Oxyl radicals, redox-sensitive signalling cascades and antioxidants

Genestra, Marcelo

doi:10.1016/j.cellsig.2007.04.009

Cited by 4,930Redox biology and oxidative stressAntioxidant Activity and Oxidative StressNitric Oxide and Endothelin Effects

Oxyl radicals, redox-sensitive signalling cascades and antioxidants

Genestra, Marcelo·2007·Cellular Signalling

DOI 10.1016/j.cellsig.2007.04.009

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Abstract

Oxidative stress is an increase in the reduction potential or a large decrease in the reducing capacity of the cellular redox couples. A particularly destructive aspect of oxidative stress is the production of reactive oxygen species (ROS), which include free radicals and peroxides. Some of the less reactive of these species can be converted by oxidoreduction reactions with transition metals into more aggressive radical species that can cause extensive cellular damage. In animals, ROS may influence cell proliferation, cell death (either apoptosis or necrosis) and the expression of genes, and may be involved in the activation of several signalling pathways, activating cell signalling cascades, such as those involving mitogen-activated protein kinases. Most of these oxygen-derived species are produced at a low level by normal aerobic metabolism and the damage they cause to cells is constantly repaired. The cellular redox environment is preserved by enzymes and antioxidants that maintain the reduced state through a constant input of metabolic energy. This review summarizes current studies that have been regarding the production of ROS and the general redox-sensitive targets of cell signalling cascades.

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“The CYP reaction together with POR releases superoxide as a by-product of the oxidase reaction [36], Figure 14.”
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Superoxide radicals, hydrogen peroxide, singlet oxygen and hypochlorous acid HOCl are generated in the cell membrane through the action of the enzymes NADPH oxidase, myeloperoxidase and xanthine oxidase.
“Superoxide radicals, hydrogen peroxide, singlet oxygen and hypochlorous acid HOCl are generated in the cell membrane through the action of the enzymes NADPH oxidase, myeloperoxidase and xanthine oxidase [35,36].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [36]

Free Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855 · see citing works
Untitled work
Fridovich (1978) · doi:10.1126/science.210504 · Cited by 3,329 · see citing works
NF-κB: Ten Years After
Baeuerle, P. A., & Baltimore, D. (1996) · Cell · doi:10.1016/s0092-8674(00)81318-5 · Cited by 3,002 · see citing works
Requirement for Generation of H 2 O 2 for Platelet-Derived Growth Factor Signal Transduction
Sundaresan, M., Yu, Z.-X., Ferrans, V. J., Irani, K., & Finkel, T. (1995) · Science · doi:10.1126/science.270.5234.296 · Cited by 2,520 · see citing works
Antioxidant and Prooxidant Behavior of Flavonoids: Structure-Activity Relationships
Cao, G., Sofic, E., & Prior, R. L. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00351-6 · Cited by 2,415 · see citing works
Mammalian thioredoxin is a direct inhibitor of apoptosis signal‐regulating kinase (ASK) 1
Saitoh, M., Nishitoh, H., Fujii, M., Takeda, K., Tobiume, K., Sawada, Y., Kawabata, M., Miyazono, K., & Ichijo, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.9.2596 · Cited by 2,377 · see citing works
Induction of Apoptosis by ASK1, a Mammalian MAPKKK That Activates SAPK/JNK and p38 Signaling Pathways
Ichijo, H., Nishida, E., Irie, K., ten Dijke, P., Saitoh, M., Moriguchi, T., Takagi, M., Matsumoto, K., Miyazono, K., & Gotoh, Y. (1997) · Science · doi:10.1126/science.275.5296.90 · Cited by 2,310 · see citing works
NADPH Oxidase: An Update
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147 · see citing works
Alpha-lipoic acid as a biological antioxidant
Packer, L., Witt, E. H., & Tritschler, H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00017-r · Cited by 1,995 · see citing works
Autocrine T-cell suicide mediated by APO-1/(Fas/CD95)
Dhein, J., Walczak, H., Bäumler, C., Debatin, K., & Krammer, P. (1995) · Nature · doi:10.1038/373438a0 · Cited by 1,814 · see citing works
Production of Reactive Oxygen Species by Mitochondria
Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304854200 · Cited by 1,616 · see citing works
Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death.
Zamzami, N., Marchetti, P., Castedo, M., Decaudin, D., Macho, A., Hirsch, T., Susin, S. A., Petit, P. X., Mignotte, B., & Kroemer, G. (1995) · The Journal of experimental medicine · doi:10.1084/jem.182.2.367 · Cited by 1,567 · see citing works
Signal transduction by the c-Jun N-terminal kinase (JNK) — from inflammation to development
Ip, Y. T., & Davis, R. J. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80143-9 · Cited by 1,538 · see citing works
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 · see citing works
The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy
Lemasters, J. J., Nieminen, A.-L., Qian, T., Trost, L. C., Elmore, S. P., Nishimura, Y., Crowe, R. A., Cascio, W. E., Bradham, C. A., Brenner, D. A., et al. (1998) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00112-1 · Cited by 1,387 · see citing works
A Role for Uric Acid in the Progression of Renal Disease
Kang, D., Nakagawa, T., Feng, L., Watanabe, S., Han, L., Mazzali, M., Truong, L. D., Harris, R. C., & Johnson, R. J. (2002) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000034910.58454.fd · Cited by 1,306 · see citing works
Oxidative stress and gene regulation
Allen, R. G., & Tresini, M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00242-7 · Cited by 1,297 · see citing works
Mechanisms of Cell Death in Oxidative Stress
Ryter, S. W., Kim, H. P., Hoetzel, A., Park, J. W., Nakahira, K., Wang, X., & Choi, A. M. K. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.9.49 · Cited by 1,262 · see citing works
Signal transduction via the MAP kinases: proceed at your own RSK.
Blenis, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.5889 · Cited by 1,258 · see citing works
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208 · see citing works
Crystal structure of the Src family tyrosine kinase Hck
Sicheri, F., Moarefi, I., & Kuriyan, J. (1997) · Nature · doi:10.1038/385602a0 · Cited by 1,181 · 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
MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.
Sun, H., Charles, C. H., Lau, L. F., & Tonks, N. K. (1993) · Cell · doi:10.1016/0092-8674(93)90383-2 · Cited by 1,156 · see citing works
Reactive Oxygen Intermediates Mediate a Systemic Signal Network in the Establishment of Plant Immunity
Álvarez, M. E., Pennell, R. I., Meijer, P., Ishikawa, A., Dixon, R. A., & Lamb, C. (1998) · Cell · doi:10.1016/s0092-8674(00)81405-1 · Cited by 1,154 · see citing works
Antioxidant potential of ferulic acid
Graf, E. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90184-i · Cited by 1,115 · see citing works
Regulation of JNK signaling by GSTp
Adler, V., Yin, Z., Fuchs, S. Y., Benezra, M., Rosario, L., Tew, K. D., Pincus, M. R., Sardana, M., Henderson, C. J., Wolf, C. R., et al. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1321 · Cited by 1,105 · see citing works
Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
Meng, T.-C., Fukada, T., & Tonks, N. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00445-8 · Cited by 1,040 · see citing works
Update on Mechanisms of Ischemic Acute Kidney Injury
Devarajan, P. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010017 · Cited by 1,026 · see citing works
Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
Lee, S.-R., Kwon, K.-S., Kim, S.-R., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15366 · Cited by 969 · see citing works
Modulation of Protein Kinase Activity and Gene Expression by Reactive Oxygen Species and Their Role in Vascular Physiology and Pathophysiology
Griendling, K. K., Sorescu, D., Lassegue, B. P., & Ushio‐Fukai, M. (2000) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.20.10.2175 · Cited by 955 · see citing works
Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
Hubbard, S. R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5572 · Cited by 954 · see citing works
Free radical-induced damage to DNA: mechanisms and measurement
Dizdaroglu, M., Jaruga, P., Birincioglu, M., & Rodriguez, H. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00826-2 · Cited by 953 · see citing works
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 · see citing works
Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation.
Schulze‐Osthoff, K., Bakker, A. C., Vanhaesebroeck, B., Beyaert, R., Jacob, W. A., & Fiers, W. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42768-8 · Cited by 935 · see citing works
Lipotoxicity: when tissues overeat
Schaffer, J. E. (2003) · Current Opinion in Lipidology · doi:10.1097/00041433-200306000-00008 · Cited by 914 · see citing works
Towards the physiological function of uric acid
Becker, B. F. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90143-i · Cited by 833 · see citing works
Nuclear factor κB is activated in macrophages and epithelial cells of inflamed intestinal mucosa
Rogler, G., Brand, K., Vogl, D., Page, S., Hofmeister, R., Andus, T., Knuechel, R., Baeuerle, P. A., Schölmerich, J., & Groß, V. (1998) · Gastroenterology · doi:10.1016/s0016-5085(98)70202-1 · Cited by 715 · see citing works
Extracellular Signal-Regulated Kinase and p38 Subgroups of Mitogen-Activated Protein Kinases Regulate Inducible Nitric Oxide Synthase and Tumor Necrosis Factor-α Gene Expression in Endotoxin-Stimulated Primary Glial Cultures
Bhat, N. R., Zhang, P., Lee, J. C., & Hogan, E. L. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-05-01633.1998 · Cited by 714 · see citing works
New concepts in reactive oxygen species and cardiovascular reperfusion physiology
Becker, L. C. (2003) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.10.025 · Cited by 703 · see citing works
Role of redox potential and reactive oxygen species in stress signaling
Adler, V., Yin, Z., Tew, K. D., & Ronai, Z. A. (1999) · Oncogene · doi:10.1038/sj.onc.1203128 · Cited by 691 · see citing works
Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats.
Aikawa, R., Komuro, I., Yamazaki, T., Zou, Y., Kudoh, S., Tanaka, M. H., Shiojima, I., Hiroi, Y., & Yazaki, Y. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119709 · Cited by 687 · see citing works
Complex I-mediated reactive oxygen species generation: modulation by cytochrome c and NAD(P)+ oxidation–reduction state
Kushnareva, Y., Murphy, A. N., & Andreyev, A. Y. (2002) · Biochemical Journal · doi:10.1042/bj20021121 · Cited by 677 · see citing works
p38 Mitogen-activated Protein Kinase Is a Critical Component of the Redox-sensitive Signaling Pathways Activated by Angiotensin II
Ushio‐Fukai, M., Alexander, R. W., Akers, M., & Griendling, K. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.15022 · Cited by 650 · see citing works
ASK1 Is Essential for JNK/SAPK Activation by TRAF2
Nishitoh, H., Saitoh, M., Mochida, Y., Takeda, K., Nakano, H., Rothe, M., Miyazono, K., & Ichijo, H. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80283-x · Cited by 647 · see citing works
Mitochondrial calcium signalling and cell death: Approaches for assessing the role of mitochondrial Ca2+ uptake in apoptosis
Hajnóczky, G., Csordás, G., Das, S., Garcı́a-Pérez, C., Saotome, M., Roy, S. S., & Yi, M. (2006) · Cell Calcium · doi:10.1016/j.ceca.2006.08.016 · Cited by 613 · see citing works
Activation of protein kinase C by tyrosine phosphorylation in response to H 2 O 2
Konishi, H., Tanaka, M., Takemura, Y., Matsuzaki, H., Ono, Y., Kikkawa, U., & Nishizuka, Y. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11233 · Cited by 604 · see citing works
The thioredoxin system in cancer
Arnér, E. S. J., & Holmgren, A. (2006) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2006.10.009 · Cited by 589 · see citing works
Programmed cell death and Bcl‐2 protection in the absence of a nucleus.
Jacobson, M. D., Burne, J. F., & RAFF, M. C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06459.x · Cited by 548 · see citing works
Regulation of gene expression by insulin
O’Brien, R. M., & Granner, D. K. (1996) · Physiological Reviews · doi:10.1152/physrev.1996.76.4.1109 · Cited by 547 · see citing works
Activation of Apoptosis Signal-Regulating Kinase 1 (ASK1) by Tumor Necrosis Factor Receptor-Associated Factor 2 Requires Prior Dissociation of the ASK1 Inhibitor Thioredoxin
Liu, H., Nishitoh, H., Ichijo, H., & Kyriakis, J. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.6.2198-2208.2000 · Cited by 545 · see citing works
Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents.
Knebel, A., Rahmsdorf, H. J., Ullrich, A., & Herrlich, P. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00916.x · Cited by 514 · see citing works
Activation of the Protein Kinase ERK5/BMK1 by Receptor Tyrosine Kinases
Kamakura, S., Moriguchi, T., & Nishida, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26563 · Cited by 514 · see citing works
Inhibition of cell proliferation by alpha-tocopherol. Role of protein kinase C.
Boscoboinik, D. O., Szewczyk, A. M., Hensey, C. E., & Azzi, A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38102-x · Cited by 507 · see citing works
Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
Yamaguchi, H. Q., & Hendrickson, W. A. (1996) · Nature · doi:10.1038/384484a0 · Cited by 495 · see citing works
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 · see citing works
A cascade of tyrosine autophosphorylation in the beta-subunit activates the phosphotransferase of the insulin receptor.
White, M. F., Shoelson, S. E., Keutmann, H. T., & Kahn, C. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69163-x · Cited by 476 · see citing works
Purification of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase
Dupuy, C., Ohayon, R., Valent, A., Noël‐Hudson, M., Dème, D., & Virion, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37265 · Cited by 464 · see citing works
Interactions of oxidants with vascular signaling systems
Wolin, M. S. (2000) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.20.6.1430 · Cited by 463 · see citing works
Reactive Oxygen Species Generation and Mitochondrial Dysfunction in the Apoptotic Response to Bortezomib, a Novel Proteasome Inhibitor, in Human H460 Non-small Cell Lung Cancer Cells
Ling, Y., Liebes, L., Zou, Y., & Perez-Soler, R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302559200 · Cited by 458 · see citing works
IκB–NF-κB Structures
Baeuerle, P. A. (1998) · Cell · doi:10.1016/s0092-8674(00)81694-3 · Cited by 443 · see citing works
A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis
Trinei, M., Giorgio, M., Cicalese, A., Barozzi, S., Ventura, A., Migliaccio, E., Milia, E., Padura, I. M., Raker, V. A., Maccarana, M., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1205513 · Cited by 436 · see citing works
The insulinomimetic agents H2O2 and vanadate stimulate protein tyrosine phosphorylation in intact cells.
Heffetz, D., Bushkin, I., Dror, R., & Zick, Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39885-0 · Cited by 429 · see citing works
Activation of an H2O2-generating NADH Oxidase in Human Lung Fibroblasts by Transforming Growth Factor β1
Thannickal, V. J., & Fanburg, B. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30334 · Cited by 424 · see citing works
Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
Chadha, A. S., Sytnyk, V., Leshchyns’ka, I., & Schachner, M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200409127 · Cited by 419 · see citing works
Differential Activation of Mitogen-Activated Protein Kinases by H 2 O 2 and O 2 − in Vascular Smooth Muscle Cells
Baas, A. S., & Berk, B. C. (1995) · Circulation Research · doi:10.1161/01.res.77.1.29 · Cited by 416 · see citing works
Redox state is a central modulator of the balance between self-renewal and differentiation in a dividing glial precursor cell
Smith, J., Ladi, E., Mayer-Pröschel, M., & Noble, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170209797 · Cited by 399 · see citing works
Phospholipase A2, reactive oxygen species, and lipid peroxidation in cerebral ischemia
Rao, A. M., & Hatcher, J. F. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.044 · Cited by 392 · see citing works
Thioredoxin Promotes ASK1 Ubiquitination and Degradation to Inhibit ASK1-Mediated Apoptosis in a Redox Activity-Independent Manner
Liu, Y., & Wang, M. (2002) · Circulation Research · doi:10.1161/01.res.0000022160.64355.62 · Cited by 388 · see citing works
The Origin of the Oxidative Burst in Plants
Bolwell, G. P., Butt, V. S., Davies, D. R., et al. (1995) · Free Radical Research · doi:10.3109/10715769509065273 · Cited by 383 · see citing works
Deletion of the p66 Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet
Napoli, C., Martin-Padura, I., de Nigris, F., Giorgio, M., Mansueto, G., Somma, P., Condorelli, M., Sica, G., De Rosa, G., & Pelicci, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0336359100 · Cited by 380 · see citing works
Mitochondria and Ischemia/Reperfusion Injury
Honda, H. M., Kôrge, P., & Weiss, J. N. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1341.022 · Cited by 377 · see citing works
p38 Kinase Is Activated in the Alzheimer's Disease Brain
Hensley, K., Floyd, R. A., Zheng, N., Nael, R., Robinson, K. A., Nguyen, X., Pye, Q. N., Stewart, C. A., Geddes, J., Markesbery, W. R., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722053.x · Cited by 373 · see citing works
Renal lipid metabolism and lipotoxicity
Bobulescu, I. A. (2010) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e32833aa4ac · Cited by 366 · see citing works
Neuronal Nitric Oxide Synthase Activation and Peroxynitrite Formation in Ischemic Stroke Linked to Neural Damage
Eliasson, M. J. L., Huang, Z., Ferrante, R. J., Sasamata, M., Molliver, M. E., Snyder, S. H., & Moskowitz, M. A. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-14-05910.1999 · Cited by 366 · see citing works
Roles of Superoxide Radical Anion in Signal Transduction Mediated by Reversible Regulation of Protein-tyrosine Phosphatase 1B
Barrett, W. C., DeGnore, J. P., Keng, Y., Zhang, Z., Yim, M. B., & Chock, P. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34543 · Cited by 355 · see citing works
Structural Basis for Autoinhibition of the EphB2 Receptor Tyrosine Kinase by the Unphosphorylated Juxtamembrane Region
Wybenga-Groot, L. E., Baskin, B., Ong, S. H., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00496-2 · Cited by 341 · see citing works
rac1 Regulates a Cytokine-Stimulated, Redox-Dependent Pathway Necessary for NF-κB Activation
Sulciner, D. J., Irani, K., Yu, Z., Ferrans, V. J., Goldschmidt‐Clermont, P. J., & Finkel, T. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.7115 · Cited by 339 · see citing works
Redox Paradox
Goldstein, B. J., Mahadev, K., & Wu, X. (2005) · Diabetes · doi:10.2337/diabetes.54.2.311 · Cited by 326 · see citing works
Childhood obesity.
Lakshman, R., Elks, C. E., & Ong, K. K. (2012) · Circulation · doi:10.1161/circulationaha.111.047738 · Cited by 318 · see citing works
Divergent signalling via APO‐1/Fas and the TNF receptor, two homologous molecules involved in physiological cell death.
Schulze‐Osthoff, K., Krammer, P., & Dröge, W. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06780.x · Cited by 302 · see citing works
S-Glutathiolation of Ras Mediates Redox-sensitive Signaling by Angiotensin II in Vascular Smooth Muscle Cells
Adachi, T. K., Pimentel, D. R., Heibeck, T. H., Hou, X., Lee, Y. J., Jiang, B., Ido, Y., & Cohen, R. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313320200 · Cited by 301 · see citing works
Blockade of p38 Mitogen-activated Protein Kinase Pathway Inhibits Inducible Nitric-oxide Synthase Expression in Mouse Astrocytes
Silva, J. D., Pierrat, B., Mary, J., & Lesslauer, W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28373 · Cited by 301 · see citing works
MEKK1 Is Required for MPK4 Activation and Regulates Tissue-specific and Temperature-dependent Cell Death in Arabidopsis
Ichimura, K., Casais, C., Peck, S. C., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605319200 · Cited by 300 · see citing works
Hydrogen Peroxide Generated during Cellular Insulin Stimulation Is Integral to Activation of the Distal Insulin Signaling Cascade in 3T3-L1 Adipocytes
Mahadev, K., Wu, X., Zilbering, A., Zhu, L., Lawrence, J. T. R., & Goldstein, B. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105061200 · Cited by 298 · see citing works
The Life Span Determinant p66Shc Localizes to Mitochondria Where It Associates with Mitochondrial Heat Shock Protein 70 and Regulates Trans-membrane Potential
Orsini, F., Migliaccio, E., Moroni, M., Contursi, C., Raker, V. A., Piccini, D., Martín-Padura, I., Pelliccia, G., Trinei, M., Bono, M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401844200 · Cited by 293 · see citing works
Crystal structures of the myristylated catalytic subunit of cAMP‐dependent protein kinase reveal open and closed conformations
Zheng, J., Knighton, D. R., Taylor, S. S., Xuong, N., Sowadski, J. M., & Eyck, L. F. T. (1993) · Protein Science · doi:10.1002/pro.5560021003 · Cited by 281 · see citing works
Molecular Determinants of Selectivity in 5-Hydroxytryptamine1B Receptor-G Protein Interactions
Bae, H., Anderson, K., Flood, L. A., Skiba, N. P., Hamm, H. E., & Graber, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32071 · Cited by 278 · see citing works
Distinct effects of glutathione disulphide on the nuclear transcription factors κB and the activator protein‐1
Galter, D., Mihm, S., & Dröge, W. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18776.x · Cited by 275 · see citing works
c-Src Is Required for Oxidative Stress-mediated Activation of Big Mitogen-activated Protein Kinase 1 (BMK1)
Abe, J., Takahashi, M., Ishida, M., Lee, J.-D., & Berk, B. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.33.20389 · Cited by 272 · see citing works
UV-induced signal transduction
Bender, K., Blattner, C., Knebel, A., Iordanov, M. S., Herrlich, P., & Rahmsdorf, H. J. (1997) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(96)07459-3 · Cited by 267 · see citing works
Src and Cas Mediate JNK Activation but Not ERK1/2 and p38 Kinases by Reactive Oxygen Species
Yoshizumi, M., Abe, J., Haendeler, J., Huang, Q., & Berk, B. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11706 · Cited by 263 · see citing works
Regulation by Insulin of Gene Expression in Human Skeletal Muscle and Adipose Tissue
Ducluzeau, P., Peretti, N., Laville, M., Andréelli, F., Véga, N., Riou, J. P., & Vidal, H. (2001) · Diabetes · doi:10.2337/diabetes.50.5.1134 · Cited by 263 · see citing works
Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis
Gaut, J. P., Yeh, G. C., Tran, H. D., Byun, J., Henderson, J. P., Richter, G. M., Brennan, M., Lusis, A. J., Belaaouaj, A., Hotchkiss, R. S., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211190298 · Cited by 262 · see citing works
Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
Zhu, X., Kim, J. L., Newcomb, J. R., Rose, P., Stover, D. R., Toledo, L. M., Zhao, H., & Morgenstern, K. A. (1999) · Structure · doi:10.1016/s0969-2126(99)80086-0 · Cited by 257 · see citing works
Determination of the mechanism of free radical generation in human aortic endothelial cells exposed to anoxia and reoxygenation.
Zweier, J. L., Broderick, R., Kuppusamy, P., Thompson-Gorman, S. L., & Lutty, G. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51062-6 · Cited by 244 · see citing works
Redox Regulation of Cellular Stress Response in Aging and Neurodegenerative Disorders: Role of Vitagenes
Calabrese, V., Guagliano, E., Sapienza, M. A., Panebianco, M., Calafato, S., Puleo, E., Pennisi, G., Mancuso, C., Butterfield, D. A., & Stella, A. G. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9203-y · Cited by 241 · see citing works
Pathophysiological Roles of ASK1-MAP Kinase Signaling Pathways
Nagai, H., Noguchi, T., Takeda, K., & Ichijo, H. (2007) · BMB Reports · doi:10.5483/bmbrep.2007.40.1.001 · Cited by 239 · see citing works
Hydrogen Peroxide as a Paracrine Vascular Mediator: Regulation and Signaling Leading to Dysfunction
Ardanaz, N., & Pagano, P. J. (2006) · Experimental Biology and Medicine · doi:10.1177/153537020623100302 · Cited by 228 · see citing works
Expression and Modulation of an NADPH Oxidase in Mammalian Astrocytes
Abramov, A. Y., Jacobson, J., Wientjes, F. B., Hothersall, J. S., Canevari, L., & Duchen, M. R. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1632-05.2005 · Cited by 228 · see citing works
Myeloperoxidase produces nitrating oxidants in vivo
Gaut, J. P., Byun, J., Tran, H. D., Lauber, W. M., Carroll, J. A., Hotchkiss, R. S., Belaaouaj, A., & Heinecke, J. W. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15021 · Cited by 225 · see citing works
The Role of p38 Mitogen-Activated Protein Kinase in IL-1β Transcription
Baldassare, J. J., Bi, Y., & Bellone, C. J. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.9.5367 · Cited by 224 · see citing works
Fas mediates apoptosis in human monocytes by a reactive oxygen intermediate dependent pathway
Um, H., Orenstein, J. M., & Wahl, S. M. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.9.3469 · Cited by 223 · see citing works
Novel pharmacological approaches to the treatment of renal ischemia-reperfusion injury: a comprehensive review
Chatterjee, P. K. (2007) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-007-0183-5 · Cited by 221 · see citing works
A new concept of cellular uptake and intracellular trafficking of long‐chain fatty acids
Stremmel, W., Pohl, J., Ring, A., & Herrmann, T. R. W. (2001) · Lipids · doi:10.1007/s11745-001-0809-2 · Cited by 218 · see citing works
Redox regulation of signal transduction: tyrosine phosphorylation and calcium influx.
Staal, F. J. T., Anderson, M. T., Staal, G. E. J., Herzenberg, L. A., Gitler, C., & Herzenberg, L. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.9.3619 · Cited by 217 · see citing works
Oxidation of Fatty Acids Is the Source of Increased Mitochondrial Reactive Oxygen Species Production in Kidney Cortical Tubules in Early Diabetes
Rosca, M. G., Vazquez, E. J., Chen, Q., Kerner, J., Kern, T. S., & Hoppel, C. L. (2012) · Diabetes · doi:10.2337/db11-1437 · Cited by 216 · see citing works
Oxidative Stress Induces Premature Senescence by Stimulating Caveolin-1 Gene Transcription through p38 Mitogen-Activated Protein Kinase/Sp1–Mediated Activation of Two GC-Rich Promoter Elements
Dasari, A., Bartholomew, J. N., Volonté, D., & Galbiati, F. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1236 · Cited by 215 · see citing works
Regulation by cytokines of extracellular superoxide dismutase and other superoxide dismutase isoenzymes in fibroblasts.
Marklund, S. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50482-3 · Cited by 213 · see citing works
Regulation of Immune Responses by NF-κB/Rel Transcription Factors
Sha, W. C. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.187.2.143 · Cited by 195 · see citing works
NAD(P)H Oxidase-Derived Reactive Oxygen Species as Mediators of Angiotensin II Signaling
Hanna, I. R., Taniyama, Y., Szöcs, K., Ročić, P., & Griendling, K. K. (2002) · Antioxidants and Redox Signaling · doi:10.1089/152308602762197443 · Cited by 194 · see citing works
Erythropoietin: a Model System for Studying Oxygen-Dependent Gene Regulation
Bunn, H. F., Gu, J., Huang, L. E., Park, J., & Zhu, H. (1998) · Journal of Experimental Biology · doi:10.1242/jeb.201.8.1197 · Cited by 187 · see citing works
Macrophages regulate intracellular glutathione levels of lymphocytes. Evidence for an immunoregulatory role of cysteine
Gmünder, H., Eck, H., Benninghoff, B., Roth, S., & Dröge, W. (1990) · Cellular Immunology · doi:10.1016/0008-8749(90)90184-s · Cited by 186 · see citing works
Redox regulation of PTEN and protein tyrosine phosphatases in H2O2‐mediated cell signaling
Cho, S.-H., Lee, C., Ahn, Y., Kim, H., Kim, H., Ahn, C., Yang, K., & Lee, S.-R. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00112-7 · Cited by 185 · see citing works
Activation of the Lck tyrosine protein kinase by hydrogen peroxide requires the phosphorylation of Tyr-394.
Hardwick, J. S., & Sefton, B. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4527 · Cited by 181 · see citing works
Internal pH changes associated with the activity of NADPH oxidase of human neutrophils. Further evidence for the presence of an H+ conducting channel
HENDERSON, L. M., Chappell, J., & Jones, O. (1988) · Biochemical Journal · doi:10.1042/bj2510563 · Cited by 180 · see citing works
Fluid Shear Stress Stimulates Big Mitogen-activated Protein Kinase 1 (BMK1) Activity in Endothelial Cells
Chen, Y., Takahashi, M., Okuda, M., Lee, J., & Berk, B. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.143 · Cited by 176 · see citing works
Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite
Peshenko, I. V., & Shichi, H. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00579-2 · Cited by 170 · see citing works
Comparative toxicity of oleic acid and linoleic acid on Jurkat cells
Cury‐Boaventura, M. F., Pompéia, C., & Curi, R. (2004) · Clinical Nutrition · doi:10.1016/j.clnu.2003.12.004 · Cited by 169 · see citing works
Regulation of gene expression by the small GTPase Rho through the ERK6 (p38γ) MAP kinase pathwayPreprint
Marinissen, M. J., Chiariello, M., & Gutkind, J. S. (2001) · Genes & Development · doi:10.1101/gad.855801 · Cited by 167 · see citing works
The Role of K+Channels in Determining Pulmonary Vascular Tone, Oxygen Sensing, Cell Proliferation, and Apoptosis: Implications in Hypoxic Pulmonary Vasoconstriction and Pulmonary Arterial Hypertension
Moudgil, R., Michelakis, E. D., & Archer, S. L. (2006) · Microcirculation · doi:10.1080/10739680600930222 · Cited by 167 · see citing works
ROS Fusion Tyrosine Kinase Activates a SH2 Domain–Containing Phosphatase-2/Phosphatidylinositol 3-Kinase/Mammalian Target of Rapamycin Signaling Axis to Form Glioblastoma in Mice
Charest, A., Wilker, E., McLaughlin, M. E., Lane, K. M., Gowda, R., Coven, S., McMahon, K., Kovach, S., Feng, Y., Yaffe, M. B., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1193 · Cited by 164 · see citing works
Enhancement of T Cell Receptor Signaling by a Mild Oxidative Shift in the Intracellular Thiol Pool
Hehner, S. P., Breitkreutz, R., Shubinsky, G., Unsoeld, H., Schulze‐Osthoff, K., Schmitz, M. L., & Dröge, W. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.8.4319 · Cited by 163 · see citing works
Hydrogen Peroxide Stimulates c-Src-mediated Big Mitogen-activated Protein Kinase 1 (BMK1) and the MEF2C Signaling Pathway in PC12 Cells
Suzaki, Y., Yoshizumi, M., Kagami, S., Koyama, A. H., Taketani, Y., Houchi, H., Tsuchiya, K., Takeda, E., & Tamaki, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111790200 · Cited by 163 · see citing works
Oxygen sensing and signaling: impact on the regulation of physiologically important genes
Zhu, H., & Bunn, H. F. (1999) · Respiration Physiology · doi:10.1016/s0034-5687(99)00024-9 · Cited by 162 · see citing works
The p66Shc Longevity Gene Is Silenced through Epigenetic Modifications of an Alternative Promoter
Ventura, A., Luzi, L., Pacini, S., Baldari, C. T., & Pelicci, P. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200280200 · Cited by 162 · see citing works
Attenuation of Interstitial Fibrosis and Tubular Apoptosis in db/db Transgenic Mice Overexpressing Catalase in Renal Proximal Tubular Cells
Brezniceanu, M.-L., Liu, F., Wei, C., Chénier, I., Godin, N., Zhang, S., Filep, J. G., Ingelfinger, J. R., & Chan, J. S. D. (2007) · Diabetes · doi:10.2337/db07-0013 · Cited by 161 · see citing works
p66Shc-generated Oxidative Signal Promotes Fat Accumulation
Berniakovich, I., Trinei, M., Stendardo, M., Migliaccio, E., Minucci, S., Bernardi, P., Pelicci, P. G., & Giorgio, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804362200 · Cited by 161 · see citing works
New perspectives on the biochemistry of superoxide anion and the efficiency of superoxide dismutases
Deby, C. M. T., & Goutier, R. (1990) · Biochemical Pharmacology · doi:10.1016/0006-2952(90)90043-k · Cited by 160 · see citing works
Oxidative stress and vascular remodelling
Fortuño, A., José, G. S., Moreno, M. U., Dı́ez, J., & Zalba, G. (2005) · Experimental Physiology · doi:10.1113/expphysiol.2005.030098 · Cited by 155 · see citing works
Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide.
Hayes, G. R., & Lockwood, D. H. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.22.8115 · Cited by 155 · see citing works
Activation of p38MAPK in Microglia After Ischemia
Walton, K. M., DiRocco, R. J., Bartlett, B. A., et al. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70041764.x · Cited by 151 · see citing works
Mitochondrial reactive oxygen species regulate the temporal activation of nuclear factor κB to modulate tumour necrosis factor-induced apoptosis: evidence from mitochondria-targeted antioxidants
Hughes, G., Murphy, M. P., & Ledgerwood, E. C. (2005) · Biochemical Journal · doi:10.1042/bj20050078 · Cited by 151 · see citing works
Differential Oxidation of Protein-tyrosine Phosphatases
Groen, A. J., Lemeer, S., van der Wijk, T., Overvoorde, J., Heck, A. J. R., Östman, A., Barford, D., Slijper, M., & den Hertog, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412424200 · Cited by 142 · see citing works
Reactive Oxygen Species and p38 Mitogen-Activated Protein Kinase Activate Bax to Induce Mitochondrial Cytochrome c Release and Apoptosis in Response to Malonate
Gómez-Lázaro, M., Galindo, M. F., de Mera, R. M. M.-F., Fernández-Gómez, F.-J., Concannon, C. G., Segura, M. F., Comella, J. X., Prehn, J. H. M., & Jordán, J. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.030718 · Cited by 136 · see citing works
Inhibition by Uric Acid of Free Radicals that Damage Biological Molecules
Muraoka, S., & Miura, T. (2003) · Pharmacology & Toxicology · doi:10.1111/j.1600-0773.2003.pto930606.x · Cited by 136 · see citing works
Reactive Oxygen Species and Vascular Signal Transduction Mechanisms
Wolin, M. S. (1996) · Microcirculation · doi:10.3109/10739689609146778 · Cited by 135 · see citing works
Redox signalling in anchorage-dependent cell growth
Chiarugi, P., & Fiaschi, T. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.11.009 · Cited by 134 · see citing works
NADPH Oxidase p22phox and Catalase Gene Variants Are Associated with Biomarkers of Oxidative Stress and Adverse Outcomes in Acute Renal Failure
Perianayagam, M. C., Liangos, O., Kolyada, A. Y., et al. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006070806 · Cited by 134 · see citing works
p38 Kinase Is a Negative Regulator of Angiotensin II Signal Transduction in Vascular Smooth Muscle Cells
Kusuhara, M., Takahashi, E., Peterson, T. E., Abe, J., Ishida, M., Han, J., Ulevitch, R. J., & Berk, B. C. (1998) · Circulation Research · doi:10.1161/01.res.83.8.824 · Cited by 131 · see citing works
Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site
Li, S., Lu, Y., Peng, B., et al. (2006) · Biochemical Journal · doi:10.1042/bj20061066 · Cited by 127 · see citing works
Ion channel blockade attenuates aggregated alpha synuclein induction of microglial reactive oxygen species: relevance for the pathogenesis of Parkinson’s disease
Thomas, M. P., Chartrand, K., Reynolds, A. D., Vitvitsky, V., Banerjee, R. V., & Gendelman, H. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04315.x · Cited by 126 · see citing works
Sequence requirements for formation of conformational variants of tau similar to those found in Alzheimer's disease
Jicha, G. A., Berenfeld, B., & Davies, P. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990315)55:6 · Cited by 123 · see citing works
Effects of H2O2 on protein tyrosine phosphatase activity in HER14 cells
Sullivan, S. G., Chiu, D. T.-Y., Errasfa, M., Wang, J. M., Qi, J.-S., & Stern, A. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90042-6 · Cited by 122 · see citing works
Oxidative Stress Induces Protein Kinase D Activation in Intact Cells
Waldron, R. T., & Rozengurt, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m908959199 · Cited by 121 · see citing works
Oxygen intermediates are triggered early in the cytolytic pathway of human NK cells
Roder, J., Helfand, S. L., Werkmeister, J. A., McGarry, R. C., Beaumont, T. J., & Duwe, A. K. (1982) · Nature · doi:10.1038/298569a0 · Cited by 116 · see citing works
Structural Basis for Recruitment of the Adaptor Protein APS to the Activated Insulin Receptor
Hu, J., Liu, J., Ghirlando, R., Saltiel, A. R., & Hubbard, S. R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00487-8 · Cited by 116 · see citing works
Regulation of Xanthine Oxidoreductase Protein Expression by Hydrogen Peroxide and Calcium
McNally, J. S., Saxena, A., Cai, H. “., Dikalov, S., & Harrison, D. G. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000170827.16296.6e · Cited by 115 · see citing works
Novel Organic Hydroperoxide-Sensing and Responding Mechanisms for OhrR, a Major Bacterial Sensor and Regulator of Organic Hydroperoxide Stress
Panmanee, W., Vattanaviboon, P., Poole, L. B., & Mongkolsuk, S. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.4.1389-1395.2006 · Cited by 115 · see citing works
The Obesity Epidemic and Food Addiction: Clinical Similarities to Drug Dependence
Fortuna, J. L. (2012) · Journal of Psychoactive Drugs · doi:10.1080/02791072.2012.662092 · Cited by 110 · see citing works
No requirement of reactive oxygen intermediates in Fas‐mediated apoptosis
Hug, H., Enari, M., & Nagata, S. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00852-3 · Cited by 107 · see citing works
Laminar flow inhibits TNF-induced ASK1 activation by preventing dissociation of ASK1 from its inhibitor 14-3-3
Liu, Y., Yin, G., Surapisitchat, J., Berk, B. C., & Wang, M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11947 · Cited by 106 · see citing works
Genetic evidence that Shp-2 tyrosine phosphatase is a signal enhancer of the epidermal growth factor receptor in mammals
Qu, C., Yu, W., Azzarelli, B., & Feng, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8528 · Cited by 103 · see citing works
Exchange of Aspartate and Alanine
Abe, K., Hayashi, H., & Maloney, P. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.3079 · Cited by 102 · see citing works
A Dominant-Negative Form of the Major Human Abasic Endonuclease Enhances Cellular Sensitivity to Laboratory and Clinical DNA-Damaging Agents
McNeill, D. R., & Wilson, D. M. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0329 · Cited by 97 · see citing works
Oxidative stress inhibits IFN-α-induced antiviral gene expression by blocking the JAK–STAT pathway
Bona, D. D., Cippitelli, M., Fionda, C., Cammà, C., Licata, A., Santoni, A., & Craxı̀, A. (2006) · Journal of Hepatology · doi:10.1016/j.jhep.2006.01.037 · Cited by 96 · see citing works
Protein kinase C and phospholipase D: intimate interactions in intracellular signaling
Becker, K. P., & Hannun, Y. A. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-4531-7 · Cited by 93 · see citing works
Oxidative stress and redox regulation of phospholipase D in myocardial disease
Tappia, P. S., Dent, M. R., & Dhalla, N. S. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.03.025 · Cited by 91 · see citing works
1001 Protein Kinases Redux—Towards 2000
Hunter, T. (1994) · Seminars in Cell Biology · doi:10.1006/scel.1994.1044 · Cited by 90 · see citing works
In vivo functions of mitogen-activated protein kinases: conclusions from knock-in and knock-out mice
Gerits, N., Kostenko, S., & Moens, U. L. (2007) · Transgenic Research · doi:10.1007/s11248-006-9052-0 · Cited by 89 · see citing works
Chapter 13 Nitrone-Based Free Radical Traps as Neuroprotective Agents in Cerebral Ischaemia and Other Pathologies
Hensley, K., Carney, J. M., Stewart, C. A., Tabatabaie, T., Pye, Q. N., & Floyd, R. A. (1996) · International review of neurobiology · doi:10.1016/s0074-7742(08)60725-4 · Cited by 86 · see citing works
Aldosterone Stimulates Vascular Smooth Muscle Cell Proliferation Via Big Mitogen-Activated Protein Kinase 1 Activation
Ishizawa, K., Izawa, Y., Ito, H., Miki, C., Miyata, K., Fujita, Y., Kanematsu, Y., Tsuchiya, K., Tamaki, T., Nishiyama, A., et al. (2005) · Hypertension · doi:10.1161/01.hyp.0000172622.51973.f5 · Cited by 86 · see citing works
Regulation of T-cell activation and T-cell growth factor (TCGF) production by hydrogen peroxide
Roth, S., & Dröge, W. (1987) · Cellular Immunology · doi:10.1016/0008-8749(87)90224-3 · Cited by 84 · see citing works
Effect of Iodide on Nicotinamide Adenine Dinucleotide Phosphate Oxidase Activity and Duox2 Protein Expression in Isolated Porcine Thyroid Follicles
Morand, S. C., Chaaraoui, M., Kaniewski, J., Dème, D., Ohayon, R., Noël‐Hudson, M., Virion, A., & Dupuy, C. (2003) · Endocrinology · doi:10.1210/en.2002-220981 · Cited by 83 · see citing works
Protective effect of ferulic acid on nicotine-induced DNA damage and cellular changes in cultured rat peripheral blood lymphocytes: A comparison with N-acetylcysteine
Sudheer, A. R., Muthukumaran, S., Kalpana, C., et al. (2006) · Toxicology in Vitro · doi:10.1016/j.tiv.2006.11.006 · Cited by 82 · see citing works
Phosphorylation of the insulin receptor kinase by phosphocreatine in combination with hydrogen peroxide: the structural basis of redox priming
Schmid, E., Hotz‐Wagenblatt, A., Hack, V., & Dröge, W. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.12.1491 · Cited by 81 · see citing works
p66 Inhibits Pro-survival Epidermal Growth Factor Receptor/ERK Signaling during Severe Oxidative Stress in Mouse Renal Proximal Tubule Cells
Arany, I., Faisal, A., Nagamine, Y., & Safirstein, R. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708799200 · Cited by 81 · see citing works
P53 Impairs Endothelium-Dependent Vasomotor Function Through Transcriptional Upregulation of P66shc
Kim, C., Jung, S.-B., Naqvi, A., Hoffman, T. A., DeRicco, J. S., Yamamori, T., Cole, M. P., Jeon, B. H., & Irani, K. (2008) · Circulation Research · doi:10.1161/circresaha.108.181644 · Cited by 81 · see citing works
Retinoids as ligands and coactivators of protein kinase C alpha
Imam, A., Hoyos, B. E., Swenson, C. D., Levi, E., Chua, R. A., Viriya, E. T., & Hämmerling, U. (2000) · The FASEB Journal · doi:10.1096/fj.00-0329fje · Cited by 81 · see citing works
Lipotoxicity in renal proximal tubular cells: Relationship between endoplasmic reticulum stress and oxidative stress pathways
Katsoulieris, E. N., Mabley, J. G., Samai, M. H., Sharpe, M. A., Green, I. C., & Chatterjee, P. K. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.021 · Cited by 80 · see citing works
The Cysteine-Rich Regions of the Regulatory Domains of Raf and Protein Kinase C as Retinoid Receptors
Hoyos, B. E., Imam, A., Chua, R. A., Swenson, C. D., Tong, G., Levi, E., Noy, N., & Hämmerling, U. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.6.835 · Cited by 79 · see citing works
p66SHC: The apoptotic side of Shc proteins
Pellegrini, M., Pacini, S., & Baldari, C. T. (2005) · APOPTOSIS · doi:10.1007/s10495-005-6057-8 · Cited by 78 · see citing works
Conformationally Constrained Analogues of Diacylglycerol (DAG). 16. How Much Structural Complexity Is Necessary for Recognition and High Binding Affinity to Protein Kinase C?
Nacro, K., Bienfait, B., Lee, J., et al. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm9904607 · Cited by 76 · see citing works
Toxicity of aromatic disulphides. I. Generation of superoxide radical and hydrogen peroxide by aromatic disulphides in vitro
Munday, R. (1985) · Journal of Applied Toxicology · doi:10.1002/jat.2550050613 · Cited by 76 · see citing works
Regulation of cardiotrophin-1 expression in mouse embryonic stem cells by HIF-1α and intracellular reactive oxygen species
Ateghang, B., Wartenberg, M., Gassmann, M., & Sauer, H. (2006) · Journal of Cell Science · doi:10.1242/jcs.02798 · Cited by 75 · see citing works
New insights into the roles of ReL/NF-kappa B transcription factors in immune function, hemopoiesis and human disease.
Grossmann, M., Nakamura, Y., Grumont, R., & Gerondakis, S. (1999) · International Journal of Biochemistry and Cell Biology · doi:10.1016/s1357-2725(99)00068-0 · Cited by 73 · see citing works
Redox priming of the insulin receptor β‐chain associated with altered tyrosine kinase activity and insulin responsiveness in the absence of tyrosine autophosphorylation
Schmid, E., Benna, J. E., Galter, D., Klein, G., & Dröge, W. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.10.863 · Cited by 73 · see citing works
Hydrogen peroxide and hydroxyl radicals mediate palmitate-induced cytotoxicity to hepatoma cells: Relation to mitochondrial permeability transition
Srivastava, S., & Chan, C. (2006) · Free Radical Research · doi:10.1080/10715760600943900 · Cited by 73 · see citing works
Albumin-bound fatty acids induce mitochondrial oxidant stress and impair antioxidant responses in proximal tubular cells
Ishola, D., Post, J. A., van Timmeren, M. M., Bakker, S. J. L., Goldschmeding, R., Koomans, H. A., Braam, B. G., & Joles, J. A. (2006) · Kidney International · doi:10.1038/sj.ki.5001629 · Cited by 72 · see citing works
Increased activity and sensitivity of mitochondrial respiratory enzymes to tumor necrosis factor alpha-mediated inhibition is associated with increased cytotoxicity in drug-resistant leukemic cell lines
Jia, L., Kelsey, S., Grahn, M. F., et al. (1996) · Blood · doi:10.1182/blood.v87.6.2401.bloodjournal8762401 · Cited by 72 · see citing works
Energy metabolism and cytotoxicity
Portilla, D. (2003) · Seminars in Nephrology · doi:10.1016/s0270-9295(03)00088-3 · Cited by 70 · see citing works
Intracellular Distribution of Mammalian Protein Kinase a Catalytic Subunit Altered by Conserved Asn2 Deamidation
Pepperkok, R., Hotz‐Wagenblatt, A., König, N., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.715 · Cited by 70 · see citing works
Molecular effects of fermented papaya preparation on oxidative damage, MAP Kinase activation and modulation of the benzo[a]pyrene mediated genotoxicity
Aruoma, O. I., Colognato, R., Fontana, I., Gartlon, J., Migliore, L., Koike, K., Coecke, S., Lamy, E., Mersch‐Sundermann, V., Laurenza, I., et al. (2006) · BioFactors · doi:10.1002/biof.5520260205 · Cited by 69 · see citing works
Src and Cas Are Essentially but Differentially Involved in Angiotensin II-Stimulated Migration of Vascular Smooth Muscle Cells via Extracellular Signal-Regulated Kinase 1/2 and c-Jun NH2-Terminal Kinase Activation
Kyaw, M. H., Yoshizumi, M., Tsuchiya, K., et al. (2004) · Molecular Pharmacology · doi:10.1124/mol.65.4.832 · Cited by 69 · see citing works
Sustained activation of proton channels and NADPH oxidase in human eosinophils and murine granulocytes requires PKC but not cPLA2α activity
Morgan, D., Cherny, V. V., Finnegan, A., et al. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.124248 · Cited by 68 · see citing works
Activation of Nuclear Factor κB In vivo Selectively Protects the Murine Small Intestine against Ionizing Radiation-Induced Damage
Wang, Y., Meng, A., Lang, H., Brown, S. A., Konopa, J. L., Kindy, M. S., Schmiedt, R. A., THOMPSON, J. S., & Zhou, D. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0591 · Cited by 67 · see citing works
Accumulation of nonesterified fatty acids causes the sustained energetic deficit in kidney proximal tubules after hypoxia-reoxygenation
Feldkamp, T., Kribben, A., Roeser, N. F., Senter, R. A., & Weinberg, J. M. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00305.2005 · Cited by 65 · see citing works
Regulation of ribosomal DNA transcription by insulin
Hannan, K. M., Rothblum, L. I., & Jefferson, L. S. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.1.c130 · Cited by 65 · see citing works
Roles for NAD(P)H oxidases and reactive oxygen species in vascular oxygen sensing mechanisms
Wolin, M. S., Burke-Wolin, T., & Mohazzab-H., K. M. (1999) · Respiration Physiology · doi:10.1016/s0034-5687(99)00023-7 · Cited by 64 · see citing works
The role of NADPH oxidase and MAP kinase phosphatase in UV‐B‐dependent gene expression in Arabidopsis
Kalbina, I., & Strid, Å. (2006) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2006.01555.x · Cited by 62 · see citing works
The proximal promoter region of the human heme oxygenase gene contains elements involved in stimulation of transcriptional activity by a variety of agents including oxidants
Tyrrell, R. M., Applegate, L. A., & Tromvoukis, Y. (1993) · Carcinogenesis · doi:10.1093/carcin/14.4.761 · Cited by 62 · see citing works
Acute renal failure: From renal physiology to the renal transcriptome
Safirstein, R. L. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.09110.x · Cited by 60 · see citing works
Cellular Oxidative Processes in Relation to Renal Disease
WARDLE, E. N. (2005) · American Journal of Nephrology · doi:10.1159/000083477 · Cited by 60 · see citing works
Role of MAPK in the Regulation of Double-Stranded RNA- and Encephalomyocarditis Virus-Induced Cyclooxygenase-2 Expression by Macrophages
Steer, S. A., Moran, J. M., Christmann, B. S., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.5.3413 · Cited by 59 · see citing works
Chronic nicotine exposure augments renal oxidative stress and injury through transcriptional activation of p66shc
Arany, I., Clark, J., Reed, D. K., & Juncos, L. A. (2013) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfs596 · Cited by 59 · see citing works
Is obesity a risk factor for chronic kidney disease in children?
Gunta, S. S., & Mak, R. (2013) · Pediatric nephrology (Berlin, West) · doi:10.1007/s00467-012-2353-z · Cited by 58 · see citing works
p66SHC-mediated mitochondrial dysfunction in renal proximal tubule cells during oxidative injury
Arany, I., Faisal, A., Clark, J. S., Vera, T., Baliga, R., & Nagamine, Y. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00639.2009 · Cited by 57 · see citing works
Catalytic Inactivation of Protein Tyrosine Phosphatase CD45 and Protein Tyrosine Phosphatase 1B by Polyaromatic Quinones
Wang, Q., Dubé, D., Friesen, R. W., et al. (2004) · Biochemistry · doi:10.1021/bi035986e · Cited by 56 · see citing works
Inhibition of protein tyrosine phosphatase 1B by reactive oxygen species leads to maintenance of Ca2+ influx following store depletion in HEK 293 cells
Bogeski, I., Bozem, M., Sternfeld, L., Hofer, H. W., & Schulz, I. (2006) · Cell Calcium · doi:10.1016/j.ceca.2006.03.003 · Cited by 56 · see citing works
Activation of c-Raf Kinase by Ultraviolet Light
Hoyos, B., Imam, A., Korichneva, I., Levi, E., Chua, R., & Hammerling, U. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110750200 · Cited by 55 · see citing works
Targeting protein kinase C and “non-kinase” phorbol ester receptors: Emerging concepts and therapeutic implications
Kazanietz, M. G. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.07.034 · Cited by 51 · see citing works

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Apoptosis: A Review of Programmed Cell Death
Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853 · see citing works
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084 · see citing works
Oxidative stress, aging, and diseases
Liguori, I., Russo, G., Curcio, F., Bulli, G., Aran, L., Della-Morte, D., Gargiulo, G., Testa, G., Cacciatore, F., Bonaduce, D., et al. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s158513 · Cited by 3,979 · see citing works
A Mitochondrial Paradigm of Metabolic and Degenerative Diseases, Aging, and Cancer: A Dawn for Evolutionary Medicine
Wallace, D. C. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095751 · Cited by 3,185 · see citing works
Free Radicals, Antioxidants in Disease and Health
Department of Pharmacy, L. S. P. C. H., Pham-Huy, L. A., He, H., Department of Analytical Chemistry, C. P. U., Pham-Huyc, C., & Laboratory of Toxicology, F. O. P. (2008) · International Journal of Biomedical Science · doi:10.59566/ijbs.2008.4089 · Cited by 3,058 · see citing works
Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases
Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-014-0446-0 · Cited by 2,886 · see citing works
Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production
Powers, S. K., & Jackson, M. J. (2008) · Physiological Reviews · doi:10.1152/physrev.00031.2007 · Cited by 2,459 · see citing works
Oxidative Stress: An Essential Factor in the Pathogenesis of Gastrointestinal Mucosal Diseases
Bhattacharyya, A., Chattopadhyay, R., Mitra, S., & Crowe, S. E. (2014) · Physiological Reviews · doi:10.1152/physrev.00040.2012 · Cited by 2,484 · see citing works
The mitochondrial permeability transition pore and its role in cell death
CROMPTON, M. (1999) · Biochemical Journal · doi:10.1042/bj3410233 · Cited by 2,432 · see citing works
Reactive Oxygen Species in Metabolic and Inflammatory Signaling
Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q., & Griendling, K. K. (2018) · Circulation Research · doi:10.1161/circresaha.117.311401 · Cited by 2,081 · see citing works
Ros and ros-mediated cellular signaling
Zhang, J., Wang, X., Vikash, V., Ye, Q., Wu, D., Liu, Y., & Dong, W. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4350965 · Cited by 1,980 · see citing works
Redox regulation of cell survival
Trachootham, D., Lu, W., Ogasawara, M. A., Valle, N. R.-D., & Huang, P. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1957 · Cited by 1,781 · see citing works
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845 · see citing works
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750 · see citing works
Mitochondrial dysfunction and oxidative stress in metabolic disorders - A step towards mitochondria based therapeutic strategies
Bhatti, J. S., Bhatti, G. K., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.010 · Cited by 1,655 · see citing works
Diabetes mellitus and oxidative stress—A concise review
Asmat, U., Abad, K., & Ismail, K. (2016) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2015.03.013 · Cited by 1,570 · see citing works
Selective degradation of mitochondria by mitophagy
Kim, I., Rodriguez-Enriquez, S., & Lemasters, J. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.034 · Cited by 1,558 · see citing works
Determination of Antioxidants by DPPH Radical Scavenging Activity and Quantitative Phytochemical Analysis of Ficus religiosa
Baliyan, S., Mukherjee, R., Priyadarshini, A., Vibhuti, A., Gupta, A., Pandey, R. P., & Chang, C.-M. (2022) · Molecules · doi:10.3390/molecules27041326 · Cited by 1,485 · see citing works
The role of oxidative stress in neurodegenerative diseases
Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355 · see citing works
Adiponectin, Leptin, and Fatty Acids in the Maintenance of Metabolic Homeostasis through Adipose Tissue Crosstalk
Stern, J. H., Rutkowski, J. M., & Scherer, P. E. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.04.011 · Cited by 1,031 · see citing works
Role of oxidative stress in Alzheimer’s disease
HUANG, W.-J., ZHANG, X., & CHEN, W.-W. (2016) · Biomedical Reports · doi:10.3892/br.2016.630 · Cited by 1,023 · see citing works
Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990 · see citing works
ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells
Snezhkina, A. V., Kudryavtseva, A. V., Kardymon, O. L., Savvateeva, M. V., Melnikova, N. V., Krasnov, G. S., & Dmitriev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6175804 · Cited by 934 · see citing works
Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives
Hajam, Y. A., Rani, R., Ganie, S. Y., Sheikh, T. A., Javaid, D., Qadri, S. S., Pramodh, S., Alsulimani, A., Alkhanani, M. F., Harakeh, S., et al. (2022) · Cells · doi:10.3390/cells11030552 · Cited by 915 · see citing works
Pulmonary Oxidative Stress, Inflammation and Cancer: Respirable Particulate Matter, Fibrous Dusts and Ozone as Major Causes of Lung Carcinogenesis through Reactive Oxygen Species Mechanisms
Valavanidis, A., Vlachogianni, T., Fiotakis, K., & Loridas, S. (2013) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph10093886 · Cited by 910 · see citing works
Placental Origins of Chronic Disease
Burton, G. J., Fowden, A. L., & Thornburg, K. L. (2016) · Physiological Reviews · doi:10.1152/physrev.00029.2015 · Cited by 717 · see citing works
Diabetes associated cell stress and dysfunction: role of mitochondrial and non-mitochondrial ROS production and activity.
Newsholme, P., Haber, E. P., Hirabara, S. M., Rebelato, E. L. O., Procopio, J., Morgan, D., Oliveira‐Emilio, H. C., Carpinelli, A. R., & Curi, R. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2007.135871 · Cited by 684 · see citing works
Redox status expressed as GSH:GSSG ratio as a marker for oxidative stress in paediatric tumour patients
ZITKA, O., SKALICKOVA, S., GUMULEC, J., MASARIK, M., ADAM, V., HUBALEK, J., TRNKOVA, L., KRUSEOVA, J., ECKSCHLAGER, T., & KIZEK, R. (2012) · Oncology Letters · doi:10.3892/ol.2012.931 · Cited by 664 · see citing works
Association of Gestational Diabetes With Maternal Disorders of Glucose Metabolism and Childhood Adiposity
Lowe, W. L., Scholtens, D. M., Lowe, L. P., Kuang, A., Nodzenski, M., Talbot, O., Catalano, P. M., Linder, B., Brickman, W. J., Clayton, P., et al. (2018) · JAMA · doi:10.1001/jama.2018.11628 · Cited by 591 · see citing works
Redox regulation of mitochondrial function
Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works
β-Amyloid Peptides Induce Mitochondrial Dysfunction and Oxidative Stress in Astrocytes and Death of Neurons through Activation of NADPH Oxidase
Abramov, A. Y., Canevari, L., & Duchen, M. R. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4042-03.2004 · Cited by 587 · see citing works
The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
Bell, E. L., Klimova, T. A., Eisenbart, J., Moraes, C. T., Murphy, M. P., Budinger, G. R. S., & Chandel, N. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609074 · Cited by 568 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Role of mitochondrial reverse electron transport in ros signaling: Potential roles in health and disease
Scialò, F., Fernández-Ayala, D. J., & Sanz, A. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00428 · Cited by 517 · see citing works
Amyloid Beta and Phosphorylated Tau-Induced Defective Autophagy and Mitophagy in Alzheimer’s Disease
Reddy, P. H., & Oliver, D. M. (2019) · Cells · doi:10.3390/cells8050488 · Cited by 496 · see citing works
The redox stress hypothesis of aging
Sohal, R. S., & Orr, W. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.445 · Cited by 473 · see citing works
Oxidative stress and aberrant signaling in aging and cognitive decline
Dröge, W., & Schipper, H. M. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00294.x · Cited by 479 · see citing works
Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
Childhood and Adolescent Obesity in the United States: A Public Health Concern
Sanyaolu, A., Okorie, C., Qi, X., Locke, J., & Rehman, S. (2019) · Global Pediatric Health · doi:10.1177/2333794x19891305 · Cited by 471 · 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
Immune mechanisms linked to depression via oxidative stress and neuroprogression
Bakunina, N., Pariante, C. M., & Zunszain, P. A. (2015) · Immunology · doi:10.1111/imm.12443 · Cited by 444 · see citing works
Lipid-Based Delivery Systems and Intestinal Lymphatic Drug Transport: A Mechanistic Update
Trevaskis, N. L., Charman, W. N., & Porter, C. J. H. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.09.007 · Cited by 442 · see citing works
The Power of Plasticity—Metabolic Regulation of Hepatic Stellate Cells
Trivedi, P., Wang, S., & Friedman, S. L. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2020.10.026 · Cited by 427 · see citing works
Mitochondria and ageing: Role in heart, skeletal muscle and adipose tissue
Boengler, K., Kosiol, M., Mayr, M., Schulz, R., & Rohrbach, S. (2017) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12178 · Cited by 421 · see citing works
Therapeutic potential of mood stabilizers lithium and valproic acid:Beyond bipolar disorder
Chiu, C.-T., Wang, Z., Hunsberger, J. G., & Chuang, D.-M. (2013) · Pharmacological Reviews · doi:10.1124/pr.111.005512 · Cited by 404 · see citing works
Cell biology of the mitochondrion
van der Bliek, A. M., Sedensky, M. M., & Morgan, P. G. (2017) · Genetics · doi:10.1534/genetics.117.300262 · Cited by 388 · see citing works
Reactive oxygen species and oxidative stress in osteoclastogenesis, skeletal aging and bone diseases
Callaway, D. A., & Jiang, J. X. (2015) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-015-0656-4 · Cited by 393 · see citing works
The role of mitochondria in protection of the heart by preconditioning
Halestrap, A. P., Clarke, S. J., & Khaliulin, I. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.05.008 · Cited by 390 · see citing works
Deletion of the p66 Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet
Napoli, C., Martin-Padura, I., de Nigris, F., Giorgio, M., Mansueto, G., Somma, P., Condorelli, M., Sica, G., De Rosa, G., & Pelicci, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0336359100 · Cited by 380 · see citing works
Redox control of senescence and age-related disease.
Chandrasekaran, A., Idelchik, M. D. P. S., & Melendez, J. A. (2017) · Redox Biology · doi:10.1016/j.redox.2016.11.005 · Cited by 360 · see citing works
Lipotoxicity and Diabetic Nephropathy: Novel Mechanistic Insights and Therapeutic Opportunities
Opazo-Ríos, L., Mas, S., Marín-Royo, G., Mezzano, S., Gómez-Guerrero, C., Moreno, J. A., & Egido, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072632 · Cited by 363 · see citing works
Dietary Sources and Bioactivities of Melatonin
Meng, X., Li, Y., Li, S., Zhou, Y., Gan, R.-Y., Xu, D.-P., & Li, H.-B. (2017) · Nutrients · doi:10.3390/nu9040367 · Cited by 362 · see citing works
Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works
Evolutionary conservation of the clk-1 -dependent mechanism of longevity: loss of mclk1 increases cellular fitness and lifespan in mice
Liu, X., Jiang, N., Hughes, B., Bigras, E., Shoubridge, E., & Hekimi, S. (2005) · Genes & Development · doi:10.1101/gad.1352905 · Cited by 345 · see citing works
Manganese Superoxide Dismutase: Guardian of the Powerhouse
Holley, A. K., Bakthavatchalu, V., Velez-Roman, J. M., & St. Clair, D. K. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12107114 · Cited by 358 · see citing works
Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
Reactive Oxygen Species Regulate T Cell Immune Response in the Tumor Microenvironment
Chen, X., Song, M., Zhang, B., & Zhang, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1580967 · Cited by 326 · see citing works
Lipid accumulation induced by APOE4 impairs microglial surveillance of neuronal-network activity
Victor, M. B., Leary, N., Luna, X., Meharena, H. S., Scannail, A. N., Bozzelli, P. L., Samaan, G., Murdock, M. H., von Maydell, D., Effenberger, A. H., et al. (2022) · Cell Stem Cell · doi:10.1016/j.stem.2022.07.005 · Cited by 316 · see citing works
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 · see citing works
NRF2 as a Therapeutic Target in Neurodegenerative Diseases
Brandes, M. S., & Gray, N. E. (2020) · ASN Neuro · doi:10.1177/1759091419899782 · Cited by 297 · see citing works
Antioxidants, Redox Signaling, and Pathophysiology in Schizophrenia: An Integrative View
Yao, J. K., & Keshavan, M. S. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3603 · Cited by 285 · see citing works
Studies of Mitochondrial and Nonmitochondrial Sources Implicate Nicotinamide Adenine Dinucleotide Phosphate Oxidase(s) in the Increased Skeletal Muscle Superoxide Generation That Occurs During Contractile Activity
Sakellariou, G. K., Vasilaki, A., Palomero, J., Kayani, A., Zibrik, L., McArdle, A., & Jackson, M. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4623 · Cited by 276 · see citing works
Aging Hallmarks and Progression and Age-Related Diseases: A Landscape View of Research Advancement
Tenchov, R., Sasso, J. M., Wang, X., & Zhou, Q. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00531 · Cited by 276 · see citing works
Heme Degradation and Vascular Injury
Belcher, J. D., Beckman, J. D., Balla, G., Balla, J., & Vercellotti, G. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2822 · Cited by 257 · see citing works
Cardiac dysfunction induced by high-fat diet is associated with altered myocardial insulin signalling in rats
Ouwens, D. M., Boer, C., Fodor, M., de Galan, P., Heine, R. J., Maassen, J. A., & Diamant, M. (2005) · Diabetologia · doi:10.1007/s00125-005-1755-x · Cited by 256 · see citing works
ROS-induced ROS release orchestrated by Nox4, Nox2, and mitochondria in VEGF signaling and angiogenesis
Kim, Y.-M., Kim, S.-J., Tatsunami, R., Yamamura, H., Fukai, T., & Ushio-Fukai, M. (2017) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00346.2016 · Cited by 251 · see citing works
NADPH Oxidase-Derived Reactive Oxygen Species Mediate the Cerebrovascular Dysfunction Induced by the Amyloid β Peptide
Park, L., Anrather, J., Zhou, P., Frys, K., Pitstick, R., Younkin, S., Carlson, G. A., & Iadecola, C. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.5207-04.2005 · Cited by 244 · see citing works
Genetic deletion of p66 Shc adaptor protein prevents hyperglycemia-induced endothelial dysfunction and oxidative stress
Camici, G. G., Schiavoni, M., Francia, P., Bachschmid, M., Martin-Padura, I., Hersberger, M., Tanner, F. C., Pelicci, P., Volpe, M., Anversa, P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609656104 · Cited by 249 · see citing works
A Mitochondrial Oscillator Dependent on Reactive Oxygen Species
Cortassa, S., Aon, M. A., Winslow, R. L., & O’Rourke, B. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.041749 · Cited by 235 · see citing works
Mechanisms of selective autophagy and mitophagy: Implications for neurodegenerative diseases
Chu, C. T. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.015 · Cited by 218 · see citing works
Nox enzymes as novel targets for drug development
Lambeth, J. D., Krause, K.-H., & Clark, R. A. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0123-6 · Cited by 212 · see citing works
Friedreich Ataxia Mouse Models with Progressive Cerebellar and Sensory Ataxia Reveal Autophagic Neurodegeneration in Dorsal Root Ganglia
Simon, D., Seznec, H., Gansmuller, A., Carelle, N., Weber, P., Metzger, D., Rustin, P., Koenig, M., & Puccio, H. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4549-03.2004 · Cited by 205 · see citing works
The role of mitochondrial dysfunction in age-related diseases
Lane, R. K., Hilsabeck, T., & Rea, S. L. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.05.021 · Cited by 205 · see citing works
Hypoxic Reactive Oxygen Species Regulate the Integrated Stress Response and Cell Survival
Liu, L., Wise, D. R., Diehl, J. A., & Simon, M. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805056200 · Cited by 206 · see citing works
Purple Corn ( Zea mays L.) Phenolic Compounds Profile and Its Assessment as an Agent Against Oxidative Stress in Isolated Mouse Organs
Ramos-Escudero, F., Muñoz, A. M., Alvarado-Ortíz, C., Alvarado, Á., & Yáñez, J. A. (2012) · Journal of Medicinal Food · doi:10.1089/jmf.2010.0342 · Cited by 204 · see citing works
Altered mitochondrial function in insulin-deficient and insulin-resistant states
Ruegsegger, G. N., Creo, A. L., Cortes, T. M., Dasari, S., & Nair, K. S. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120843 · Cited by 202 · see citing works
Protection against renal ischemia–reperfusion injury in vivo by the mitochondria targeted antioxidant MitoQ
Dare, A. J., Bolton, E. A., Pettigrew, G. J., Bradley, J. A., Saeb-Parsy, K., & Murphy, M. P. (2015) · Redox Biology · doi:10.1016/j.redox.2015.04.008 · Cited by 202 · see citing works
Current Concepts of Neurodegenerative Mechanisms in Alzheimer’s Disease
Magalingam, K. B., Radhakrishnan, A., Ping, N. S., & Haleagrahara, N. (2018) · BioMed Research International · doi:10.1155/2018/3740461 · Cited by 178 · see citing works
Bax inhibition protects against free fatty acid-induced lysosomal permeabilization
Feldstein, A. E., Werneburg, N. W., Li, Z., Bronk, S. F., & Gores, G. J. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00509.2005 · Cited by 174 · see citing works
The sigma-1 receptor protects against cellular oxidative stress and activates antioxidant response elements.
Pal, A., Fontanilla, D., Gopalakrishnan, A., Chae, Y.-K., Markley, J. L., & Ruoho, A. E. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.01.030 · Cited by 177 · see citing works
VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress
Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170 · see citing works
Antioxidant N-acetyl-L-cysteine ameliorates symptoms of premature aging associated with the deficiency of the circadian protein BMAL1
Kondratov, R. V., Vykhovanets, O., Kondratova, A. A., & Antoch, M. P. (2009) · Aging · doi:10.18632/aging.100113 · Cited by 159 · see citing works
Oxidative stress causes bone loss in estrogen-deficient mice through enhanced bone marrow dendritic cell activation
Grassi, F., Tell, G., Robbie-Ryan, M., Gao, Y., Terauchi, M., Yang, X., Romanello, M., Jones, D. P., Weitzmann, M. N., & Pacifici, R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703610104 · Cited by 150 · see citing works
The Eye, Oxidative Damage and Polyunsaturated Fatty Acids
Saccà, S. C., Cutolo, C. A., Ferrari, D., Corazza, P., & Traverso, C. E. (2018) · Nutrients · doi:10.3390/nu10060668 · Cited by 150 · see citing works
Body-mass index and risk of advanced chronic kidney disease: prospective analyses from a primary care cohort of 1.4 million adults in England
Herrington, W. G., Smith, M., Bankhead, C., Matsushita, K., Stevens, S., Holt, T., Hobbs, F. D. R., Coresh, J., & Woodward, M. (2017) · PLOS ONE · doi:10.1371/journal.pone.0173515 · Cited by 141 · see citing works
Lifestyle Modifications and Nutritional Interventions in Aging-Associated Cognitive Decline and Alzheimer's Disease
Bhatti, G. K., Reddy, A. P., Reddy, P. H., & Bhatti, J. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00369 · Cited by 145 · see citing works
MicroRNA miR-27b Rescues Bone Marrow–Derived Angiogenic Cell Function and Accelerates Wound Healing in Type 2 Diabetes Mellitus
Wang, J.-M., Tao, J., Chen, D.-D., Cai, J.-J., Irani, K., Wang, Q., Yuan, H., & Chen, A. F. (2014) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.113.302104 · Cited by 144 · see citing works
Reactive Oxygen-Related Diseases: Therapeutic Targets and Emerging Clinical Indications
Casas, A. I., Dao, V. T.-V., Daiber, A., Maghzal, G. J., Di Lisa, F., Kaludercic, N., Leach, S., Cuadrado, A., Jaquet, V., Seredenina, T., et al. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6433 · Cited by 136 · see citing works
Hippocampal Astrocyte Cultures from Adult and Aged Rats Reproduce Changes in Glial Functionality Observed in the Aging Brain
Bellaver, B., Souza, D. G., Souza, D. O., & Quincozes-Santos, A. (2017) · Molecular Neurobiology · doi:10.1007/s12035-016-9880-8 · Cited by 135 · see citing works
Mitochondrial damage-associated molecular patterns and vascular function
Wenceslau, C. F., McCarthy, C. G., Szasz, T., Spitler, K., Goulopoulou, S., Webb, R. C., & Working Group on DAMPs in Cardiovascular Disease (2014) · European Heart Journal · doi:10.1093/eurheartj/ehu047 · Cited by 135 · see citing works
Melatonin attenuates acute kidney ischemia/reperfusion injury in diabetic rats by activation of the SIRT1/Nrf2/HO-1 signaling pathway
Shi, S., Lei, S., Tang, C., Wang, K., & Xia, Z. (2019) · Bioscience Reports · doi:10.1042/bsr20181614 · Cited by 135 · see citing works
Aryl Hydrocarbon Receptor in Oxidative Stress as a Double Agent and Its Biological and Therapeutic Significance
Grishanova, A. Y., & Perepechaeva, M. L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126719 · Cited by 130 · see citing works
A Possible Site of Superoxide Generation in the Complex I Segment of Rat Heart Mitochondria
Ohnishi, S. T., Ohnishi, T., Muranaka, S., Fujita, H., Kimura, H., Uemura, K., Yoshida, K.-I., & Utsumi, K. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-4117-y · Cited by 123 · see citing works
Manganese superoxide dismutase: Beyond life and death
Holley, A. K., Dhar, S. K., Xu, Y., & St. Clair, D. K. (2012) · Amino Acids · doi:10.1007/s00726-010-0600-9 · Cited by 122 · see citing works
How Inflammation Impinges on NAFLD: A Role for Kupffer Cells
Duarte, N., Coelho, I. C., Patarrão, R. S., Almeida, J. I., Penha-Gonçalves, C., & Macedo, M. P. (2015) · BioMed Research International · doi:10.1155/2015/984578 · Cited by 120 · see citing works
Inhibition of BMI1 induces autophagy-mediated necroptosis
Dey, A., Mustafi, S. B., Saha, S., Kumar Dhar Dwivedi, S., Mukherjee, P., & Bhattacharya, R. (2016) · Autophagy · doi:10.1080/15548627.2016.1147670 · Cited by 97 · see citing works
Coordinated Behavior of Mitochondria in Both Space and Time: A Reactive Oxygen Species-Activated Wave of Mitochondrial Depolarization
Brady, N. R., Elmore, S. P., van Beek, J. J. H. G. M., Krab, K., Courtoy, P. J., Hue, L., & Westerhoff, H. V. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.035097 · Cited by 118 · see citing works
Mass Spectrometry-Based Methods for Identifying Oxidized Proteins in Disease: Advances and Challenges
Verrastro, I., Pasha, S., Jensen, K., Pitt, A., & Spickett, C. (2015) · Biomolecules · doi:10.3390/biom5020378 · Cited by 114 · see citing works
Insight into the Role of the PI3K/Akt Pathway in Ischemic Injury and Post-Infarct Left Ventricular Remodeling in Normal and Diabetic Heart
Walkowski, B., Kleibert, M., Majka, M., & Wojciechowska, M. (2022) · Cells · doi:10.3390/cells11091553 · Cited by 117 · see citing works

TDAG51 deficiency promotes oxidative stress-induced apoptosis through the generation of reactive oxygen species in mouse embryonic fibroblasts
Park, E., Kim, J., Ha, T.-U., et al. (2013) · Experimental & Molecular Medicine · doi:10.1038/emm.2013.67 · Cited by 41 · see citing works
Protection of Shenlian extracts to PM2.5 infected RAW 264.7 cell damage
Liu, X.-C., Li, Y., Wang, Y., et al. (2015) · China Journal of Chinese Materia Medica · doi:10.4268/cjcmm20151025 · Cited by 4 · see citing works
Colonic Cell Proliferation and Apoptosis in Rodent Species
Chapkin, R. S., & Lupton, J. R. (1999) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-4149-3_12 · Cited by 17 · see citing works
Oxidative Stress: Apoptosis in Neuronal Injury
Loh, K. P., Huang, S. H., de Silva, R., Tan, B., & Zhu, Y. Z. (2006) · Current Alzheimer Research · doi:10.2174/156720506778249515 · Cited by 298 · see citing works
Protective Effects of Walnut Extract Against Amyloid Beta Peptide-Induced Cell Death and Oxidative Stress in PC12 Cells
Muthaiyah, B., Essa, M. M., Chauhan, V. P. S., & Chauhan, A. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0533-z · Cited by 168 · see citing works

Authors: Genestra, M.
Affiliations: University of Mississippi Medical Center (US)
Corresponding author: Genestra, Marcelo
Venue: Cellular Signalling
Publisher: Elsevier BV
Published: 2007-09
Volume: 19
Issue: 9
Pages: 1807-1819
ISSN: 0898-6568 (ISSN-L)
DOI: 10.1016/j.cellsig.2007.04.009
OpenAlex: W2078111650
Cited by: 4,930
References: 235
Citations by year: 2026: 13 · 2025: 119 · 2024: 297 · 2023: 395 · 2022: 481 · 2021: 326 · 2020: 299 · 2019: 374 · 2018: 356 · 2017: 405 · 2016: 412 · 2015: 393 · 2014: 159 · 2013: 105 · 2012: 112
FWCI: 8.82
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cellular Signalling (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Keywords: oxidative stress, reactive oxygen species, oxyl radicals, antioxidants, redox signaling, mitogen-activated protein kinase, transition metal catalysis, apoptosis, cell proliferation, gene expression
MeSH terms: Animals, Antioxidants, Humans, Oxidation-Reduction, Signal Transduction, Reactive Oxygen Species, Oxidative Stress, MAP Kinase Signaling System

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Oxyl radicals, redox-sensitive signalling cascades and antioxidants

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