Cited by 524Cancer-related Molecular PathwaysCell death mechanisms and regulationPI3K/AKT/mTOR signaling in cancer

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Coping with stress: multiple ways to activate p53

Horn, H F, Vousden, K H·2007·Oncogene

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Abstract

Over the years, p53 has been shown to sit at the centre of an increasingly complex web of incoming stress signals and outgoing effector pathways. The number and diversity of stress signals that lead to p53 activation illustrates the breadth of p53's remit - responding to a wide variety of potentially oncogenic insults to prevent tumour development. Interestingly, different stress signals can use different and independent pathways to activate p53, and there is some evidence that different stress signals can mediate different responses. How each of the responses to p53 contributes to inhibition of malignant progression is beginning to be clarified, with the hope that identification of responses that are key to tumour suppression will allow a more focused and effective search for new therapeutic targets. In this review, we will highlight some recently identified roles for p53 in tumour suppression, and discuss some of the numerous mechanisms through which p53 can be regulated and activated.

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Damage-mediated Phosphorylation of Human p53 Threonine 18 through a Cascade Mediated by a Casein 1-like Kinase
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Tumour incidence, spectrum and ploidy in mice with a large deletion in the p53 gene.
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p300/CBP/p53 interaction and regulation of the p53 response
Grossman, S. R. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02226.x · Cited by 275
Mutual Dependence of MDM2 and MDMX in Their Functional Inactivation of p53
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Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells in vivo
Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260
The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation
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Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.
Meulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F. A. S., Ovaa, H., Abraham, T. E., Dirks, R. W., & Jochemsen, A. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.024 · Cited by 260
E4F1 Is an Atypical Ubiquitin Ligase that Modulates p53 Effector Functions Independently of Degradation
Cam, L. L., Linares, L. K., Paul, C., Julien, E., Lacroix, M., Hatchi, E., Triboulet, R., Bossis, G., Shmueli, A., Rodríguez, M. S., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.031 · Cited by 251
Genetic Inactivation of the Transcription Factor TIF-IA Leads to Nucleolar Disruption, Cell Cycle Arrest, and p53-Mediated Apoptosis
Yuan, X., Zhou, Y., Casanova, E., Chai, M., Kiss, É., Gröne, H., Schütz, G., & Grummt, I. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.05.023 · Cited by 250
Essential role of ribosomal protein L11 in mediating growth inhibition‐induced p53 activation
Bhat, K., Itahana, K., Jin, A., & Zhang, Y. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600247 · Cited by 249
MDM2 promotes ubiquitination and degradation of MDMX
Pan, Y., & Chen, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5113-5121.2003 · Cited by 246 · cited 14×
“…(Sharp et al., 1999; Tanimura et al., 1999), which results in the stabilization of Mdm2 (Stad et al., 2001; Gu et al., 2002) or the Mdm2-mediated degradation of MdmX (de Graaf et al., 2003; Kawai et al., 2003; Pan and Chen, 2003), depending on the relative expression levels of the two proteins.”
BackgroundInfluential
p53 Stabilization and Transactivation by a von Hippel-Lindau Protein
Roe, J., Kim, H., Lee, S.-M., Kim, S.-T., Cho, E., & Youn, H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.04.006 · Cited by 245
Critical role for Daxx in regulating Mdm2
Tang, J., Qu, L., Zhang, J., Wang, W., Michaelson, J. S., Degenhardt, Y., El‐Deiry, W. S., & Yang, X. (2006) · Nature Cell Biology · doi:10.1038/ncb1442 · Cited by 242
p53 in recombination and repair
Gatz, S. A., & Wiesmüller, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401903 · Cited by 242
p53 and Nur77/TR3 – transcription factors that directly target mitochondria for cell death induction
Moll, U. M., Marchenko, N. D., & Zhang, X.-K. (2006) · Oncogene · doi:10.1038/sj.onc.1209601 · Cited by 241
Identification of ALDH4 as a p53-inducible gene and its protective role in cellular stresses
Yoon, K., Nakamura, Y., & Arakawa, H. (2004) · Journal of Human Genetics · doi:10.1007/s10038-003-0122-3 · Cited by 240
C-Terminal Ubiquitination of p53 Contributes to Nuclear Export
Lohrum, M. A. E., Woods, D. B., Ludwig, R. L., Bálint, É., & Vousden, K. H. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8521-8532.2001 · Cited by 237
Self-citation
Polymorphisms in the p53 pathway
Pietsch, E. C., Humbey, O., & Murphy, M. E. (2006) · Oncogene · doi:10.1038/sj.onc.1209367 · Cited by 236
MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin
Hu, B., Gilkes, D. M., Farooqi, B., Sebti, S. M., & Chen, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600147200 · Cited by 236
Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms
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The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation and degradation of p53
Higashitsuji, H., Higashitsuji, H., Itoh, K., Sakurai, T., Nagao, T., Sumitomo, H., Masuda, T., Dawson, S. P., Shimada, Y., Mayer, R. J., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.06.006 · Cited by 229
The role of p53 in hypoxia-induced apoptosis
Hammond, E. M., & Giaccia, A. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.154 · Cited by 213
MdmX Protects p53 from Mdm2-Mediated Degradation
Jackson, M. W., & Berberich, S. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1001-1007.2000 · Cited by 211 · cited 1×
“However, MdmX does not show E3 activity (Jackson and Berberich, 2000; Stad et al., 2001) and functions predominantly by directly inhibiting p53’s transcriptional activity (Shvarts et al., 1996; Francoz et al., 2006).”
Background
MDM2 Promotes Cell Motility and Invasiveness by Regulating E-Cadherin Degradation
Yang, J.-Y., Zong, C. S., Xia, W., Wei, Y., Ali-Seyed, M., Li, Z., Broglio, K., Berry, D. A., & Hung, M.-C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00172-06 · Cited by 211
Tumor suppression and normal aging in mice with constitutively high p53 activity
Mendrysa, S. M., O'Leary, K. A., McElwee, M. K., Michalowski, J., Eisenman, R. N., Powell, D. A., & Perry, M. E. (2006) · Genes & Development · doi:10.1101/gad.1378506 · Cited by 210
YY1 inhibits the activation of the p53 tumor suppressor in response to genotoxic stress
Gronroos, E. C., Terentiev, A. A., Punga, T., & Ericsson, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402283101 · Cited by 209
FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity
Abida, W. M., Nikolaev, A. Y., Zhao, W., Zhang, W., & Gu, W. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609001200 · Cited by 207
Degradation of the Tumor Suppressor Smad4 by WW and HECT Domain Ubiquitin Ligases
Morén, A., Imamura, T., Miyazono, K., Heldin, C., & Moustakas, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414027200 · Cited by 200
Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53
Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z. A., Brownell, J. E., Liu, L. F., Lutzker, S. G., Saleem, A., & Rubin, E. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400300200 · Cited by 192
HAUSP is Required for p53 Destabilization
Cummins, J. M., & Vogelstein, B. (2004) · Cell Cycle · doi:10.4161/cc.3.6.924 · Cited by 190
Complicating the complexity of p53
Yee, K. S. Y., & Vousden, K. H. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi122 · Cited by 190
Self-citation
Mdmx as an essential regulator of p53 activity
Marine, J., & Jochemsen, A. G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.151 · Cited by 189
Levels of HdmX expression dictate the sensitivity of normal and transformed cells to Nutlin-3
Patton, J. T., Mayo, L. D., Singhi, A. D., Gudkov, A. V., Stark, G. R., & Jackson, M. W. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3832 · Cited by 189
ATM-Mediated Phosphorylations Inhibit Mdmx/Mdm2 Stabilization by HAUSP in Favor of p53 Activation
Meulmeester, E., Pereg, Y., Shiloh, Y., & Jochemsen, A. G. (2005) · Cell Cycle · doi:10.4161/cc.4.9.1981 · Cited by 173
DNA damage-induced MDMX degradation is mediated by MDM2
Kawai, H., Wiederschain, D., Kitao, H., Stuart, J., Tsai, K. K. C., & Yuan, Z.-M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308295200 · Cited by 163 · cited 14×
“…(Sharp et al., 1999; Tanimura et al., 1999), which results in the stabilization of Mdm2 (Stad et al., 2001; Gu et al., 2002) or the Mdm2-mediated degradation of MdmX (de Graaf et al., 2003; Kawai et al., 2003; Pan and Chen, 2003), depending on the relative expression levels of the two proteins.”
BackgroundInfluential
Hdmx modulates the outcome of p53 activation in human tumor cells
Wade, M., Wong, E. T., Tang, M., Stommel, J. M., & Wahl, G. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605405200 · Cited by 163
Synergistic roles of Mdm2 and Mdm4 for p53 inhibition in central nervous system development
Xiong, S., Van Pelt, C. S., Elizondo-Fraire, A. C., Liu, G., & Lozano, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508500103 · Cited by 155
Human Kruppel-like Factor 5 Is a Target of the E3 Ubiquitin Ligase WWP1 for Proteolysis in Epithelial Cells
Chen, C., Sun, X., Guo, P., Dong, X., Sethi, P., Cheng, X., Zhou, J., Ling, J., Simons, J. W., Lingrel, J. B., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506183200 · Cited by 155
Sequence‐specific DNA binding by p53: identification of target sites and lack of binding to p53 ‐ MDM2 complexes.
Zauberman, A., Barak, Y., Ragimov, N., Levy, N., & Oren, M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05941.x · Cited by 151
DAP-kinase induces apoptosis by suppressing integrin activity and disrupting matrix survival signals
Wang, W., Kuo, J., Yao, C. J., & Chen, R. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200204050 · Cited by 150
Cancer-Associated Mutations in the MDM2 Zinc Finger Domain Disrupt Ribosomal Protein Interaction and Attenuate MDM2-Induced p53 Degradation
Lindström, M. S., Jin, A., Deisenroth, C., Wolf, G. W., & Zhang, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01307-06 · Cited by 149
ATM Engages Autodegradation of the E3 Ubiquitin Ligase COP1 After DNA Damage
Dornan, D., Shimizu, H., Mah, A. S., Dudhela, T., Eby, M. T., O’Rourke, K. M., Seshagiri, S., & Dixit, V. M. (2006) · Science · doi:10.1126/science.1127335 · Cited by 145
Hdmx protein stability is regulated by the ubiquitin ligase activity of Mdm2
de Graaf, P., Little, N. A., Ramos, Y. F. M., Meulmeester, E., Letteboer, S. J. F., & Jochemsen, A. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213034200 · Cited by 143 · cited 1×
“…(Sharp et al., 1999; Tanimura et al., 1999), which results in the stabilization of Mdm2 (Stad et al., 2001; Gu et al., 2002) or the Mdm2-mediated degradation of MdmX (de Graaf et al., 2003; Kawai et al., 2003; Pan and Chen, 2003), depending on the relative expression levels of the two proteins.”
Background
MDMX regulation of p53 response to ribosomal stress
Gilkes, D. M., Chen, L., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601424 · Cited by 142
Regulation of p53 localization and transcription by the HECT domain E3 ligase WWP1
Laine, A., & Ronai, Z. A. (2006) · Oncogene · doi:10.1038/sj.onc.1209924 · Cited by 133
Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth
McDonald, E. R., & El‐Deiry, W. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307459101 · Cited by 121
Mdm2 is involved in the ubiquitination and degradation of G‐protein‐coupled receptor kinase 2
Salcedo, A., Mayor, F., & Penela, P. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601351 · Cited by 119
Gankyrin Is an Ankyrin-repeat Oncoprotein That Interacts with CDK4 Kinase and the S6 ATPase of the 26 S Proteasome
Dawson, S. P., Apcher, S., Mee, M., Mayer, R. J., Higashitsuji, H., Baker, R. T., Uhle, S., Dubiel, W., & Fujita, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107313200 · Cited by 119
Loss of the ARF tumor suppressor reverses premature replicative arrest but not radiation hypersensitivity arising from disabled atm function.
Kamijo, T., van de Kamp, E. H., Chong, M. J., Zindy, F., Diehl, J. A., Sherr, C. J., & McKinnon, P. J. (1999) · PubMed · Cited by 117
p23, a simple protein with complex activities
Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116
Policing of oncogene activity by p53
Efeyan, A., García-Cao, I., Herranz, D., Velasco-Miguel, S., & Serrano, M. (2006) · Nature · doi:10.1038/443159a · Cited by 116
Savior and slayer: the two faces of p53
Bensaad, K., & Vousden, K. H. (2005) · Nature Medicine · doi:10.1038/nm1205-1278 · Cited by 113
Self-citation
SUMO-1 and p53
Melchior, F., & Hengst, L. (2002) · Cell Cycle · doi:10.4161/cc.1.4.131 · Cited by 109
MAGE-A4 Interacts with the Liver Oncoprotein Gankyrin and Suppresses Its Tumorigenic Activity
Nagao, T., Higashitsuji, H., Nonoguchi, K., Sakurai, T., Dawson, S. P., Mayer, R. J., Itoh, K., & Fujita, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206104200 · Cited by 108
Expression of SUMO-2/3 Induced Senescence through p53- and pRB-mediated Pathways
Li, T., Santockyte, R., Shen, R., Tekle, E., Wang, G., Yang, D. C. H., & Chock, P. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608236200 · Cited by 107
p53-Independent Activities of MDM2 and Their Relevance to Cancer Therapy
Zhang, Z., & Zhang, R. (2005) · Current Cancer Drug Targets · doi:10.2174/1568009053332618 · Cited by 104
Increased p53 activity does not accelerate telomere‐driven ageing
García‐Cao, I., García‐Cao, M., Tomás‐Loba, A., Martin‐Caballero, J., Flores, J. M., Klatt, P., Blasco, M. A., & Serrano, M. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400667 · Cited by 102 · cited 1×
“Increasing potential p53 activity, by adding an extra copy of p53 or reducing (but not eliminating) expression of Mdm2, resulted in apparently normal mice that were resistant to tumour development (Garcia-Cao et al., 2002, 2006; Mendrysa et al., 2006).”
Background
Regulation of p53 Localization and Activity by Ubc13
Laine, A. M., Topisirović, I., Zhai, D., Reed, J. C., Borden, K. L. B., & Ronai, Z. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01156-06 · Cited by 101
Identification of p53 Sequence Elements That Are Required for MDM2-Mediated Nuclear Export
Gu, J., Nie, L., Wiederschain, D., & Yuan, Z.-M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8533-8546.2001 · Cited by 100
NMR indicates that the small molecule RITA does not block p53-MDM2 binding in vitro
Krajewski, M., Ozdowy, P., D’Silva, L., Rothweiler, U., & Holak, T. A. (2005) · Nature Medicine · doi:10.1038/nm1105-1135 · Cited by 96
Unleashing the power of p53: lessons from mice and men: Figure 1.Preprint
Poyurovsky, M. V., & Prives, C. L. (2006) · Genes & Development · doi:10.1101/gad.1397506 · Cited by 96
Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing p53 function
Andrews, P., He, Y. J., & Xiong, Y. (2006) · Oncogene · doi:10.1038/sj.onc.1209490 · Cited by 95
Overexpression of p 28/ gankyrin in human hepatocellular carcinoma and its clinical significance
Fu, X. (2002) · World Journal of Gastroenterology · doi:10.3748/wjg.v8.i4.638 · Cited by 91
Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)
Megidish, T., Xu, J., & Xu, C. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200001200 · Cited by 89
Human PIRH2 Enhances Androgen Receptor Signaling through Inhibition of Histone Deacetylase 1 and Is Overexpressed in Prostate Cancer
Logan, I. R., Gaughan, L., McCracken, S. R., Sapountzi, V., Leung, H. Y., & Robson, C. N. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00147-06 · Cited by 88
CARPs Are Ubiquitin Ligases That Promote MDM2-independent p53 and Phospho-p53ser20 Degradation
Yang, W., Rozan, L. M., McDonald, E. R., Navaraj, A., Liu, J. J., Matthew, E. M., Wang, W., Dicker, D. T., & El‐Deiry, W. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610793200 · Cited by 88
The Oncoprotein Gankyrin Negatively Regulates Both p53 and RB by Enhancing Proteasomal Degradation
Higashitsuji, H., Liu, Y., Mayer, R. J., & Fujita, J. (2005) · Cell Cycle · doi:10.4161/cc.4.10.2107 · Cited by 82
WWP1-dependent ubiquitination and degradation of the lung Krüppel-like factor, KLF2
Zhang, X., Srinivasan, S. V., & Lingrel, J. B. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.02.033 · Cited by 78
Ubiquitin and Ubiquitin-Like Modifications of the p53 Family
Watson, I. R., & Irwin, M. S. (2006) · Neoplasia · doi:10.1593/neo.06439 · Cited by 77
p53 Proteasomal Degradation: Poly-Ubiquitination is Not the Whole Story
Asher, G., & Shaul, Y. (2005) · Cell Cycle · doi:10.4161/cc.4.8.1900 · Cited by 74
SUMO-specific protease SUSP4 positively regulates p53 by promoting Mdm2 self-ubiquitination
Lee, M. H., Lee, S. W., Lee, E. J., Choi, S. J., Chung, S. S., Lee, J. I., Cho, J. M., Seol, J. H., Baek, S. H., Kim, K. I., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1512 · Cited by 70
E6AP Mediates Regulated Proteasomal Degradation of the Nuclear Receptor Coactivator Amplified in Breast Cancer 1 in Immortalized Cells
Mani, A., Oh, A. S., Bowden, E. T., Lahusen, T. J., Lorick, K. L., Weissman, A. M., Schlegel, R., Wellstein, A., & Riegel, A. T. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0557 · Cited by 70
A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis
Nelson, V., Davis, G. E., & Maxwell, S. A. (2001) · APOPTOSIS · doi:10.1023/a:1011392811628 · Cited by 69
Regulation of p53 and MDM2 Activity by MTBP
Brady, M., Vlatković, N., & Boyd, M. T. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.2.545-553.2005 · Cited by 69
Functional Analysis of p53 Binding under Differential Stresses
Krieg, A. J., Hammond, E. M., & Giaccia, A. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00322-06 · Cited by 65
ATM complexes with HDM2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation
de Toledo, S. M., Azzam, E. I., Dahlberg, W. K., Gooding, T. B., & Little, J. B. (2000) · Oncogene · doi:10.1038/sj.onc.1204020 · Cited by 64
Human MDM2 Isoforms Translated Differentially on Constitutive versus p53-Regulated Transcripts Have Distinct Functions in the p53/MDM2 and TSG101/MDM2 Feedback Control Loops
Cheng, T.-H., & Cohen, S. N. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00235-06 · Cited by 62
Novel cancer therapy by reactivation of the p53 apoptosis pathway
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Drosophila Topors Is a RING Finger-containing Protein That Functions as a Ubiquitin-protein Isopeptide Ligase for the Hairy Basic Helix-Loop-Helix Repressor Protein
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Tumor Suppression by p53 without Accelerated Aging: Just Enough of a Good Thing?
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Authors: Horn, H. F., & Vousden, K. H.
Affiliations: Cancer Research UK Scotland Institute (GB)
Corresponding author: Vousden, K H
ORCID: Horn, H F
Vousden, K H
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2007-02-26
Volume: 26
Issue: 9
Pages: 1306-1316
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1210263
OpenAlex: W2035188342
Semantic Scholar: ea46e0441d9175c80c0ddbd29c6fc13c60a82939
Cited by: 522
References: 167
Citations by year: 2026: 5 · 2025: 6 · 2024: 18 · 2023: 22 · 2022: 20 · 2021: 30 · 2020: 23 · 2019: 27 · 2018: 35 · 2017: 37 · 2016: 35 · 2015: 30 · 2014: 26 · 2013: 36 · 2012: 26
FWCI: 3.89
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: p53, stress signals, p53 activation, tumor suppression, stress response pathways, malignant progression, therapeutic target
MeSH terms: Humans, Neoplasms, Signal Transduction, Tumor Suppressor Protein p53, Oxidative Stress

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Coping with stress: multiple ways to activate p53

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