312-0 · Cited by 175

γ-Glutamyl Transpeptidase is Increased by Oxidative Stress in Rat Alveolar L2 Epithelial Cells

Kugelman, A., Choy, H. A., Liu, R., Shi, M. M., Gozal, E., & Forman, H. J. (1994) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.11.5.7946387 · Cited by 166

Nrf2-regulated phase II enzymes are induced by chronic ambient nanoparticle exposure in young mice with age-related impairments

Zhang, H., Liu, H., Davies, K. J. A., Sioutas, C., Finch, C. E., Morgan, T. E., & Forman, H. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.042 · Cited by 155

Cytotoxic aldehydes originating from the peroxidation of liver microsomal lipids

Benedetti, A., Comporti, M., Fulceri, R., & Esterbauer, H. (1984) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(84)90219-4 · Cited by 146

Increased Transcription of the Regulatory Subunit of γ-Glutamylcysteine Synthetase in Rat Lung Epithelial L2 Cells Exposed to Oxidative Stress or Glutathione Depletion

Tian, L., Shi, M. M., & Forman, H. J. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9997 · Cited by 142

C‐Myc is a Nrf2‐interacting protein that negatively regulates phase II genes through their electrophile responsive elements

Levy, S., & Forman, H. J. (2010) · IUBMB Life · doi:10.1002/iub.314 · Cited by 142

Biphasic Effects of 15-Deoxy-Δ 12,14 -Prostaglandin J 2 on Glutathione Induction and Apoptosis in Human Endothelial Cells

Levonen, A., Dickinson, D. A., Moellering, D. R., Mulcahy, R., Forman, H. J., & Darley-Usmar, V. M. (2001) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq1101.098488 · Cited by 141

On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology

Forman, H. J., & Azzi, A. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.5.9141504 · Cited by 139

�ber die Wirkungen von Aldehyden auf gesunde und maligne Zellen, 3. Mitt.: Synthese von homologen 4-Hydroxy-2-alkenalen, II

Esterbauer, H., & Weger, W. (1967) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/bf01167162 · Cited by 135

Differential effects of sulfhydryl reagents on activation and deactivation of the fat cell hexose transport system.

Czech, M. P. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33815-2 · Cited by 133

Oxidative stress: Excited oxygen species and enzyme activity

Cadenas, E., & Sies, H. (1985) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(85)90049-4 · Cited by 132

Variable regulation of glutamate cysteine ligase subunit proteins affects glutathione biosynthesis in response to oxidative stress

Krzywanski, D. M., Dickinson, D. A., Iles, K. E., Wigley, A. F., Franklin, C. C., Liu, R.-M., Kavanagh, T. J., & Forman, H. J. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.11.004 · Cited by 127

Activation of NFκB by the respiratory burst of macrophages

Kaul, N., & Forman, H. J. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)00178-5 · Cited by 125

Role of superoxide radical in mitochondrial dehydrogenase reactions

Forman, H. J., & Kennedy, J. A. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(74)90418-5 · Cited by 122

4-hydroxynonenal induces glutamate cysteine ligase through JNK in HBE1 cells

Dickinson, D. A., Iles, K. E., Watanabe, N., Iwamoto, T., Zhang, H., Krzywanski, D. M., & Forman, H. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00991-7 · Cited by 116

Endogenous hydrogen peroxide and peroxidative metabolism in adipocytes in response to insulin and sulfhydryl reagents

Mukherjee, S. P., Lane, R. H., & Lynn, W. S. (1978) · Biochemical Pharmacology · doi:10.1016/0006-2952(78)90332-5 · Cited by 113

Cigarette Smoke Affects Keratinocytes SRB1 Expression and Localization via H2O2 Production and HNE Protein Adducts Formation

Sticozzi, C., Belmonte, G., Pecorelli, A., Arezzini, B., Gardi, C., Maioli, E., Miracco, C., Toscano, M., Forman, H. J., & Valacchi, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033592 · Cited by 107

�ber die Wirkungen von Aldehyden auf gesunde und maligne Zellen, 2. Mitt.: Synthese von homologen 4-Hydroxy-2-alkenalen, I

Esterbauer, H., & Weger, W. (1967) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/bf01167149 · Cited by 107

Signal Transduction by Reactive Oxygen and Nitrogen Species: Pathways and Chemical Principles

Forman, H. J., Torrès, M., & Fukuto, J. (2003) · Springer eBooks · doi:10.1007/0-306-48412-9 · Cited by 104

DJ-1 protects against oxidative damage by regulating the thioredoxin/ASK1 complex

Im, J., Lee, K.-W., Junn, E., & Mouradian, M. M. (2010) · Neuroscience Research · doi:10.1016/j.neures.2010.04.002 · Cited by 94

FREE RADICAL FORMATION IN RIBOFLAVIN COMPLEXES

Isenberg, I., & Szent‐Györgyi, A. (1958) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.44.9.857 · Cited by 93

gamma-Glutamylcysteine synthetase and GSH increase in quinone-induced oxidative stress in BPAEC

Shi, M. M., Iwamoto, T., & Forman, H. J. (1994) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1994.267.4.l414 · Cited by 88

Differential paraquat uptake and redox kinetics of rat granular pneumocytes and alveolar macrophages.

Forman, H. J., Aldrich, T. K., Posner, M. A., & Fisher, A. B. (1982) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)33077-6 · Cited by 83

Superoxide dismutase as an inhibitor of reactions of semiquinone radicals

Winterbourn, C. C., French, J. K., & Claridge, R. F. C. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80953-3 · Cited by 77

Hydroperoxide-induced Increases in Intracellular Calcium Due to Annexin VI Translocation and Inactivation of Plasma Membrane Ca2+-ATPase

Hoyal, C. R., Thomas, A. P., & Forman, H. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.29205 · Cited by 76

Stimulation of the alveolar macrophage respiratory burst by ADP causes selective glutathionylation of protein tyrosine phosphatase 1B

Rinna, A., Torrès, M., & Forman, H. J. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.03.010 · Cited by 72

Histidine at the active site of superoxide dismutase

Forman, H. J., Evans, H. J., Hill, R. L., & Fridovich, I. (1973) · Biochemistry · doi:10.1021/bi00729a006 · Cited by 70

Activation of Several MAP Kinases upon Stimulation of Rat Alveolar Macrophages: Role of the NADPH Oxidase

Torrès, M., & Forman, H. J. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1225 · Cited by 69

OXYGEN POISONING

Stadie, W., & Haugaard, N. (1945) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41532-8 · Cited by 67

Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cells

Zhang, H., Court, N., & Forman, H. J. (2007) · Redox Report · doi:10.1179/135100007x162266 · Cited by 67

Oxidative Stress and Signal Transduction

Forman, H. J., & Cadenas, E. (1997) · Cited by 66

Multidrug-resistant protein-3 gene regulation by the transcription factor Nrf2 in human bronchial epithelial and non-small-cell lung carcinoma

Mahaffey, C. M., Zhang, H., Rinna, A., Holland, W. S., Mack, P. C., & Forman, H. J. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.03.023 · Cited by 64

Antioxidant enzymes of rat granular pneumocytes. Constitutive levels and effect of hyperoxia.

Forman, H. J., & Fisher, A. B. (1981) · PubMed · Cited by 62

Rat alveolar macrophages require NADPH for superoxide production in the respiratory burst. Effect of NADPH depletion by paraquat.

Forman, H. J., Nelson, J., & Fisher, A. B. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43474-6 · Cited by 60

AP-1 activation through endogenous H2O2 generation by alveolar macrophages

Iles, K. E., Dickinson, D. A., Watanabe, N., Iwamoto, T., & Forman, H. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00840-7 · Cited by 60

The Adp-stimulated Nadph Oxidase Activates The Ask-1/mkk4/jnk Pathway In Alveolar Macrophages

Liu, H., Zhang, H., Iles, K. E., Rinna, A., Merrill, G. F., Yodoi, J., Torrès, M., & Forman, H. J. (2006) · Free Radical Research · doi:10.1080/10715760600758514 · Cited by 57

Possible role of aldehydic lipid peroxidation products as chemoattractants.

Curzio, M., Esterbauer, H., Poli, G., Biasi, F., Cecchini, G., Mauro, C. D., Cappello, N., & Mu, D. (1987) · PubMed · Cited by 55

Role of Protein Kinase C in Basal and Hydrogen Peroxide-Stimulated NF-κB Activation in the Murine Macrophage J774A.1 Cell Line

Kaul, N., Gopalakrishna, R., Gundimeda, U., Choi, J., & Forman, H. J. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0487 · Cited by 54

Vitamin P

BENTHSÁTH, A., Rusznyák, S., & Szent‐Györgyi, A. (1937) · Nature · doi:10.1038/139326b0 · Cited by 52

Glutathione – From antioxidant to post-translational modifier

Forman, H. J. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.11.019 · Cited by 50

The Role of Superoxide and Hydroperoxide in the Reductive Activation of Tryptophan-2,3-dioxygenase

Brady, F., Forman, H. J., & Feigelson, P. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45862-6 · Cited by 47

Silica Induces Macrophage Cytokines through Phosphatidylcholine-Specific Phospholipase C with Hydrogen Peroxide

Liu, H., Zhang, H., & Forman, H. J. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0297oc · Cited by 46

The Sterckfontein Ape

BROOM, R. (1937) · Nature · doi:10.1038/139326a0 · Cited by 44

Electrolytic Univalent Reduction of Oxygen in Aqueous Solution Demonstrated with Superoxide Dismutase

Forman, H. J., & Fridovich, I. (1972) · Science · doi:10.1126/science.175.4019.339 · Cited by 43

Stimulation of the Rat Alveolar Macrophage Respiratory Burst by Extracellular Adenine Nucleotides

Murphy, J. K., Livingston, F. R., Gozal, E., Torrès, M., & Forman, H. J. (1993) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/9.5.505 · Cited by 41

Modulation of the Rat Alveolar Macrophage Respiratory Burst by Hydroperoxides Is Calcium Dependent

Hoyal, C. R., Gozal, E., Zhou, H., Foldenauer, K., & Forman, H. J. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0061 · Cited by 40

4-Hydroxynonenal increases γ-glutamyl transpeptidase gene expression through mitogen-activated protein kinase pathways

Zhang, H., Dickinson, D. A., Liu, R.-M., & Forman, H. J. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.031 · Cited by 39

Modulation of the 5-lipoxygenase activity of MC-9 mast cells: Activation by hydroperoxides

Bryant, R. W., She, H. S., Ng, K., & Siegel, M. I. (1986) · Prostaglandins · doi:10.1016/0090-6980(86)90043-2 · Cited by 36

Effects of t-butyl hydroperoxide on NADPH, glutathione, and the respiratory burst of rat alveolar macrophages

Sutherland, M. W., Nelson, J., Harrison, G., & Forman, H. J. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90509-0 · Cited by 35

TGFβ1 rapidly activates Src through a non-canonical redox signaling mechanism

Zhang, H., Davies, K. J. A., & Forman, H. J. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.01.001 · Cited by 33

Iron-mediated lipid peroxidation and lipid raft disruption in low-dose silica-induced macrophage cytokine production

Premasekharan, G., Nguyen, K., Contreras, J., Ramon, V., Leppert, V. J., & Forman, H. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.018 · Cited by 33

SHP-1 Inhibition by 4-Hydroxynonenal Activates Jun N-Terminal Kinase and Glutamate Cysteine Ligase

Rinna, A., & Forman, H. J. (2008) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2007-0371oc · Cited by 27

Oxygen toxicity: Loss of lung macrophage function without metabolite depletion

Sutherland, M. W., Glass, M., Nelson, J., Lyen, Y., & Forman, H. J. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90120-5 · Cited by 26

Priming of Alveolar Macrophage Respiratory Burst by H2O2 Is Prevented by Phosphatidylcholine-Specific Phospholipase C Inhibitor Tricyclodecan-9-yl-xanthate (D609)

Girón‐Calle, J., Srivatsa, K., & Forman, H. J. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.301.1.87 · Cited by 24

Alteration of serum lipid profile, SRB1 loss, and impaired Nrf2 activation in CDKL5 disorder

Pecorelli, A., Belmonte, G., Meloni, I., Cervellati, F., Gardi, C., Sticozzi, C., De Felice, C., Signorini, C., Cortelazzo, A., Leoncini, S., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.010 · Cited by 23

Release of aldehydes from rat alveolar macrophages exposed in vitro to low concentrations of nitrogen dioxide

Robison, T. W., Forman, H. J., & Thomas, M. J. (1995) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(95)00041-a · Cited by 21

Kinetic evidence indicating the absence during catalysis of an unbound ferroprotoporphyrin form of tryptophan oxygenase

Feigelson, P., & Forman, H. J. (1971) · Biochemistry · doi:10.1021/bi00781a006 · Cited by 19

Postischemic accumulation of the lipid peroxidation product 4-hydroxynonenal in rat small intestine

Grune, T., Siems, W. G., Kowalewski, J., & Esterbauer, H. (1994) · Life Sciences · doi:10.1016/0024-3205(94)00676-8 · Cited by 18

Aberrant Regulation of the MRP3 Gene in Non-small Cell Lung Carcinoma

Mahaffey, C. M., Mahaffey, N., Holland, W. S., Zhang, H., Gandara, D. R., Mack, P. C., & Forman, H. J. (2011) · Journal of Thoracic Oncology · doi:10.1097/jto.0b013e318233d753 · Cited by 17

The Nox Enzymes and the Regulated Generation of Reactive Oxygen Species

Arnold, R. S., & Lambeth, J. D. (2003) · Springer eBooks · doi:10.1007/0-306-48412-9_6 · Cited by 4

Differential paraquat (PO) accumulation and redox kinetics in rat lung cells

Forman, H. J., Aldrich, T. K., Posner, M. A., & Fisher, A. B. (1982) · Federation Proceedings · Cited by 1

Chalcone: A Privileged Structure in Medicinal Chemistry

Zhuang, C., Zhang, W., Sheng, C., Zhang, W., Xing, C., & Miao, Z. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00020 · Cited by 1,538

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Surai, P. F., Kochish, I. I., Fisinin, V. I., & Kidd, M. T. (2019) · Antioxidants · doi:10.3390/antiox8070235 · Cited by 721

Sunlight damage to cellular DNA: focus on oxidatively generated lesions

Schuch, A. P., Moreno, N. C., Schuch, N. J., Menck, C. F. M., & Garcia, C. C. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.029 · Cited by 436

ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications

Moldogazieva, N. T., Mokhosoev, I. M., Feldman, N. B., & Lutsenko, S. V. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1457217 · Cited by 297

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Fatoki, J. O., & Badmus, J. A. (2022) · Journal of Hazardous Materials Advances · doi:10.1016/j.hazadv.2022.100052 · Cited by 304

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Flohé, L. (2020) · Antioxidants · doi:10.3390/antiox9121254 · Cited by 78

Role of Reactive Oxygen Species-Mediated Signaling in Aging

Labunskyy, V. M., & Gladyshev, V. N. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4891 · Cited by 155

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Mailloux, R. J. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02905-z

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Flohé, L. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)73001-9 · Cited by 100

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