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Blinded by the Light: The Growing Complexity of p53
Open accessAbstract
While the tumor suppressor functions of p53 have long been recognized, the contribution of p53 to numerous other aspects of disease and normal life is only now being appreciated. This burgeoning range of responses to p53 is reflected by an increasing variety of mechanisms through which p53 can function, although the ability to activate transcription remains key to p53's modus operandi. Control of p53's transcriptional activity is crucial for determining which p53 response is activated, a decision we must understand if we are to exploit efficiently the next generation of drugs that selectively activate or inhibit p53.
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“Transient stress leads to induction of p53 which activates DNA repair and leads to quiescence (Vousden and Prives, 2009; Kasteri et al., 2018).”
From Mechanisms of Cellular Senescence: Cell Cycle Arrest and Senescence Associated Secretory Phenotype (2021) · cites this paper as Vousden and Prives, 2009
In the citing paper
“Consequently, p53 target genes become activated and drive cellular responses of tumor cells, which include cell cycle arrest, apoptosis and senescence. 2”
From Mdm2 inhibitors synergize with topoisomerase II inhibitors to induce p53-independent pancreatic cancer cell death (2013) · cites this paper as [2]
In the citing paper
“p53 is a key transcriptional regulator that controls multiple signals by activating genes with roles in cell cycle arrest, senescence, apoptosis, metabolism, differentiation, and survival (Vousden and Prives, 2009).”
From The Mdm network and its regulation of p53 activities: a rheostat of cancer risk (2014) · cites this paper as Vousden and Prives, 2009
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RETRACTED: hnRNP K: An HDM2 Target and Transcriptional Coactivator of p53 in Response to DNA Damage
Moumen, A., Masterson, P., O'Connor, M. J., & Jackson, S. P. (2005) · Cell · doi:10.1016/j.cell.2005.09.032 · Cited by 350
RetractedIn Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation
DeBerardinis, R. J., Lum, J. J., Hatzivassiliou, G., & Thompson, C. B. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.002 · Cited by 4,088
The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820
A microRNA component of the p53 tumour suppressor network
He, L., He, X., Lim, L. P., de Stanchina, E., Xuan, Z., Liang, Y., Xue, W., Zender, L., Magnus, J., Ridzon, D., et al. (2007) · Nature · doi:10.1038/nature05939 · Cited by 2,692
Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473
Vousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,351
Self-citationTIGAR, 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
Self-citationTransactivation of miR-34a by p53 broadly influences gene expression and promotes apoptosis
Chang, T.-C., Wentzel, E. A., Kent, O. A., Ramachandran, K., Mullendore, M., Lee, K. H., Feldmann, G., Yamakuchi, M., Ferlito, M., Lowenstein, C. J., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.010 · Cited by 2,010
Transcriptional control of human p53-regulated genes
Riley, T., Sontag, E., Chen, P., & Levine, A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2395 · Cited by 1,921
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Wu, L., Ma, C. A., Zhao, Y., & Jain, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.174755 · Cited by 94
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Berger, C. E., Qian, Y., Liu, G., Chen, H.-W., & Chen, X. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.367326 · Cited by 93
Pelisch, F., Pozzi, B., Risso, G., Muñoz, M. J., & Srebrow, A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390120 · Cited by 93
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He, F., Borcherds, W. M., Song, T., Wei, X., Das, M., Chen, L., Daughdrill, G. W., & Chen, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903077116 · Cited by 94
Raj, N., & Bam, R. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00159 · Cited by 94
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Mendonça, L. M., Machado, C. D. S., Teixeira, C. C. C., de Freitas, L. A. P., Bianchi, M. D. L. P., & Antunes, L. M. G. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.09.011 · Cited by 92
Wink, S., Hiemstra, S. W., Huppelschoten, S., Danen, E. H. J., Niemeijer, M., Hendriks, G., Vrieling, H., Herpers, B., & van de Water, B. (2014) · Chemical Research in Toxicology · doi:10.1021/tx4004038 · Cited by 93
Roh, J., Kang, S. K., Minn, I., Califano, J. A., Sidransky, D., & Koch, W. M. (2010) · Oral Oncology · doi:10.1016/j.oraloncology.2010.10.011 · Cited by 92
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Yu, F., Bracken, C. P., Pillman, K. A., Lawrence, D., Goodall, G. J., Callen, D. F., & Neilsen, P. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129190 · Cited by 92
Wei, J., Noto, J. M., Zaika, E. I., Romero–Gallo, J., Correa, P., El-Rifai, W. M., Peek, R. M., & Zaika, A. I. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205664109 · Cited by 92
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Brož, D. K., & Attardi, L. D. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp331 · Cited by 92
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Nili, E. L., Field, Y., Lubling, Y., Widom, J., Oren, M., & Segal, E. (2010) · Genome Research · doi:10.1101/gr.103945.109 · Cited by 92
Furth, N., Aylon, Y., & Oren, M. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.163 · Cited by 91
Bauer, M. R., Jones, R. N., Tareque, R. K., Springett, B. R., Dingler, F. A., Verduci, L., Patel, K. J., Fersht, A. R., Joerger, A. C., & Spencer, J. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0181 · Cited by 91
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Mazzà, D., Infante, P., Colicchia, V., Greco, A., Alfonsi, R., Siler, M., Antonucci, L., Pò, A., Smaele, E. D., Ferretti, E., et al. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.120 · Cited by 91
Hasty, P., Sharp, Z. D., Curiel, T. J., & Campisi, J. (2012) · Cell Cycle · doi:10.4161/cc.22912 · Cited by 92
Zhang, J., Feng, F., Wang, Q., Zhu, X., Fu, H., Xu, L., Liu, K., Huang, X., & Zhang, X. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2015-0360 · Cited by 91
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Jacq, X., Kemp, M. I., Martin, N. M. B., & Jackson, S. P. (2013) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-013-9635-3 · Cited by 90
Jiang, D., Brady, C. A., Johnson, T. M., Lee, E. Y., Park, E. J., Scott, M. P., & Attardi, L. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111245108 · Cited by 90
Laudato, S., Patil, N., Abba, M. L., Leupold, J. H., Benner, A., Gaiser, T., Marx, A., & Allgayer, H. (2017) · International Journal of Cancer · doi:10.1002/ijc.30854 · Cited by 90
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Sun, H., Li, L., Li, W., Yang, F., Zhang, Z., Liu, Z., & Du, W. (2021) · EMBO Reports · doi:10.15252/embr.202152537 · Cited by 90
Structure of the p53 C‐terminus bound to 14‐3‐3: Implications for stabilization of the p53 tetramer
Schumacher, B., Mondry, J., Thiel, P., Weyand, M., & Ottmann, C. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.065 · Cited by 90
Akdemir, K. C., Jain, A. K., Allton, K. L., Aronow, B. J., Xu, X., Cooney, A. J., Li, W., & Barton, M. C. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt866 · Cited by 90
The Fundamental Role of the p53 Pathway in Tumor Metabolism and Its Implication in Tumor Therapy
Shen, L., Sun, X. Y., Fu, Z., Yang, G., Li, J., & Yao, L. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-3040 · Cited by 89
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Wang, Y., Ho, T. L. F., Hariharan, A., Goh, H. C., Wong, Y. L., Verkaik, N. S., Lee, M. Y., Tam, W. L., van Gent, D. C., Venkitaraman, A. R., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113233119 · Cited by 89
Pennella, M. A., Liu, Y., Woo, J. L., Kim, C. A., & Berk, A. J. (2010) · Journal of Virology · doi:10.1128/jvi.01442-10 · Cited by 89
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Pharmacological reactivation of p53 in the era of precision anticancer medicine
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Chen, M., Wu, X., Yu, R., Li, C., Wang, L., Shen, W., & Lu, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045388 · Cited by 88
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Self-citationKing, S., Purdie, C. A., Bray, S. E., Quinlan, P., Jordan, L. B., Thompson, A. M., & Meek, D. W. (2012) · Breast Cancer Research · doi:10.1186/bcr3136 · Cited by 88
Laptenko, O., Tong, D. R., Manfredi, J. J., & Prives, C. L. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.011 · Cited by 88
Self-citationSchlereth, K., Heyl, C., Krampitz, A.-M., Mernberger, M., Finkernagel, F., Scharfe, M., Jarek, M., Leich, E., Rosenwald, A., & Stiewe, T. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003726 · Cited by 87
NFκB/p53 crosstalk—a promising new therapeutic target
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Kim, K. M., Ahn, A.-R., Park, H. S., Jang, K. Y., Moon, W. S., Kang, M. J., Ha, G. W., Lee, M. R., & Chung, M. J. (2022) · BMC Cancer · doi:10.1186/s12885-022-10039-y · Cited by 87
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Long, J., Parkin, B. L., Ouillette, P. D., Bixby, D. L., Shedden, K., Erba, H. P., Wang, S., & Malek, S. N. (2010) · Blood · doi:10.1182/blood-2010-01-261628 · Cited by 87
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Solozobova, V. (2011) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v2.i9.202 · Cited by 87
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Moulder, D. E., Hatoum, D., Tay, E. S. E., Lin, Y., & McGowan, E. M. (2018) · Cancers · doi:10.3390/cancers10060189 · Cited by 87
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Kelsen, D. P. (2023) · Frontiers research topics · doi:10.3389/978-2-8325-4252-1 · Cited by 87
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Morachis, J. M., Murawsky, C. M., & Emerson, B. M. (2010) · Genes & Development · doi:10.1101/gad.1856710 · Cited by 86
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Rahman, N., Khan, H. Z., Zia, A., Khan, A., Fakhri, S., Aschner, M., Gul, K., & Saso, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111315 · Cited by 86
Bertamino, A., Soprano, M., Musella, S., Rusciano, M. R., Sala, M., Vernieri, E., Sarno, V. D., Limatola, A., Carotenuto, A., Cosconati, S., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400311n · Cited by 86
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Fan, Y., Lee, T. V., Xu, D., Chen, Z., Lamblin, A.-F., Steller, H., & Bergmann, A. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.182 · Cited by 86
Kolukula, V. K., Sahu, G., Wellstein, A., Rodriguez, O. C., Preet, A., Iacobazzi, V., D’Orazi, G., Albanese, C., Palmieri, F., & Avantaggiati, M. L. (2014) · Oncotarget · doi:10.18632/oncotarget.1831 · Cited by 86
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Hofmann, T. G., Glas, C., & Bitomsky, N. (2012) · BioEssays · doi:10.1002/bies.201200060 · Cited by 86
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Jeay, S., Gaulis, S., Ferretti, S., Bitter, H., Ito, M., Valat, T., Murakami, M., Ruetz, S., Guthy, D. A., Rynn, C., et al. (2015) · eLife · doi:10.7554/elife.06498 · Cited by 85
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Jovanović, K., Escure, G., Demonchy, J., Willaume, A., de Wyngaert, Z. V., Farhat, M.-M., Chauvet, P., Facon, T. T. F., Quesnel, B., & Manier, S. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2018.00665 · Cited by 86
Chen, Y., Zhang, X., Machado, A. C. D., Ding, Y. C., Chen, Z., Qin, P. Z., Rohs, R., & Chen, L. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt584 · Cited by 85
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Wagner, T., Brand, P., Heinzel, T., & Krämer, O. H. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.07.010 · Cited by 85
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Hollstein, M. C., Alexandrov, L. B., Wild, C. P., Ardin, M., & Zavadil, J. (2016) · Oncogene · doi:10.1038/onc.2016.192 · Cited by 85
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Self-citationDistinct p53 genomic binding patterns in normal and cancer-derived human cells
Botcheva, K., McCorkle, S., McCombie, W. R., Dunn, J. J., & Anderson, C. W. (2011) · Cell Cycle · doi:10.4161/cc.10.24.18383 · Cited by 84
Li, T., Liu, X., Jiang, L., Manfredi, J. J., Zha, S., & Gu, W. (2016) · Oncotarget · doi:10.18632/oncotarget.7864 · Cited by 84
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Lessel, D., Wu, D., Trujillo, C., Ramezani, T., Lessel, I., Alwasiyah, M. K., Saha, B., Hisama, F. M., Rading, K., Goebel, I., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci92171 · Cited by 84
Self-citationValidation of MdmX as a therapeutic target for reactivating p53 in tumors
Garcia, D., Warr, M. R., Martins, C. P., Brown Swigart, L., Passegué, E., & Evan, G. I. (2011) · Genes & Development · doi:10.1101/gad.16722111 · Cited by 83
Reviving the guardian of the genome: Small molecule activators of p53
Nguyen, D., Liao, W., Zeng, S. X., & Lu, H. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.03.013 · Cited by 84
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Kawashima, H., Takatori, H., Suzuki, K., Iwata, A., Yokota, M., Suto, A., Minamino, T., Hirose, K., & Nakajima, H. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300509 · Cited by 84
Galluzzi, L., Morselli, E., Kepp, O., Vitale, I., Pinti, M., & Kroemer, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3504 · Cited by 83
Molecular mechanisms of asbestos-induced lung epithelial cell apoptosis
Liu, G., Beri, R., Mueller, A., & Kamp, D. W. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.03.047 · Cited by 83
Wang, W., Qin, J., Voruganti, S., Wang, M., Sharma, H., Patil, S. A., Zhou, J., Wang, H., Mukhopadhyay, D., Buolamwini, J. K., et al. (2014) · Gastroenterology · doi:10.1053/j.gastro.2014.07.001 · Cited by 83
Liu, Y., Xing, R., Zhang, X., Dong, W., Zhang, J., Yan, Z. P., Li, W., Cui, J., & Lu, Y. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.06.002 · Cited by 83
Brandl, A., Wagner, T., Uhlig, K. M., Knauer, S. K., Stauber, R. H., Melchior, F., Schneider, G., Heinzel, T., & Krämer, O. H. (2012) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjs013 · Cited by 83
Bauer, M. R., Jones, R. N., Baud, M. G. J., Wilcken, R., Boeckler, F. M., Fersht, A. R., Joerger, A. C., & Spencer, J. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00315 · Cited by 83
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Ryu, H.-W., Shin, D.-H., Lee, D. H., Choi, J., Han, G., Lee, K. Y., & Kwon, S. H. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.01.033 · Cited by 82
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Zhu, Y., Dean, A. E., Horikoshi, N., Heer, C. D., Spitz, D. R., & Gius, D. R. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120844 · Cited by 82
Zhao, S., Chi, H., Yang, Q., Chen, S., Wu, C., Lai, G., Xu, K., Su, K., Luo, H., Peng, G., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1090040 · Cited by 82
Roudier, E. A., Gineste, C., Wazna, A., Dehghan, K., Dominique Desplanches, C., & Birot, O. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2010.193243 · Cited by 82
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Zhuang, J., Wang, P., Huang, X., Chen, X. S., Kang, J., & Hwang, P. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310908110 · Cited by 82
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Zawacka‐Pankau, J., & Selivanova, G. (2015) · Journal of Internal Medicine · doi:10.1111/joim.12336 · Cited by 82
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Flöter, J., Kaymak, I., & Schulze, A. (2017) · Metabolites · doi:10.3390/metabo7020021 · Cited by 81
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Cui, D., Xiong, X., Shu, J., Dai, X.-Q., Sun, Y., & Zhao, Y. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.12.032 · Cited by 82
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Hume, S., Grou, C. P. O., Lascaux, P., D’Angiolella, V., Legrand, A. J., Ramadan, K., & Dianov, G. L. (2021) · Nature Communications · doi:10.1038/s41467-021-27124-8 · Cited by 81
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Aylon, Y., & Oren, M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026328 · Cited by 81
Metadata
- Authors
- Vousden, K. H., & Prives, C.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- Columbia University (US)
- Corresponding author
- Vousden, Karen H.
- Prives, Carol
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 137
- Issue
- 3
- Pages
- 413-431
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2133959309
- Semantic Scholar
- 018e8ed8c8694d45cfd9ffaf967368345fe22af6
- Cited by
- 3,163
- References
- 232
- Citations by year
- 2026: 128 · 2025: 154 · 2024: 127 · 2023: 168 · 2022: 149 · 2021: 166 · 2020: 175 · 2019: 149 · 2018: 171 · 2017: 191 · 2016: 228 · 2015: 202 · 2014: 258 · 2013: 263 · 2012: 228
- FWCI
- 17.35
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1538 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- Cancer Research UK
- National Cancer Institute (R01CA077742, CA77742)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- p53, tumor suppressor, transcriptional activation, p53 activators, p53 inhibitors, p53 regulation
- MeSH terms
- Animals, Cell Survival, Cell Transformation, Neoplastic, Gene Expression Regulation, Humans, Mutation, Stress, Physiological, Transcriptional Activation, Tumor Suppressor Protein p53, Apoptosis, Cell Proliferation, Mice
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