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Reactive oxygen species in tumor progression
Open accessAbstract
The generation of reactive oxygen radicals in mammalian cells profoundly affects numerous critical cellular functions, and the absence of efficient cellular detoxification mechanisms which remove these radicals can result in several human diseases. Growing evidence suggests that reactive oxygen species (ROS) within cells act as second messengers in intracellular signaling cascades which induce and maintain the oncogenic phenotype of cancer cells. ROS are tumorigenic by virtue of their ability to increase cell proliferation, survival, cellular migration, and also by inducing DNA damage leading to genetic lesions that initiate tumorigenicity and sustain subsequent tumor progression. However, it is also known that ROS can induce cellular senescence and cell death and can therefore function as anti-tumorigenic agents. Therefore, the mechanisms by which cells respond to reactive oxygen species depends on the molecular background of cell and tissues, the location of ROS production and the concentration of individual ROS species. Carcinoma cells produce ROS at elevated rates in vitro, and in vivo many tumors appear persistent to oxidative stress. Thus, the finding that a diet rich in antioxidants or the elimination of ROS by antioxidant compounds prevents the development of certain cancers provided the setting for subsequent investigation of the tumorigenic actions of reactive oxygen species. This review outlines the current knowledge on the various roles of ROS in tumor development and progression.
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Citations
Cites
Death Receptors: Signaling and Modulation
Ashkenazi, A., & Dixit, V. M. (1998) · Science · doi:10.1126/science.281.5381.1305 · Cited by 5,866
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
Hypoxia — a key regulatory factor in tumour growth
Harris, A. L. (2002) · Nature Reviews Cancer · doi:10.1038/nrc704 · Cited by 5,177
Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
An Essential Role for NF-κB in Preventing TNF-α-Induced Cell Death
Beg, A. A., & Baltimore, D. (1996) · Science · doi:10.1126/science.274.5288.782 · Cited by 3,047
Mitochondrial free radical generation, oxidative stress, and aging
Cadenas, E., & Davies, K. J. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00317-8 · Cited by 3,010
Karin, M., Liu, Z.-G., & Zandi, E. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80068-3 · Cited by 2,893
NF-κB at the crossroads of life and death
Karin, M., & Lin, A. (2002) · Nature Immunology · doi:10.1038/ni0302-221 · Cited by 2,709
Tumor Hypoxia: Definitions and Current Clinical, Biologic, and Molecular Aspects
Hockel, M., & Vaupel, P. (2001) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/93.4.266 · Cited by 2,662 · cited 1×
“This adaptation of tumor cells to hypoxia contributes to the malignant phenotype and to aggressive tumor progression (27), and low oxygen tension in tumors is associated with increased metastasis and poor survival of patients in several squamous tumors (28, 29).”
BackgroundBoveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
TNF- and Cancer Therapy-Induced Apoptosis: Potentiation by Inhibition of NF-κB
Wang, C.-Y., Mayo, M. W., & Baldwin, A. S. (1996) · Science · doi:10.1126/science.274.5288.784 · Cited by 2,617
Suppression of TNF-α-Induced Apoptosis by NF-κB
Van Antwerp, D. J., Martin, S. J., Kafri, T., Green, D. R., & Verma, I. M. (1996) · Science · doi:10.1126/science.274.5288.787 · Cited by 2,581
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Robin Harris, J., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,544
Production of large amounts of hydrogen peroxide by human tumor cells.
Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,526
Prooxidant States and Tumor Promotion
Cerutti, P. A. (1985) · Science · doi:10.1126/science.2981433 · Cited by 2,497
NF-κB in cancer: from innocent bystander to major culprit
Karin, M., Cao, Y., Greten, F. R., & Li, Z.-W. (2002) · Nature Reviews Cancer · doi:10.1038/nrc780 · Cited by 2,478
Tumor necrosis factor signaling
Wajant, H., Pfizenmaier, K., & Scheurich, P. (2003) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401189 · Cited by 2,359
WISEMAN, H., & HALLIWELL, B. (1996) · Biochemical Journal · doi:10.1042/bj3130017 · Cited by 2,345
Cantley, L. C., & Neel, B. G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4240 · Cited by 2,006
Liu, Z.-G., Hsu, H., Goeddel, D. V., & Karin, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81375-6 · Cited by 1,937
Sirtuin activators mimic caloric restriction and delay ageing in metazoans
Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868
Biological effects of resveratrol
Frémont, L. (2000) · Life Sciences · doi:10.1016/s0024-3205(99)00410-5 · Cited by 1,663
Forkhead transcription factor FOXO3a protects quiescent cells from oxidative stress
Kops, G. J. P. L., Dansen, T. B., Polderman, P. E., Saarloos, I., Wirtz, K. W. A., Coffer, P. J., Huang, T.-T., Bos, J. L., Medema, R. H., & Burgering, B. M. T. (2002) · Nature · doi:10.1038/nature01036 · Cited by 1,580
Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
Imlay, J. A., Chin, S. M., & Linn, S. (1988) · Science · doi:10.1126/science.2834821 · Cited by 1,555 · cited 1×
“H2O2 itself is not reactive toward DNA and most of its effects are due to the production of hydroxyl ions via the Fenton reaction (9).”
BackgroundMatrix Metalloproteinases: Biologic Activity and Clinical Implications
Nelson, A. R., Fingleton, B., Rothenberg, M. L., & Matrisian, L. M. (2000) · Journal of Clinical Oncology · doi:10.1200/jco.2000.18.5.1135 · Cited by 1,554
Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543
Regulation of matrix metalloproteinase expression in tumor invasion
Westermarck, J., & Kähäri, V. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.8.781 · Cited by 1,494
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
Schreck, R., Albermann, K., & Baeuerle, P. A. (1992) · Free Radical Research Communications · doi:10.3109/10715769209079515 · Cited by 1,401
Role of resveratrol in prevention and therapy of cancer: preclinical and clinical studies.
Aggarwal, B. B., Bhardwaj, A., Aggarwal, R. S., Seeram, N. P., Shishodia, S., & Takada, Y. (2004) · PubMed · Cited by 1,395
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393
NF-κB Controls Cell Growth and Differentiation through Transcriptional Regulation of Cyclin D1
Guttridge, D. C., Albanese, C., Reuther, J. Y., Pestell, R. G., & Baldwin, A. S. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5785 · Cited by 1,312
TUMOR NECROSIS FACTOR RECEPTOR AND Fas SIGNALING MECHANISMS
Wallach, D., Varfolomeev, E. E., Malinin, N. L., Goltsev, Y. V., Kovalenko, A. V., & Boldin, M. P. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.331 · Cited by 1,312
Persistent oxidative stress in cancer
Toyokuni, S., Okamoto, K., Yodoi, J., & Hiai, H. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01368-b · Cited by 1,219
Activation of Mitogen-activated Protein Kinase by H2O2
Guyton, K. Z., Liu, Y., Gorospe, M., Xu, Q., & Holbrook, N. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4138 · Cited by 1,212
ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
Tobiume, K., Matsuzawa, A., Takahashi, T., Nishitoh, H., Morita, K., Takeda, K., Minowa, O., Miyazono, K., Noda, T., & Ichijo, H. (2001) · EMBO reports · doi:10.1093/embo-reports/kve046 · Cited by 1,210
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I. C., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208
Transcription factors as targets for cancer therapy
Darnell, J. E. (2002) · Nature Reviews Cancer · doi:10.1038/nrc906 · Cited by 1,194
Superoxide and hydrogen peroxide in relation to mammalian cell proliferation
Burdon, R. H. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00198-s · Cited by 1,173
How NF-κB is activated: the role of the IκB kinase (IKK) complex
Karin, M. (1999) · Oncogene · doi:10.1038/sj.onc.1203219 · Cited by 1,156
Rajagopalan, S., Meng, X. P., Ramasamy, S., Harrison, D. G., & Galis, Z. S. (1996) · Journal of Clinical Investigation · doi:10.1172/jci119076 · Cited by 1,141
Aberrant rel/nfkb genes and activity in human cancer
Rayet, B., & Gélinas, C. (1999) · Oncogene · doi:10.1038/sj.onc.1203221 · Cited by 1,110
Oncogenic alterations of metabolism
Dang, C. V., & Semenza, G. L. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01344-9 · Cited by 1,106
Reversible Inactivation of the Tumor Suppressor PTEN by H2O2
Lee, S.-R., Yang, K.-S., Kwon, J., Lee, C., Jeong, W., & Rhee, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111899200 · Cited by 1,057
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
Wang, C.-Y., Cusack, J. C., Liu, R., & Baldwin, A. S. (1999) · Nature Medicine · doi:10.1038/7410 · Cited by 988
The Role of Phosphoinositide 3-Kinase Lipid Products in Cell Function
Rameh, L. E., & Cantley, L. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8347 · Cited by 987
Lin, A. W., Barradas, M., Stone, J. C., van Aelst, L., Serrano, M., & Lowe, S. W. (1998) · Genes & Development · doi:10.1101/gad.12.19.3008 · Cited by 945
Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism
Wong, G. H. W., & Goeddel, D. V. (1988) · Science · doi:10.1126/science.3263703 · Cited by 914
Manna, S. K., Mukhopadhyay, A., & Aggarwal, B. B. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.12.6509 · Cited by 879
c-Myc Can Induce DNA Damage, Increase Reactive Oxygen Species, and Mitigate p53 Function
Vafa, O., Wade, M., Kern, S., Beeche, M., Pandita, T. K., Hampton, G. M., & Wahl, G. M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00520-8 · Cited by 876
IκB Kinase Promotes Tumorigenesis through Inhibition of Forkhead FOXO3a
Hu, M. C.-T., Lee, D.-F., Xia, W., Golfman, L. S., Ou-Yang, F., Yang, J.-Y., Zou, Y., Bao, S., Hanada, N., Saso, H., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00302-2 · Cited by 868
DNA Repair Pathway Stimulated by the Forkhead Transcription Factor FOXO3a Through the Gadd45 Protein
Tran, H., Brunet, A., Grenier, J. M., Datta, S. R., Fornace, A. J., DiStefano, P. S., Chiang, L. W., & Greenberg, M. E. (2002) · Science · doi:10.1126/science.1068712 · Cited by 860
Redox Regulation of Forkhead Proteins Through a p66shc -Dependent Signaling Pathway
Nemoto, S., & Finkel, T. (2002) · Science · doi:10.1126/science.1069004 · Cited by 818
Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
Neumann, C. A., Krause, D. S., Carman, C. V., Das, S., Dubey, D. P., Abraham, J. L., Bronson, R. T., Fujiwara, Y., Orkin, S. H., & Van Etten, R. A. (2003) · Nature · doi:10.1038/nature01819 · Cited by 801
Subbaramaiah, K., Chung, W. J., Michaluart, P., Telang, N., Tanabe, T., Inoue, H., Jang, M., Pezzuto, J. M., & Dannenberg, A. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21875 · Cited by 786
Is NF-kappaB the sensor of oxidative stress?
Li, N., & Karin, M. (1999) · PubMed · Cited by 786
WANG, X., MARTINDALE, J. L., LIU, Y., & HOLBROOK, N. J. (1998) · Biochemical Journal · doi:10.1042/bj3330291 · Cited by 736
Protein kinase C signaling and oxidative stress
Gopalakrishna, R., & Jaken, S. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00221-5 · Cited by 701
Redox regulation of transcriptional activators
Sun, Y., & Oberley, L. W. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)00109-8 · Cited by 692
Recent advances torwards understanding redox mechanisms in the activation of nuclear factor κb
Janssen-Heininger, Y. M. W., Poynter, M. E., & Baeuerle, P. A. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00218-5 · Cited by 666
Tyrosine Phosphorylation of IκB-α Activates NF-κB without Proteolytic Degradation of IκB-α
Imbert, V., Rupec, R. A., Livolsi, A., Pahl, H. L., Traenckner, E. B.-M., Mueller-Dieckmann, C., Farahifar, D., Rossi, B., Auberger, P., Baeuerle, P. A., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)80153-1 · Cited by 660
Meier, B., Radeke, H. H., Selle, S., Younes, M., Sies, H., Resch, K., & Habermehl, G. G. (1989) · Biochemical Journal · doi:10.1042/bj2630539 · Cited by 654
Hydrogen Peroxide: A Key Messenger That Modulates Protein Phosphorylation Through Cysteine Oxidation
Rhee, S. G., Bae, Y. S., Lee, S.-R., & Kwon, J. (2000) · Science's STKE · doi:10.1126/stke.2000.53.pe1 · Cited by 644
Cloning of Two Human Thyroid cDNAs Encoding New Members of the NADPH Oxidase Family
De Deken, X., Wang, D., Many, M.-C., Costagliola, S., Libert, F., Vassart, G., Dumont, J. E., & Miot, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000916200 · Cited by 638
The contribution of endogenous sources of DNA damage to the multiple mutations in cancer
Jackson, A. L., & Loeb, L. A. (2001) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/s0027-5107(01)00091-4 · Cited by 630
Kissner, R., Nauser, T., Bugnon, P., Lye, P. G., & Koppenol, W. H. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970160x · Cited by 629
Metalloproteinases: role in breast carcinogenesis, invasion and metastasis
Duffy, M. J., Maguire, T. M., Hill, A., McDermott, E., & O'Higgins, N. (2000) · Breast Cancer Research · doi:10.1186/bcr65 · Cited by 628
ROS, stress‐activated kinases and stress signaling in cancer
Benhar, M., Engelberg, D., & Levitzki, A. (2002) · The EMBO Reports · doi:10.1093/embo-reports/kvf094 · Cited by 600
Schulze-Osthoff, K., Beyaert, R., Vandevoorde, V., Haegeman, G., & Fiers, W. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05978.x · Cited by 577
Huot, J., Houle, F., Marceau, F., & Landry, J. (1997) · Circulation Research · doi:10.1161/01.res.80.3.383 · Cited by 567
Lo, Y. Y. C., & Cruz, T. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11727 · Cited by 533
Reactive oxygen species in oncogenic transformation
Behrend, L., Henderson, G., & Zwacka, R. M. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311441 · Cited by 531
Shackelford, R. E., Kaufmann, W. K., & Paules, R. S. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00224-0 · Cited by 524
Biological Effects of Resveratrol
Bhat, K. P. L., Kosmeder, J. W., & Pezzuto, J. M. (2001) · Antioxidants & Redox Signaling · doi:10.1089/152308601317203567 · Cited by 507
Skin Tumor-Promoting Activity of Benzoyl Peroxide, a Widely Used Free Radical-Generating Compound
Slaga, T. J., Klein-Szanto, A. J. P., Triplett, L. L., Yotti, L. P., & Trosko, J. E. (1981) · Science · doi:10.1126/science.6791284 · Cited by 502
Takada, Y., Mukhopadhyay, A., Kundu, G. C., Mahabeleshwar, G. H., Singh, S., & Aggarwal, B. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212389200 · Cited by 495
Stivala, L. A., Savio, M., Carafoli, F., Perucca, P., Bianchi, L., Maga, G., Forti, L., Pagnoni, U. M., Albini, A., Prosperi, E., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101846200 · Cited by 492
A Molecular Redox Switch on p21
Lander, H. M., Hajjar, D. P., Hempstead, B. L., Mirza, U. A., Chait, B. T., Campbell, S., & Quilliam, L. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4323 · Cited by 488
Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1
Arnold, R. S., Shi, J., Murad, E., Whalen, A. M., Sun, C. Q., Polavarapu, R., Parthasarathy, S., Petros, J. A., & Lambeth, J. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101505898 · Cited by 486
Regulation of reactive-oxygen-species generation in fibroblasts by Rac 1
SUNDARESAN, M., YU, Z.-X., FERRANS, V. J., SULCINER, D. J., GUTKIND, S., IRANI, K. J., GOLDSCHMIDT-CLERMONT, P. J., & FINKEL, T. (1996) · Biochemical Journal · doi:10.1042/bj3180379 · Cited by 486
Hypochlorous Acid Oxygenates the Cysteine Switch Domain of Pro-matrilysin (MMP-7)
Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106958200 · Cited by 482
Li, P.-F. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.6027 · Cited by 478
Church, S. L., Grant, J. W., Ridnour, L. A., Oberley, L. W., Swanson, P. E., Meltzer, P. S., & Trent, J. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.3113 · Cited by 473
Brown, N. S., & Bicknell, R. (2001) · Breast Cancer Research · doi:10.1186/bcr315 · Cited by 462
CHEN, Q. M., BARTHOLOMEW, J. C., CAMPISI, J., ACOSTA, M., REAGAN, J. D., & AMES, B. N. (1998) · Biochemical Journal · doi:10.1042/bj3320043 · Cited by 445
Mitochondrial redox control of matrix metalloproteinases
Nelson, K. K., & Melendez, J. A. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.06.008 · Cited by 441
Toker, A., & Newton, A. C. (2000) · Cell · doi:10.1016/s0092-8674(00)00110-0 · Cited by 409
Protein tyrosine phosphatases: mechanisms of catalysis and regulation
Denu, J. M., & Dixon, J. E. (1998) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(98)80095-1 · Cited by 399
Cancer Chemopreventive Activity of Resveratrol
BHAT, K. P. L., & PEZZUTO, J. M. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb02918.x · Cited by 398
Role of Rac1 and Oxygen Radicals in Collagenase-1 Expression Induced by Cell Shape Change
Kheradmand, F., Werner, E., Tremble, P., Symons, M., & Werb, Z. (1998) · Science · doi:10.1126/science.280.5365.898 · Cited by 391
Cui, S., Reichner, J. S., Mateo, R. B., & Albina, J. E. (1994) · PubMed · Cited by 374
An overview of the relationship between oxidative stress and chemical carcinogenesis
Trush, M. A., & Kensler, T. W. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90077-g · Cited by 372
Bowden, E. T., Barth, M., Thomas, D., Glazer, R. I., & Mueller, S. C. (1999) · Oncogene · doi:10.1038/sj.onc.1202827 · Cited by 356
Mello Filho, A. C., & Meneghini, R. (1984) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(84)90123-4 · Cited by 347
The role of NF-κB in the regulation of cell stress responses
Wang, T., Zhang, X., & Li, J. J. (2002) · International Immunopharmacology · doi:10.1016/s1567-5769(02)00058-9 · Cited by 343
Hypoxic cervical cancers with low apoptotic index are highly aggressive.
Höckel, M., Schlenger, K., Höckel, S., & Vaupel, P. W. (1999) · PubMed · Cited by 335
SPITZ, D. R., SIM, J. E., RIDNOUR, L. A., GALOFORO, S. S., & LEE, Y. J. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06199.x · Cited by 331
Mitogen-Activated Protein Kinase Cascades as Regulators of Stress Responses
KARIN, M. (1998) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1998.tb08987.x · Cited by 326
Roebuck, K. A. (1999) · International Journal of Molecular Medicine · doi:10.3892/ijmm.4.3.223 · Cited by 325
Protein kinase D mediates a stress-induced NF-kappaB activation and survival pathway
Storz, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg009 · Cited by 325
Self-citationGottlieb, E., Vander Heiden, M. G., & Thompson, C. B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5680-5689.2000 · Cited by 317
Benhar, M., Dalyot, I., Engelberg, D., & Levitzki, A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.20.6913-6926.2001 · Cited by 306
v-SRC'S hold over actin and cell adhesions
Frame, M. C., Fincham, V. J., Carragher, N. O., & Wyke, J. A. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm779 · Cited by 305
Talley, A. K., Dewhurst, S., Perry, S. W., Dollard, S. C., Gummuluru, S., Fine, S. M., New, D., Epstein, L. G., Gendelman, H. E., & Gelbard, H. A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.5.2359 · Cited by 302
Reactive Oxygen Species and Signal Transduction
Finkel, T. (2001) · IUBMB Life · doi:10.1080/15216540252774694 · Cited by 290
Metabolism of oxygen radicals in peroxisomes and cellular implications
del Río, L. A., Sandalio, L. M., Palma, J., Bueno, P., & Corpas, F. J. (1992) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(92)90150-f · Cited by 285
Arrigo, A. (1998) · PubMed · Cited by 285
Invited Review: Oxygen sensing during intermittent hypoxia: cellular and molecular mechanisms
Prabhakar, N. R. (2001) · Journal of Applied Physiology · doi:10.1152/jappl.2001.90.5.1986 · Cited by 278
van Wetering, S., van Buul, J. D., Quik, S., Mul, F. P. J., Anthony, E. C., Klooster, J.-P. T., Collard, J. G., & Hordijk, P. L. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.9.1837 · Cited by 278
Interaction of an NF-kappa B-like factor with a site upstream of the c-myc promoter.
Duyao, M. P., Buckler, A. J., & Sonenshein, G. E. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4727 · Cited by 278
Konishi, H., Matsuzaki, H., Tanaka, M., Takemura, Y., Kuroda, S., Ono, Y., & Kikkawa, U. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00541-3 · Cited by 270
Maulik, N., & Das, D. K. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01005-5 · Cited by 267
Superoxide dismutase protects calcineurin from inactivation
Wang, X., Culotta, V. C., & Klee, C. B. (1996) · Nature · doi:10.1038/383434a0 · Cited by 266
Carballo, M., Conde, M., El Bekay, R., Martı́n-Nieto, J., Camacho, M. J., Monteseirı́n, J., Conde, J., Bedoya, F. J., & Sobrino, F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17580 · Cited by 266
SHAW, M., COHEN, P., & ALESSI, D. R. (1998) · Biochemical Journal · doi:10.1042/bj3360241 · Cited by 261
Yokomizo, A., Ono, M., Nanri, H., Makino, Y., Ohga, T., Wada, M., Okamoto, T., Yodoi, J., Kuwano, M., & Kohno, K. (1995) · PubMed · Cited by 237
Peroxiredoxins in breast carcinoma.
Karihtala, P., Mäntyniemi, A., Kang, S. W., Kinnula, V. L., & Soini, Y. (2003) · PubMed · Cited by 232
Storz, P., Döppler, H., & Toker, A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2614-2626.2004 · Cited by 227
Self-citationWenk, J., Brenneisen, P., Wlaschek, M., Poswig, A., Briviba, K., Oberley, T. D., & Scharffetter-Kochanek, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25869 · Cited by 225
Lee, Y. J., Galoforo, S. S., Berns, C. M., Chen, J. C., Davis, B. H., Sim, J. E., Corry, P. M., & Spitz, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5294 · Cited by 225
Bcl-2 Protects Macrophages from Nitric Oxide-induced Apoptosis
Meβmer, U. K., Reed, J. C., & Brüne, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.20192 · Cited by 221
Savitsky, P. A., & Finkel, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201589200 · Cited by 218
Nonn, L., Berggren, M. M., & Powis, G. (2003) · PubMed · Cited by 215
Activation of endothelial cell phospholipase D by hydrogen peroxide and fatty acid hydroperoxide.
Natarajan, V., Taher, M. M., Roehm, B., Parinandi, N. L., Schmid, H. H., Kiss, Z., & Garcia, J. G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54023-0 · Cited by 211
Oxidative Stress and AP-1 Activity in Tamoxifen-Resistant Breast Tumors In Vivo
Schiff, R. (2000) · Journal of the National Cancer Institute · doi:10.1093/jnci/92.23.1926 · Cited by 211
Reed, S. G., Nathan, C. F., Pihl, D. L., Rodricks, P., Shanebeck, K., Conlon, P. J., & Grabstein, K. H. (1987) · The Journal of experimental medicine · doi:10.1084/jem.166.6.1734 · Cited by 209
Hydrogen peroxide as a mediator of programmed cell death in the blastocyst
Pierce, G. B., Parchment, R. E., & Lewellyn, A. L. (1991) · Differentiation · doi:10.1111/j.1432-0436.1991.tb00880.x · Cited by 206
Phospholiphase A2 dependent release of fatty acids from peroxidized membranes
Sevanian, A., & Kim, E. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90130-8 · Cited by 200
The Role of Hydrogen Peroxide in Endothelial Proliferative Responses
Stone, J. R., & Collins, T. (2002) · Endothelium · doi:10.1080/10623320214733 · Cited by 200
Catalase Activity Is Regulated by c-Abl and Arg in the Oxidative Stress Response
Cao, C., Leng, Y., & Kufe, D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301292200 · Cited by 186
Production of hydrogen peroxide by rabbit articular chondrocytes. Enhancement by cytokines.
Tiku, M. L., Liesch, J. B., & Robertson, F. M. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.145.2.690 · Cited by 185
Oxidative Stress and Tumour Cell Proliferation
Burdon, R. H., Gill, V., & Rice-Evans, C. (1990) · Free Radical Research Communications · doi:10.3109/10715769009109669 · Cited by 181
Targeting of protein kinase C delta to mitochondria in the oxidative stress response.
Majumder, P. K., Mishra, N. C., Sun, X., Bharti, A. K., Kharbanda, S. M., Saxena, S. P., & Kufe, D. W. (2001) · PubMed · Cited by 171
Min, D. S., Kim, E.-G., & Exton, J. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29986 · Cited by 170
Activation of the Cytoplasmic c-Abl Tyrosine Kinase by Reactive Oxygen Species
Sun, X., Majumder, P., Shioya, H., Wu, F., Kumar, S., Weichselbaum, R., Kharbanda, S., & Kufe, D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000099200 · Cited by 169
How do Abl family kinases regulate cell shape and movement?
Hernández, S. E., Krishnaswami, M., Miller, A. L., & Koleske, A. J. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2003.11.003 · Cited by 165
The role of AP-1, NF-кB and ROS/ NOS in skin carcinogenesis: The JB6 model is predictive
Dhar, A., Young, M. R., & Colburn, N. H. (2002) · Springer eBooks · doi:10.1007/978-1-4615-1087-1_21 · Cited by 151
Regulation of receptor protein‐tyrosine phosphatase α by oxidative stress
Blanchetot, C., Tertoolen, L. G. J., & den Hertog, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.4.493 · Cited by 145
Oncogenic tyrosine kinases and the dna-damage response
Skórski, T. (2002) · Nature reviews. Cancer · doi:10.1038/nrc799 · Cited by 138
Chung, Y. M., Bae, Y. S., & Lee, S. Y. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01301-1 · Cited by 134
Choi, J. H., Tn, K., Kim, S., Baek, S., Jh, K., Lee, & Kim, J.-R. (2002) · PubMed · Cited by 130
Glutathione Peroxidase 1 Is Regulated by the c-Abl and Arg Tyrosine Kinases
Cao, C., Leng, Y., Huang, W., Liu, X., & Kufe, D. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305770200 · Cited by 128
3'-phosphoinositide-dependent kinase-1 (PDK-1) in PI 3-kinase signaling
Störz, P., & Toker, A. (2002) · Frontiers in bioscience · doi:10.2741/storz · Cited by 119
Tyrosine Phosphorylation of Protein Kinase D in the Pleckstrin Homology Domain Leads to Activation
Störz, P., Döppler, H. R., Johannes, F., & Toker, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213224200 · Cited by 119
Hauck, C. R., Hsia, D. A., Ilić, D., & Schlaepfer, D. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100760200 · Cited by 118
Kim, H. J., Chae, H. Z., KIM, Y., Kim, Y. H., Hwang, T. S., Park, E.-M., & Park, Y.-M. (2003) · Cell Biology and Toxicology · doi:10.1023/b:cbto.0000004952.07979.3d · Cited by 109
Kumar, S., Bharti, A. K., Mishra, N. C., Raina, D., Kharbanda, S. M., Saxena, S. P., & Kufe, D. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101414200 · Cited by 108
Activation Loop Phosphorylation Controls Protein Kinase D-Dependent Activation of Nuclear Factor κB
Störz, P., Döppler, H. R., & Toker, A. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.000687 · Cited by 102
Malignant transformation by mutant Rel proteins
Gilmore, T. D. (1991) · Trends in Genetics · doi:10.1016/0168-9525(91)90421-l · Cited by 98
Reactive oxygen intermediates as second messengers of a general pathogen response.
Pa, B., Ra, R., & Hl, P. (1996) · PubMed · Cited by 95
Focal Adhesion Kinase Regulation by Oxidative Stress in Different Cell Types
Mahdi, M. H. B., Andrieu, V., & Pasquier, C. (2000) · IUBMB Life · doi:10.1080/713803721 · Cited by 93
The Actin Cytoskeleton Reorganization Induced by Rac1 Requires the Production of Superoxide
Moldovan, L., Irani, K., Moldovan, N. I., Finkel, T., & Goldschmidt‐Clermont, P. J. (1999) · Antioxidants and Redox Signaling · doi:10.1089/ars.1999.1.1-29 · Cited by 92
Nauser, T., & Schöneich, C. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0293599 · Cited by 92
Involvement of TRAF4 in Oxidative Activation of c-Jun N-terminal Kinase
Xu, Y. C., Wu, R. F., Gu, Y., Yang, Y. S., Yang, M.-C., Nwariaku, F. E., & Terada, L. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202665200 · Cited by 90
Hydrogen Peroxide in Relation to Proliferation and Apoptosis in BHK-21 Hamster Fibroblasts
Burdon, R. H., Gill, V., & Alliangana, D. (1996) · Free Radical Research · doi:10.3109/10715769609088004 · Cited by 88
Stewart, J. R., & O’Brian, C. A. (2004) · Investigational New Drugs · doi:10.1023/b:drug.0000011787.75522.ec · Cited by 86
Urea-associated oxidative stress and Gadd153/CHOP induction
Zhang, Z., Yang, X.-Y., & Cohen, D. (1999) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.1999.276.5.f786 · Cited by 81
Prasad, N. K., Topping, R. S., Zhou, D., & Decker, S. J. (2000) · Biochemistry · doi:10.1021/bi000387i · Cited by 80
Jones, C. M., Lawrence, A. D., Wardman, P., & Burkitt, M. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311337 · Cited by 80
A STAT3 dimer formed by inter-chain disulphide bridging during oxidative stress
Li, L., & Shaw, P. E. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.014 · Cited by 79
Kundu, N., Zhang, S., & Fulton, A. M. (1995) · Clinical & Experimental Metastasis · doi:10.1007/bf00144014 · Cited by 78
Jackson, J. G., Yoneda, T., Clark, G. M., & Yee, D. (2000) · PubMed · Cited by 78
Wang, Y., Schattenberg, J. M., Rigoli, R. M., Störz, P., & Czaja, M. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404170200 · Cited by 77
The Peroxisome in Oxidative Stress
Dansen, T. B., & WIRTZ, K. W. A. (2001) · IUBMB Life · doi:10.1080/152165401753311762 · Cited by 77
Mammalian Peroxisomes: Metabolism of Oxygen and Reactive Oxygen Species
Singh, I. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb18648.x · Cited by 74
Protein kinase C μ is down-regulated in androgen-independent prostate cancer
Jaggi, M., Rao, P. S., Smith, D. J., Hemstreet, G. P., & Balaji, K. C. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01161-6 · Cited by 73
Integrins and Coagulation: A Role for ROS/Redox Signaling?
Gregg, D., de Carvalho, D. D., & Kovacic, H. (2004) · Antioxidants and Redox Signaling · doi:10.1089/1523086041361604 · Cited by 61
Thiyl radicals abstract hydrogen atoms from carbohydrates: reactivity and selectivity
Pogocki, D. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00559-7 · Cited by 57
Schedule and concentration-dependent induction of apoptosis in leukemia cells by nitric oxide
Shami, P., Sauls, D., & Weinberg, J. (1998) · Leukemia · doi:10.1038/sj.leu.2401131 · Cited by 57
Potential Molecular Mechanisms of Oxidant-Induced Carcinogenesis
Jackson, J. H. (1994) · Environmental Health Perspectives · doi:10.1289/ehp.94102s10155 · Cited by 53
Therapeutic Potential of Natural Compounds that Regulate the Activity of Protein Kinase C
Carter, C. A., & Kane, C. J. M. (2004) · Current Medicinal Chemistry · doi:10.2174/0929867043364090 · Cited by 52
Downregulation of peroxiredoxin V stimulates formation of etoposide‐induced double‐strand DNA breaks
Kropotov, A., Grudinkin, P. S., Pleskach, N. M., Gavrilov, B. A., Tomilin, N., & Zhivotovsky, B. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.011 · Cited by 40
Augmentation of cytokine-induced nitric oxide synthesis by hydrogen peroxide
Milligan, S. A., Owens, M. W., & Grisham, M. B. (1996) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1996.271.1.l114 · Cited by 38
Rust, W. L., Kingsley, K., Petnicki, T., Padmanabhan, S., Carper, S. W., & Plopper, G. E. (1999) · Molecular Cell Biology Research Communications · doi:10.1006/mcbr.1999.0130 · Cited by 32
Lee, S., Na, Y.-P., & Lee, J.-B. (2003) · Journal of the American Academy of Dermatology · doi:10.1067/s0190-9622(03)01485-3 · Cited by 32
A Molecular Redox Switch on p21 ras: STRUCTURAL BASIS FOR THE NITRIC OXIDE-p21rasINTERACTION
Lander, H. M., Quilliam, L. A., Hajjar, D. P., et al. (2021) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/f60b-8440 · Cited by 24
Potential Molecular Mechanisms of Oxidant-Induced Carcinogenesis
Jackson, J. H. (1994) · Environmental Health Perspectives · doi:10.2307/3432232 · Cited by 13
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Free radicals, metals and antioxidants in oxidative stress-induced cancer
Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680
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Metadata
- Authors
- Storz, P.
- Venue
- Frontiers in Bioscience
- Publisher
- IMR Press
- Published
- 2005
- Volume
- 10
- Issue
- 1-3
- Pages
- 1881
- ISSN
- 1093-4715 (ISSN-L)
- 1093-9946
- DOI
- 10.2741/1667
- OpenAlex
- W1543746024
- Cited by
- 957
- References
- 180
- FWCI
- 11.52
- Type
- journal article
- Language
- en
- Open access
- bronze
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.