Activation of p53 by Oxidative Stress Involves Platelet-derived Growth Factor-β Receptor-mediated Ataxia Telangiectasia Mutated (ATM) Kinase Activation
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Phosphorylation of the p53 tumor suppressor protein is a critical event in the up-regulation and activation of p53 during cellular stress. In this study, we characterized the signaling pathway linking oxidative stress to p53 through the platelet-derived growth factor beta (PDGF beta) receptor and the ataxia telangiectasia mutated (ATM) kinase. In response to H2O2, we observed phosphorylation of p53 specifically at serine 15, but not serine 9, 20, or 392. Phosphorylation of Ser-15 was correlated with enhanced induction and functional activation of p53 manifest as transcription of the p53 target p21CIP/WAF. We found that H2O2 induced phosphorylation of the PDGF beta receptor and increased ATM kinase activity, two events integral to p53 activation as either AG1433 (a PDGF beta receptor inhibitor) or caffeine (an ATM kinase inhibitor) inhibited Ser-15 phosphorylation. Similarly, p53 activation by H2O2 was inhibited by kinase-inactive forms of the PDGF beta receptor or ATM. Inhibition of ATM kinase had no effect on H2O2-induced PDGF beta receptor tyrosine phosphorylation, whereas PDGF beta receptor suppression with RNA interference impaired H2O2-induced ATM activation, indicating that ATM lies downstream to the PDGF beta receptor in this signaling cascade. Functionally, inhibition of the PDGF beta receptor abrogated the inhibition of cell proliferation, and promotion of apoptosis due to H2O2 treatment. Thus, these data link PDGF beta receptor transactivation to H2O2-induced p53 phosphorylation and suggest a functional role for growth factor receptors in modulation of p53 function.
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Hydrogen peroxide induces p53 phosphorylation at serine 15 and cell cycle arrest in an ATM-dependent manner in human umbilical vein endothelial cells.
“Hydrogen peroxide induces p53 phosphorylation at Serine 15 and cell cycle arrest in an ATM-dependent manner in human umbilical vein endothelial cells [70].”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [70]
Cites
p53, the cellular gatekeeper for growth and division
Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693 · see citing works
Oxidants, antioxidants, and the degenerative diseases of aging.
Ames, B. N., Shigenaga, M. K., & Hagen, T. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.7915 · Cited by 5,958 · see citing works
A Single Ataxia Telangiectasia Gene with a Product Similar to PI-3 Kinase
Savitsky, K., Bar-Shira, A., Gilad, S., Rotman, G., Ziv, Y., Vanagaite, L., Tagle, D. A., Smith, S., Uziel, T., Sfez, S., et al. (1995) · Science · doi:10.1126/science.7792600 · Cited by 2,785 · see citing works
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
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100 · see citing works
Activation of the ATM Kinase by Ionizing Radiation and Phosphorylation of p53
Canman, C. E., Lim, D.-S., Cimprich, K. A., Taya, Y., Tamai, K., Sakaguchi, K., Appella, E., Kastan, M. B., & Siliciano, J. D. (1998) · Science · doi:10.1126/science.281.5383.1677 · Cited by 2,042 · see citing works
Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951 · see citing works
Enhanced Phosphorylation of p53 by ATM in Response to DNA Damage
Banin, S., Moyal, L., Shieh, S.-Y., Taya, Y., Anderson, C. W., Chessa, L., Smorodinsky, N. I., Prives, C., Reiss, Y., Shiloh, Y., et al. (1998) · Science · doi:10.1126/science.281.5383.1674 · Cited by 1,797 · see citing works
The p66shc adaptor protein controls oxidative stress response and life span in mammals
Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712 · see citing works
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
A role for ATR in the DNA damage-induced phosphorylation of p53
Tibbetts, R. S., Brumbaugh, K. M., Williams, J. M., Sarkaria, J. N., Cliby, W. A., Shieh, S.-Y., Taya, Y., Prives, C., & Abraham, R. T. (1999) · Genes & Development · doi:10.1101/gad.13.2.152 · Cited by 1,046 · 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
Rosette, C., & Karin, M. (1996) · Science · doi:10.1126/science.274.5290.1194 · Cited by 1,034 · see citing works
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
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945 · see citing works
Regulation and function of the p53 tumor suppressor protein
Ryan, K. M., Phillips, A. C., & Vousden, K. H. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00216-7 · Cited by 721 · see citing works
Selective induction of E2F1 in response to DNA damage, mediated by ATM-dependent phosphorylation.
Lin, W.-C., Lin, F., & Nevins, J. R. (2001) · PubMed Central · Cited by 440 · see citing works
Natural Antioxidants in Human Health and Disease
(1994) · Elsevier eBooks · doi:10.1016/c2009-0-03361-3 · Cited by 427 · see citing works
A p53 Amino-Terminal Nuclear Export Signal Inhibited by DNA Damage-Induced Phosphorylation
Zhang, Y., & Xiong, Y. (2001) · Science · doi:10.1126/science.1058637 · Cited by 378 · see citing works
Rotman, G. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.10.1555 · Cited by 322 · see citing works
Linseman, D. A., Benjamin, C. W., & Jones, D. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12563 · Cited by 290 · see citing works
Hammond, E. M., Dorie, M. J., & Giaccia, A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212360200 · Cited by 282 · see citing works
Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
Lambeth, J. D. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200201000-00003 · Cited by 282 · 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
Loss of the ataxia–telangiectasia gene product causes oxidative damage in target organs
Barlow, C., Dennery, P. A., Shigenaga, M. K., Smith, M. A., Morrow, J. D., Roberts, L. J., Wynshaw-Boris, A. J., & Levine, R. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9915 · Cited by 246 · see citing works
The Inactivation Mechanism of Low Molecular Weight Phosphotyrosine-protein Phosphatase by H2O2
Caselli, A., Marzocchini, R., Camici, G., Manao, G., Moneti, G., Pieraccini, G., & Ramponi, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.49.32554 · Cited by 213 · see citing works
Hall-Jackson, C. A., Cross, D. A. E., MORRICE, N. A., & Smythe, C. (1999) · Oncogene · doi:10.1038/sj.onc.1203077 · Cited by 213 · see citing works
Chen, K., Vita, J. A., Berk, B. C., & Keaney, J. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011766200 · Cited by 200 · see citing works
Self-citationMin, D. S., Kim, E., & Exton, J. H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29986 · Cited by 174 · see citing works
Heeneman, S., Haendeler, J., Saito, Y., Ishida, M., & Berk, B. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909616199 · Cited by 162 · see citing works
Reactive Oxygen Species Activate p90 Ribosomal S6 Kinase via Fyn and Ras
Abe, J., Okuda, M., Huang, Q., Yoshizumi, M., & Berk, B. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.3.1739 · Cited by 141 · see citing works
Turenne, G. A., Paul, P., Laflair, L., & Price, B. D. (2001) · Oncogene · doi:10.1038/sj.onc.1204665 · Cited by 120 · see citing works
González-Rubio, M., Voit, S., Rodrı́guez-Puyol, D., Weber, M. F. A., & Marx, M. (1996) · Kidney International · doi:10.1038/ki.1996.299 · Cited by 87 · see citing works
Requirement of ATM in UVA-induced Signaling and Apoptosis
Zhang, Y., Ma, W., Kaji, A., Bode, A. M., & Dong, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110245200 · Cited by 87 · see citing works
Chen, K., Inoue, M., & Okada, A. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1087 · Cited by 86 · see citing works
Self-citationMechanism of thiamine uptake by human jejunal brush-border membrane vesicles
Dudeja, P. K., Tyagi, S., Kavilaveettil, R. J., Gill, R. K., & Said, H. M. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.3.c786 · Cited by 79 · see citing works
DNA-dependent Protein Kinase-independent Activation of p53 in Response to DNA Damage
Burma, S., Kurimasa, A., Xie, G., Taya, Y., Araki, R., Abe, M., Crissman, H. A., Ouyang, H., Li, G. C., & Chen, D. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.17139 · Cited by 73 · see citing works
Marston, N., Crook, T., & Vousden, K. H. (1994) · PubMed · Cited by 70 · see citing works
Ward, A. J., Olive, P. L., Burr, A., & Rosin, M. P. (1994) · Environmental and Molecular Mutagenesis · doi:10.1002/em.2850240205 · Cited by 60 · see citing works
Serine phosphorylation in the NH2 terminus of p53 facilitates transactivation.
Mayr, G. A., Reed, M. J., Wang, P., Wang, Y., Schweds, J. F., & Tegtmeyer, P. (1995) · PubMed · Cited by 53 · see citing works
Vile, G. F. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00748-5 · Cited by 49 · see citing works
Wang, R. J., Ananthaswamy, H. N., Nixon, B. T., Hartman, P. S., & Eisenstark, A. (1980) · Radiation Research · doi:10.2307/3575378 · Cited by 34 · see citing works
Hypersensitivity of ataxia-telangiectasia fibroblasts to a nitric oxide donor
Green, M. H. L., Marcovitch, A. J., Harcourt, S. A., Lowe, J. E., Green, I. C., & Arlett, C. F. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00336-x · Cited by 26 · see citing works
Vuillaume, M., Best‐Belpomme, M., Lafont, R., Hubert, M., Decroix, Y., & Sarasin, A. R. (1989) · Carcinogenesis · doi:10.1093/carcin/10.8.1375 · Cited by 10 · see citing works
Flagged first, then by citations
1 of the 45 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
TIGAR, a p53-Inducible Regulator of Glycolysis and Apoptosis
Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C., Nakano, K., Bartrons, R., Gottlieb, E., & Vousden, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.05.036 · Cited by 2,019 · 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
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438 · see citing works
ATM Activation by Oxidative Stress
Guo, Z., Kozlov, S., Lavin, M. F., Person, M. D., & Paull, T. T. (2010) · Science · doi:10.1126/science.1192912 · Cited by 1,079 · see citing works
Hydrogen peroxide sensing, signaling and regulation of transcription factors
Marinho, H. S., Real, C., Cyrne, L., Soares, H., & Antunes, F. (2014) · Redox Biology · doi:10.1016/j.redox.2014.02.006 · Cited by 851 · see citing works
DNA damage responses to oxidative stress
Barzilai, A., & Yamamoto, K.-I. (2004) · DNA Repair · doi:10.1016/j.dnarep.2004.03.002 · Cited by 796 · see citing works
Suzuki, S., Tanaka, T., Poyurovsky, M. V., Nagano, H., Mayama, T., Ohkubo, S., Lokshin, M., Hosokawa, H., Nakayama, T., Suzuki, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002459107 · Cited by 705 · see citing works
DNA damage-induced activation of ATM and ATM-dependent signaling pathways
Kurz, E. U., & Lees‐Miller, S. P. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.03.029 · Cited by 478 · see citing works
Regulation of ROS signal transduction by NADPH oxidase 4 localization
Chen, K., Kirber, M. T., Xiao, H. Q., Yang, Y., & Keaney, J. F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200709049 · Cited by 468 · see citing works
Self-citationChen, J., & Russo, J. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.06.004 · Cited by 330 · see citing works
Radiation-induced cell signaling: inside-out and outside-in
Valerie, K. C., Yacoub, A., Hagan, M. P., Curiel, D. T., Fisher, P. B., Grant, S., & Dent, P. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0596 · Cited by 329 · see citing works
Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
Yang, Y., Ludwig, R. L., Jensen, J. P., Pierre, S. A., Medaglia, M. V., Davydov, I. V., Safiran, Y. J., Oberoi, P., Kenten, J. H., Phillips, A. C., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.04.029 · Cited by 321 · see citing works
Tumor suppressor genes and ROS: complex networks of interactions
Vurusaner, B., Poli, G., & Başağa, H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.035 · Cited by 292 · see citing works
Yan, S., Sorrell, M., & Berman, Z. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1666-4 · Cited by 247 · see citing works
Suraweera, A., Bécherel, O. J., Chen, P., Rundle, N. T., Woods, R. G., Nakamura, J., Gatei, M. H., Criscuolo, C., Filla, A., Chessa, L., et al. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200701042 · Cited by 196 · see citing works
Hagenbuchner, J., Kuznetsov, A. V., Obexer, P., & Ausserlechner, M. J. (2012) · Oncogene · doi:10.1038/onc.2012.500 · Cited by 175 · see citing works
Metabolic changes in cancer: beyond the Warburg effect
Wu, W., & Zhao, S. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gms104 · Cited by 173 · see citing works
Reactive Oxygen Species Induced p53 Activation: DNA Damage, Redox Signaling, or Both?
Shi, T., & Dansen, T. B. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8074 · Cited by 164 · see citing works
The neurological phenotype of ataxia-telangiectasia: Solving a persistent puzzle
Biton, S., Barzilai, A., & Shiloh, Y. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.03.006 · Cited by 133 · see citing works
Regulation of the protein disulfide proteome by mitochondria in mammalian cells
Yang, Y., Song, Y., & Loscalzo, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702027104 · Cited by 129 · see citing works
Iron Deprivation in Cancer––Potential Therapeutic Implications
Heath, J. L., Weiss, J. M., Lavau, C., & Wechsler, D. S. (2013) · Nutrients · doi:10.3390/nu5082836 · Cited by 121 · see citing works
Chen, K., Thomas, S. R., Albano, A., Murphy, M. P., & Keaney, J. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404859200 · Cited by 116 · see citing works
Self-citationDeletion of the PDGFR-β Gene Affects Key Fibroblast Functions Important for Wound Healing
Gao, Z., Sasaoka, T., Fujimori, T., Oya, T., Ishii, Y., Sabit, H., Kawaguchi, M., Kurotaki, Y., Naito, M., Wada, T., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m413081200 · Cited by 111 · see citing works
Caveolin-1, cellular senescence and age-related diseases
Zou, H., Stoppani, E., Volonte, D., & Galbiati, F. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.11.001 · Cited by 112 · see citing works
Ismail, I. H., Nyström, S., Nygren, J., & Hammarsten, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411588200 · Cited by 103 · see citing works
Osteolineage niche cells initiate hematopoietic stem cell mobilization
Mayack, S. R., & Wagers, A. J. (2008) · Blood · doi:10.1182/blood-2008-01-133710 · Cited by 101 · see citing works
RetractedMammalian Antioxidant Defenses Are Not Inducible by H2O2
Desaint, S., Luriau, S., Aude, J.-C., Rousselet, G., & Tolédano, M. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401888200 · Cited by 96 · see citing works
Mai, W., Yan, J.-L., Wang, L., Zheng, Y., Xin, Y., & Wang, W.-N. (2010) · Aquatic Toxicology · doi:10.1016/j.aquatox.2010.07.025 · Cited by 95 · see citing works
Reactive Oxygen Species–Mediated Signal Transduction in the Endothelium
Chen, K., & Keaney, J. F. (2004) · Endothelium · doi:10.1080/10623320490482655 · Cited by 91 · see citing works
Self-citationEarly Single Cell Bifurcation of Pro- and Antiapoptotic States during Oxidative Stress
Nair, V. D., Yuen, T., Olanow, C. W., & Sealfon, S. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312135200 · Cited by 90 · see citing works
Hagemeier, S. R., Barlow, E. A., Meng, Q., & Kenney, S. C. (2012) · Journal of Virology · doi:10.1128/jvi.01850-12 · Cited by 82 · see citing works
Mouse brains deficient in neuronal PDGF receptor‐β develop normally but are vulnerable to injury
Ishii, Y., Oya, T., Zheng, L., Gao, Z., Kawaguchi, M., Sabit, H., Matsushima, T., Tokunaga, A., Ishizawa, S., Hori, E., et al. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03922.x · Cited by 82 · see citing works
Activation of p53 signaling initiates apoptotic death in a cellular model of Parkinson’s disease
Nair, V. D. (2006) · APOPTOSIS · doi:10.1007/s10495-006-6316-3 · Cited by 80 · see citing works
Huang, A., Zhang, Y., Chen, K., Hatakeyama, K., & Keaney, J. F. (2004) · Circulation Research · doi:10.1161/01.res.0000153669.24827.df · Cited by 79 · see citing works
Self-citationAnter, E., Chen, K., Shapira, O. M., Karas, R. H., & Keaney, J. F. (2005) · Circulation Research · doi:10.1161/01.res.0000168807.63013.56 · Cited by 78 · see citing works
Self-citationPekovic, V., & Hutchison, C. J. (2008) · Journal of Anatomy · doi:10.1111/j.1469-7580.2008.00928.x · Cited by 75 · see citing works
Biton, S., Dar, I., Mittelman, L. A., Pereg, Y., Barzilai, A., & Shiloh, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601895200 · Cited by 74 · see citing works
Ifere, G. O., Barr, E., Equan, A., Gordon, K., Singh, U. P., Chaudhary, J., Igietseme, J. U., & Ananaba, G. A. (2009) · Cancer Detection and Prevention · doi:10.1016/j.cdp.2008.12.002 · Cited by 72 · see citing works
Kim, T.-S., Kawaguchi, M., Suzuki, M., Jung, C., Asai, K., Shibamoto, Y., Lavin, M. F., Khanna, K. K., & Miura, Y. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.004689 · Cited by 69 · see citing works
Volonté, D., Kahkonen, B., Shapiro, S. D., Di, Y. P., & Galbiati, F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c800225200 · Cited by 66 · see citing works
Kaushal, G. P., Liu, L., Kaushal, V., Hong, X., Melnyk, O. V., Seth, R., Safirstein, R. L., & Shah, S. V. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00391.2003 · Cited by 63 · see citing works
Hydrogen peroxide is a mediator of indole‐3‐acetic acid/horseradish peroxidase‐induced apoptosis
Kim, D.-S., Jeon, S., Jeong, Y., Kim, S.-Y., Kwon, S., & Park, K.-C. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.01.073 · Cited by 62 · see citing works
Ets-1 regulates energy metabolism in cancer cells
Verschoor, M. L., Wilson, L. A., Verschoor, C. P., & Singh, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013565 · Cited by 59 · see citing works
The regulation of energy generating metabolic pathways by p53
Corcoran, C. A., Huang, Y., & Sheikh, M. S. (2006) · Cancer Biology & Therapy · doi:10.4161/cbt.5.12.3617 · Cited by 57 · see citing works
Verschoor, M. L., Wilson, A., & Singh, G. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y09-135 · Cited by 57 · see citing works
Gugliesi, F., Mondini, M., Ravera, R., Robotti, A., Andrea, M. D., Gribaudo, G., Gariglio, M., & Landolfo, S. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0904507 · Cited by 56 · see citing works
Zhang, F., Ni, C., Kong, D., Zhang, X., Zhu, X., Chen, L., Lu, Y., & Zheng, S. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.09.016 · Cited by 53 · see citing works
Nuntharatanapong, N., Chen, K., Sinhaseni, P., & Keaney, J. F. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00901.2004 · Cited by 49 · see citing works
Self-citationFeedback Control of p53 Translation by REDD1 and mTORC1 Limits the p53-Dependent DNA Damage Response
Vadysirisack, D. D., Baenke, F., Ory, B., Lei, K., & Ellisen, L. W. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05541-11 · Cited by 48 · see citing works
Gurjala, A. N., Liu, W. R., Mogford, J. E., Procaccini, P. S. A., & Mustoe, T. A. (2005) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2005.00079.x · Cited by 42 · see citing works
Gu, C., Zhang, Y., Hu, Q., Wu, J., Ren, H., Liu, C., & Wang, G. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.250 · Cited by 39 · see citing works
Shimasaki, Y., Pan, N., Messina, L. M., Li, C., Chen, K., Liu, L., Cooper, M. P., Vita, J. A., & Keaney, J. F. (2013) · Circulation Research · doi:10.1161/circresaha.113.301319 · Cited by 38 · see citing works
Self-citationGene Expression in the Lung of p53 Mutant Mice Exposed to Cigarette Smoke
Izzotti, A., Cartiglia, C., Longobardi, M., Bagnasco, M., Merello, A., You, M., Lubet, R. A., & Flora, S. D. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1420 · Cited by 37 · see citing works
Unfolded protein response is activated in aged retinas
Lenox, A. R., Bhootada, Y., Gorbatyuk, O. S., Fullard, R. J., & Gorbatyuk, M. S. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.10.019 · Cited by 34 · see citing works
Ke, X., McKnight, R. A., Wang, Z.-M., Yu, X., Wang, L., Callaway, C. W., Albertine, K. H., & Lane, R. H. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00701.2004 · Cited by 34 · see citing works
High glucose induces mitochondrial p53 phosphorylation by p38 MAPK in pancreatic RINm5F cells
Flores-López, L. A., Díaz-Flores, M., García-Macedo, R., Ávalos‐Rodríguez, A., Vergara-Onofre, M., Cruz, M., Contreras‐Ramos, A., Königsberg, M., & Ortega‐Camarillo, C. (2013) · Molecular Biology Reports · doi:10.1007/s11033-013-2595-2 · Cited by 33 · see citing works
Wei, Z., Guo, H., Liu, Z., Zhang, X., Liu, Q., Qian, Y., Gong, Y., & Shao, C. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.010 · Cited by 30 · see citing works
PDGF: the nuts and bolts of signalling toolbox
Farooqı, A. A., Waseem, S., Riaz, A. M., Dilawar, B. A., Mukhtar, S., Minhaj, S., Waseem, M. S., Daniel, S., Malik, B. A., Nawaz, A., et al. (2011) · Tumor Biology · doi:10.1007/s13277-011-0212-3 · Cited by 31 · see citing works
Cho, J. J., Cho, C.-L., Kao, C., Chen, C., Tseng, C., Lee, Y., Liao, L., & Hong, Y. (2012) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-12-265 · Cited by 30 · see citing works
Xia, M., Wang, M., Tashiro, S., Onodera, S., Minami, M., & Ikejima, T. (2005) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.28.226 · Cited by 29 · see citing works
BCR/ABL Recruits p53 Tumor Suppressor Protein to Induce Drug Resistance
Stokłosa, T., Słupianek, A., Datta, M., Nieborowska-Skorska, M., Nowicki, M. O., Koptyra, M., & Skórski, T. (2004) · Cell Cycle · doi:10.4161/cc.3.11.1229 · Cited by 29 · see citing works
Hypoxamirs and Mitochondrial Metabolism
Cottrill, K. A., Chan, S. Y., & Loscalzo, J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5641 · Cited by 26 · see citing works
Ascochlorin activates p53 in a manner distinct from DNA damaging agents
Jeong, J.-H., Nakajima, H., Magae, J., Furukawa, C., Taki, K., Otsuka, K., Tomita, M., Lee, I., Kim, C., Chang, H., et al. (2009) · International Journal of Cancer · doi:10.1002/ijc.24259 · Cited by 25 · see citing works
Oxidation of methionine residue at hydrophobic core destabilizes p53 tetrameric structure
Nomura, T., Kamada, R., Ito, I., Chuman, Y., Shimohigashi, Y., & Sakaguchi, K. (2008) · Biopolymers · doi:10.1002/bip.21084 · Cited by 24 · see citing works
Moradi, M.-N., Karimi, J., Khodadadi, I., Amiri, I., Karami, M., Saidijam, M., Vatannejad, A., & Tavilani, H. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.12.038 · Cited by 24 · see citing works
Oxidative stress enhances phosphorylation of p53 in neonatal rat cardiomyocytes
Long, X., Goldenthal, M. J., & Marı́n-Garcı́a, J. (2007) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-007-9470-1 · Cited by 24 · see citing works
Chen, J., & Ozanne, S. E. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.11.023 · Cited by 24 · see citing works
Recombinant Plasminogen Activator Inhibitor-1 Inhibits Intimal Hyperplasia
Wu, J., Peng, L., McMahon, G. A., Lawrence, D. A., & Fay, W. P. (2009) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.109.189514 · Cited by 23 · see citing works
Redox control of enzymatic functions: The electronics of life's circuitry
Bonini, M. G., Consolaro, M. E. L., Hart, P. C., Mao, M., de Abreu, A. L. P., & Master, А. M. (2014) · IUBMB Life · doi:10.1002/iub.1258 · Cited by 21 · see citing works
Excess Manganese-Induced Apoptosis in Chicken Cerebrums and Embryonic Neurocytes
Zhang, K., Zhu, Y., Wang, X., Zhao, X., Li, S., & Teng, X. (2017) · Biological Trace Element Research · doi:10.1007/s12011-017-0992-4 · Cited by 21 · see citing works
Multiparametric cerebellar imaging and clinical phenotype in childhood ataxia telangiectasia
Dineen, R. A., Raschke, F., McGlashan, H. L., Pszczółkowski, S., Hack, L., Cooper, A. D., Prasad, M., Chow, G., Whitehouse, W. P., & Auer, D. P. (2019) · NeuroImage Clinical · doi:10.1016/j.nicl.2019.102110 · Cited by 20 · see citing works
A278C mutation of dihydropteridine reductase decreases autophagy via mTOR signaling
Si, Q., Sun, S., & Gu, Y. (2017) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmx061 · Cited by 15 · see citing works
Ifere, G. O., Equan, A., Gordon, K., Nagappan, P., Igietseme, J. U., & Ananaba, G. A. (2010) · Cancer Epidemiology · doi:10.1016/j.canep.2010.04.009 · Cited by 14 · see citing works
Zakareia, F. A., AL-Ayadhi, L. Y., & Al-Drees, A. A. (2012) · Neurosciences · doi:10.17712/1658-3183.1949 · Cited by 12 · see citing works
Coenzyme Q2 induced p53-dependent apoptosis
Esaka, Y. H., Nagahara, Y., Hasome, Y., Nishio, R., & Ikekita, M. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.04.013 · Cited by 11 · see citing works
Genetic depletion of p53 attenuates cocaine-induced hepatotoxicity in mice
Nhu, H., Sharma, G., Sharma, N., Shin, E., Kim, D.-J., Pham, D. T., Trinh, Q. D., Jang, C., Nah, S. Y., Jeong, J. H., et al. (2018) · Biochimie · doi:10.1016/j.biochi.2018.12.009 · Cited by 10 · see citing works
Yu, C., Kim, B., Park, M., Do, Y., Kong, Y., & Kim, E. (2018) · Cell Communication and Signaling · doi:10.1186/s12964-018-0265-7 · Cited by 8 · see citing works
Flores-López, L. A., Enríquez‐Flores, S., Mora, I. D. L. M. L., García‐Torres, I., López‐Velázquez, G., Viedma‐Rodríguez, R., Ávalos‐Rodríguez, A., Contreras‐Ramos, A., & Ortega‐Camarillo, C. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13317 · Cited by 7 · see citing works
Glutamine and leukemia research: progress and clinical prospects
Wang, Z., Liu, M., & Yang, Q. (2024) · Discover Oncology · doi:10.1007/s12672-024-01245-0 · Cited by 6 · see citing works
Gambardella, G., Peluso, I., Montefusco, S., Bansal, M., Medina, D. L., Lawrence, N. D., & di Bernardo, D. (2015) · BMC Bioinformatics · doi:10.1186/s12859-015-0700-3 · Cited by 6 · see citing works
Nomura, T., Kamada, R., Ito, I., Sakamoto, K., Chuman, Y., Ishimori, K., Shimohigashi, Y., & Sakaguchi, K. (2011) · Biopolymers · doi:10.1002/bip.21594 · Cited by 4 · see citing works
Wen, C., Geervliet, M., de Vries, H., Fabà, L., den Hil, P. J. R.-V., Skovgaard, K., Savelkoul, H. F. J., Schols, H. A., Wells, J. M., Tijhaar, E. J., et al. (2023) · Animal Microbiome · doi:10.1186/s42523-023-00244-w · Cited by 3 · see citing works
Disproportionate Expression of ATM in Cerebellar Cortex During Human Neurodevelopment
Deacon, S., Dalleywater, W. J., Peat, C., Paine, S., & Dineen, R. A. (2023) · The Cerebellum · doi:10.1007/s12311-023-01560-2 · Cited by 2 · see citing works
Takahashi, K., Oyama, K., Motoshige, H., & Sakurai, K. (2010) · Journal of Biophysical Chemistry · doi:10.4236/jbpc.2010.13019 · Cited by 1 · see citing works
Marı́n-Garcı́a, J. (2010) · Humana Press eBooks · doi:10.1007/978-1-60761-147-9_7 · Cited by 1 · see citing works
P53 AND REACTIVE OXYGEN SPECIES: A CONVOLUTED STORY
Liu, B. (2007) · UKnowledge (University of Kentucky) · Cited by 1 · see citing works
Choi, A. M. K., & Wang, X. (2006) · Elsevier eBooks · doi:10.1016/b0-12-370879-6/00030-2 · Cited by 1 · see citing works
DNA Damage and Oxidative Stress Induced-p53 Activity In Astrocytes causes Growth Arrest
Humphrey, S. A. (2012) · Scholarship@Western (Western University)
Mecanismes de toxicitat de la dopamina en cèl·lules de neuroblastoma humà SH-SY5Y
Xavier, P. G. (2008) · Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona)
Kaushal, G. P., Liu, L., Kaushal, V., Hong, X., Melnyk, O. V., Seth, R., Safirstein, R. L., & Shah, S. V. (2004)
Wen, C., Geervliet, M., de Vries, H., Fabà, L., den Hil, P. J. R.-V., Skovgaard, K., Savelkoul, H. F. J., Schols, H. A., Wells, J. M., Tijhaar, E. J., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26581682
- Authors
- Chen, K., Albano, A., Ho, A., & Keaney, J. F.
- Affiliations
- Boston University (US)
- Corresponding author
- Keaney, John F.
- ORCID
- Keaney, John F.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-10
- Volume
- 278
- Issue
- 41
- Pages
- 39527-39533
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2026254485
- Cited by
- 95
- References
- 45
- Citations by year
- 2024: 3 · 2023: 2 · 2020: 1 · 2019: 1 · 2018: 3 · 2017: 3 · 2015: 3 · 2014: 4 · 2013: 6 · 2012: 8
- FWCI
- 4.48
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk055656-03)
- National Heart, Lung, and Blood Institute (P01HL060886, HL-60886)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-55656)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- p53 activation, oxidative stress, hydrogen peroxide, PDGF receptor beta, ATM kinase, p53 Ser15 phosphorylation, p21, apoptosis, cell proliferation, signaling pathways
- MeSH terms
- Animals, Base Sequence, Binding Sites, Cells, Cultured, DNA, DNA-Binding Proteins, Enzyme Activation, Humans, Hydrogen Peroxide, Phosphorylation, Signal Transduction, Transcriptional Activation, Tumor Suppressor Protein p53, 3T3 Cells, Protein Serine-Threonine Kinases, Oxidative Stress, Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Receptor, Platelet-Derived Growth Factor beta, Mitogen-Activated Protein Kinases, Tumor Suppressor Proteins, RNA Interference, p38 Mitogen-Activated Protein Kinases, Mice, Ataxia Telangiectasia Mutated Proteins
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