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The first 30 years of p53: growing ever more complex.
Open accessAbstract
Thirty years ago p53 was discovered as a cellular partner of simian virus 40 large T-antigen, the oncoprotein of this tumour virus. The first decade of p53 research saw the cloning of p53 DNA and the realization that p53 is not an oncogene but a tumour suppressor that is very frequently mutated in human cancer. In the second decade of research, the function of p53 was uncovered: it is a transcription factor induced by stress, which can promote cell cycle arrest, apoptosis and senescence. In the third decade after its discovery new functions of this protein were revealed, including the regulation of metabolic pathways and cytokines that are required for embryo implantation. The fourth decade of research may see new p53-based drugs to treat cancer. What is next is anybody's guess.
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“Both these pathways are complex as they involve many upstream regulators and downstream effectors along with varying side branches (Chau and Wang, 2003; Levine and Oren, 2009).”
From Mechanisms of Cellular Senescence: Cell Cycle Arrest and Senescence Associated Secretory Phenotype (2021) · cites this paper as Levine and Oren, 2009
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WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,218 · cited 1×
“More recently, induction of cellular senescence was identified as an additional mechanism whereby p53 curbs neoplastic processe”
Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
The retinoblastoma protein and cell cycle control
Weinberg, R. A. (1995) · Cell · doi:10.1016/0092-8674(95)90385-2 · Cited by 4,862
In 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
Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
Donehower, L. A., Harvey, M., Slagle, B. L., McArthur, M. J., Montgomery, C. A., Butel, J. S., & Bradley, A. (1992) · Nature · doi:10.1038/356215a0 · Cited by 4,649
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Self-citationTumor suppressor p53 is a direct transcriptional activator of the human bax gene
Toshiyuki, M., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90412-3 · Cited by 4,063
The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
Scheffner, M., Werness, B. A., Huibregtse, J. M., Levine, A. J., & Howley, P. M. (1990) · Cell · doi:10.1016/0092-8674(90)90409-8 · Cited by 3,995
Self-citationGerm Line p53 Mutations in a Familial Syndrome of Breast Cancer, Sarcomas, and Other Neoplasms
Malkin, D., Li, F. P., Strong, L. C., Fraumeni, J. F., Nelson, C. E., Kim, D. H., Kassel, J., Gryka, M. A., Bischoff, F. Z., Tainsky, M. A., et al. (1990) · Science · doi:10.1126/science.1978757 · Cited by 3,765
Flagged first, then by citations
1 of the 169 references couldn’t be matched to a known paper.
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Aging, Cellular Senescence, and Cancer
Campisi, J. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183653 · Cited by 2,954
Cell-free nucleic acids as biomarkers in cancer patients
Schwarzenbach, H., Hoon, D. S. �., & Pantel, K. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3066 · Cited by 2,897
ROS signalling in the biology of cancer
Moloney, J. N., & Cotter, T. G. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.05.023 · Cited by 2,019
Mechanisms of Cellular Senescence: Cell Cycle Arrest and Senescence Associated Secretory Phenotype
Kumari, R., & Jat, P. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.645593 · Cited by 1,622
The molecular landscape of head and neck cancer
Leemans, C. R., Snijders, P. J. F., & Brakenhoff, R. H. (2018) · Nature reviews. Cancer · doi:10.1038/nrc.2018.11 · Cited by 1,457
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324
Cell cycle regulation: p53-p21-RB signaling
Engeland, K. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00988-z · Cited by 1,367
Mutant p53: one name, many proteinsPreprint
Freed-Pastor, W. A., & Prives, C. L. (2012) · Genes & Development · doi:10.1101/gad.190678.112 · Cited by 1,286
Hellmann, M. D., Nathanson, T., Rizvi, H., Creelan, B. C., Sanchez-Vega, F., Ahuja, A., Ni, A., Novik, J. B., Mangarin, L. M. B., Abu-Akeel, M., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.018 · Cited by 1,095
Census and evaluation of p53 target genes
Fischer, M. (2017) · Oncogene · doi:10.1038/onc.2016.502 · Cited by 971
Rivlin, N., Brosh, R., Oren, M., & Rotter, V. (2011) · Genes & Cancer · doi:10.1177/1947601911408889 · Cited by 1,033
Self-citationElectrochemical Methods for the Analysis of Clinically Relevant Biomolecules
Labib, M., Sargent, E. H., & Kelley, S. O. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00220 · Cited by 994
Awakening guardian angels: drugging the p53 pathway
Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2763 · Cited by 881
Exploiting senescence for the treatment of cancer
Wang, L., Lankhorst, L., & Bernards, R. (2022) · Nature Reviews Cancer · doi:10.1038/s41568-022-00450-9 · Cited by 867
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 871
DNA Replication Stress as a Hallmark of Cancer
Macheret, M., & Halazonetis, T. D. (2015) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040424 · Cited by 852
Mitochondrial reactive oxygen species and cancer
Sullivan, L. B., & Chandel, N. S. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-17 · Cited by 826
Activation of SAT1 engages polyamine metabolism with p53-mediated ferroptotic responses
Ou, Y., Wang, S.-J., Li, D., Chu, B., & Gu, W. J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1607152113 · Cited by 783
Revealing strengths and weaknesses of methods for gene network inference
Marbach, D., Prill, R. J., Schaffter, T., Mattiussi, C., Floreano, D., & Stolovitzky, G. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913357107 · Cited by 755
Mutant p53 Gain-of-Function in CancerPreprint
Oren, M., & Rotter, V. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001107 · Cited by 778
Self-citationGenetic landscape of esophageal squamous cell carcinoma
Gao, Y., Chen, Z.-L., Li, J.-G., Hu, X.-D., Shi, X.-J., Sun, Z.-M., Zhang, F., Zhao, Z.-R., Li, Z.-T., Liu, Z.-Y., et al. (2014) · Nature Genetics · doi:10.1038/ng.3076 · Cited by 695
Cell cycle arrest through indirect transcriptional repression by p53: I have a DREAM
Engeland, K. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.172 · Cited by 679
The effects of deregulated DNA damage signalling on cancer chemotherapy response and resistance
Bouwman, P., & Jonkers, J. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3342 · Cited by 615
Mustafa, M., Ahmad, R., Tantry, I. Q., Ahmad, W., Siddiqui, S., Alam, M., Abbas, K., Moinuddin, Hassan, M. I., Habib, S., et al. (2024) · Cells · doi:10.3390/cells13221838 · Cited by 595
The Two Faces of Reactive Oxygen Species in Cancer
Reczek, C. R., & Chandel, N. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041916-065808 · Cited by 602
“However, when p53 is lost or mutated, as observed in more than 50% of human cancers, ROS accumulation can occur, allowing for protumorigenic signaling and cellular transformation (Levine & Oren 2009).”
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Kiraz, Y., Adan, A., Yandım, M. K., & Baran, Y. (2016) · Tumor Biology · doi:10.1007/s13277-016-5035-9 · Cited by 605
Heger, M., van Golen, R. F., Broekgaarden, M., & Michel, M. C. (2013) · Pharmacological Reviews · doi:10.1124/pr.110.004044 · Cited by 593
p53 in ferroptosis regulation: The new weapon for the old guardian
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Oncogenes and Tumor Suppressor GenesPreprint
Lee, E. Y., & Muller, W. J. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003236 · Cited by 575
Understanding the complexity of p53 in a new era of tumor suppression
Liu, Y., Su, Z., Tavana, O., & Gu, W. J. (2024) · Cancer Cell · doi:10.1016/j.ccell.2024.04.009 · Cited by 527
Mutant p53 in cancer: from molecular mechanism to therapeutic modulation
Chen, X., Zhang, T., Su, W., Dou, Z., Zhao, D., Jin, X., Lei, H., Wang, J., Xie, X., Cheng, B., et al. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05408-1 · Cited by 494
Mutant p53 Drives Pancreatic Cancer Metastasis through Cell-Autonomous PDGF Receptor β Signaling
Weissmueller, S., Manchado, E., Saborowski, M., Morris, J. P., Wagenblast, E., Davis, C. A., Moon, S.-H., Pfister, N. T., Tschaharganeh, D. F., Kitzing, T., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.066 · Cited by 466
“However, mutant p53 is neither a targetable cell-surface protein nor a druggable enzyme (Levine and Oren, 2009), and novel therapeutic modalities, such as RNAi or restoring wild-type p53 conformations, have yet to show efficacy in clinical studies (Lehmann and Pietenpol, 2012).”
Cooks, T., Pateras, I. S., Tarcic, O., Solomon, H., Schetter, A. J., Wilder, S., Lozano, G., Pikarsky, E., Forshew, T., Rozenfeld, N., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.03.022 · Cited by 478
Self-citationAcetylation Is Crucial for p53-Mediated Ferroptosis and Tumor Suppression
Wang, S.-J., Li, D., Ou, Y., Jiang, L., Chen, Y., Zhao, Y., & Gu, W. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.022 · Cited by 466
Dimitrova, N., Zamudio, J. R., Jong, R. M., Soukup, D., Resnick, R., Sarma, K., Ward, A. J., Raj, A., Lee, J. T., Sharp, P. A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.04.025 · Cited by 445
STAT3 Target Genes Relevant to Human Cancers
Carpenter, R., & Lo, H.-W. (2014) · Cancers · doi:10.3390/cancers6020897 · Cited by 511
Tumour-associated mutant p53 drives the Warburg effect
Zhang, C., Liu, J., Liang, Y., Wu, R., Zhao, Y., Hong, X., Lin, M., Yu, H., Liu, L., Levine, A. J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3935 · Cited by 434
Self-citationA dominant-negative effect drives selection of TP53 missense mutations in myeloid malignancies
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The MDM2-p53 pathway revisited
Nag, S. A., Jiangjiang, Q., Kalkunte, S. S., Ming-hai, W., & Zhang, R. (2013) · Journal of Biomedical Research · doi:10.7555/jbr.27.20130030 · Cited by 436
Cancer genetics and genomics of human FOX family genes
Katoh, M., Igarashi, M., Fukuda, H., Nakagama, H., & Katoh, M. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.09.017 · Cited by 401
The role of mutant p53 in human cancer
Goh, A. M., Coffill, C. R., & Lane, D. P. (2010) · The Journal of Pathology · doi:10.1002/path.2784 · Cited by 408
Xu-Monette, Z. Y., Wu, L., Visco, C., Tai, Y. C., Tzankov, A., Liu, W., Montes‐Moreno, S., Dybkær, K., Chiu, A., Orazi, A., et al. (2012) · Blood · doi:10.1182/blood-2012-05-433334 · Cited by 404
MDM2 inhibition: an important step forward in cancer therapy
Konopleva, M. Y., Martinelli, G., Daver, N. G., Papayannidis, C., Wei, A. H., Higgins, B., Ott, M., Mascarenhas, J. O., & Andreeff, M. (2020) · Leukemia · doi:10.1038/s41375-020-0949-z · Cited by 380
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Nechiporuk, T., Kurtz, S. E., Nikolova, O. H., Liu, T., Jones, C. L., D’Alessandro, A., Culp‐Hill, R., d’Almeida, A., Joshi, S. K., Rosenberg, M. W., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0125 · Cited by 392
Brady, C. A., & Attardi, L. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.064501 · Cited by 400
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Li, X.-L. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i1.84 · Cited by 381
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Bondar, T., & Medzhitov, R. (2010) · Cell Stem Cell · doi:10.1016/j.stem.2010.03.002 · Cited by 342
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Reed, S. M., & Quelle, D. E. (2014) · Cancers · doi:10.3390/cancers7010030 · Cited by 344
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Yue, X., Zhao, Y., Xu, Y., Zheng, M., Feng, Z., & Hu, W. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.030 · Cited by 308
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Fischer, M., Quaas, M., Steiner, L., & Engeland, K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv927 · Cited by 339
Uxa, S., Castillo-Binder, P., Kohler, R., Stangner, K., Müller, G. A., & Engeland, K. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00823-x · Cited by 315
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The human long non-coding RNA-RoR is a p53 repressor in response to DNA damage
Zhang, A., Zhou, N., Huang, J., Liu, Q., Fukuda, K., Ma, D., Lü, Z., Bai, C., Watabe, K., & Mo, Y. (2012) · Cell Research · doi:10.1038/cr.2012.164 · Cited by 308
Tumor suppressor p53 and metabolism
Liu, J., Zhang, C., Hu, W., & Feng, Z. (2018) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjy070 · Cited by 311
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Schwitalla, S., Ziegler, P. K., Horst, D., Becker, V., Kerle, I., Begus-Nahrmann, Y., Lechel, A., Rudolph, K. L., Langer, R., Slotta-Huspenina, J., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2012.11.014 · Cited by 296
p53 Family and Cellular Stress Responses in Cancer
Pflaum, J., Schlosser, S., & ller, M. M. ⁄. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00285 · Cited by 309
Kotler, E., Shani, O., Goldfeld, G., Lotan‐Pompan, M., Tarcic, O., Gershoni, A., Hopf, T. A., Marks, D. S., Oren, M., & Segal, E. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.06.012 · Cited by 292
Self-citationSignaling pathways in cancer‐associated fibroblasts: recent advances and future perspectives
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The impact of acetylation and deacetylation on the p53 pathway
Brooks, C. L., & Gu, W. J. (2011) · Protein & Cell · doi:10.1007/s13238-011-1063-9 · Cited by 279
The choice between p53-induced senescence and quiescence is determined in part by the mTOR pathway.
Korotchkina, L. G., Leontieva, O. V., Bukreeva, E. I., Demidenko, Z. N., Gudkov, A. V., & Blagosklonny, M. V. (2010) · Aging · doi:10.18632/aging.100160 · Cited by 278
Deletions linked to TP53 loss drive cancer through p53-independent mechanisms
Liu, Y., Chen, C., Xu, Z., Scuoppo, C., Rillahan, C. D., Gao, J., Spitzer, B. G., Bosbach, B., Kastenhuber, E. R., Baslan, T., et al. (2016) · Nature · doi:10.1038/nature17157 · Cited by 279
Millevoi, S., Moine, H., & Vagner, S. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1113 · Cited by 291
Paradoxical suppression of cellular senescence by p53
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Tumor suppressor p53 and its mutants in cancer metabolism
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The complexity of p53-mediated metabolic regulation in tumor suppression
Liu, Y., & Gu, W. J. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.03.010 · Cited by 263
Cell Senescence: Role in Aging and Age-Related Diseases
Campisi, J., & Robert, L. (2014) · Interdisciplinary Topics in Gerontology and Geriatrics · doi:10.1159/000358899 · Cited by 240
Martin, J. W., Squire, J. A., & Zieleńska, M. (2012) · Sarcoma · doi:10.1155/2012/627254 · Cited by 254
Mutant p53 in cancer therapy—the barrier or the path
Zhou, X. Y., Hao, Q., & Lu, H. (2018) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjy072 · Cited by 248
Small RNA combination therapy for lung cancer
Xue, W., Dahlman, J. E., Tammela, T., Khan, O. F., Sood, S., Dave, A., Cai, W., Chirino, L. M., Yang, G. R., Bronson, R. T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412686111 · Cited by 247
MYC and the Control of ApoptosisPreprint
McMahon, S. B. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014407 · Cited by 240
Meitinger, F., Anzola, J. V., Kaulich, M., Richardson, A., Stender, J. D., Benner, C. W., Glass, C. K., Dowdy, S. F., Desai, A. B., Shiau, A. K., et al. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604081 · Cited by 244
Schulz‐Heddergott, R., Stark, N., Edmunds, S. J., Li, J., Conradi, L., Bohnenberger, H., Ceteci, F., Greten, F. R., Dobbelstein, M., & Moll, U. M. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.07.004 · Cited by 243
Scherz‐Shouval, R., Weidberg, H., Gonen, C., Wilder, S., Elazar, Z., & Oren, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006124107 · Cited by 243
Self-citationGenetically engineered pigs as models for human disease
Perleberg, C., Kind, A., & Schnieke, A. (2018) · Disease Models & Mechanisms · doi:10.1242/dmm.030783 · Cited by 222
Targeting tumour-supportive cellular machineries in anticancer drug development
Dobbelstein, M., & Moll, U. M. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4201 · Cited by 232
Francies, F. Z., Hull, R., Khanyile, R., & Dlamini, Z. (2020) · PubMed Central · Cited by 228
Wang, W., Nag, S. A., Zhang, X., Wang, M., Wang, H., Zhou, J., & Zhang, R. (2014) · Medicinal Research Reviews · doi:10.1002/med.21327 · Cited by 232
p53-family proteins and their regulators: hubs and spokes in tumor suppression
Collavin, L., Lunardi, A., & Sal, G. D. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.35 · Cited by 225
Ubiquitin ligases: guardians of mammalian development
Walma, D. A. C., Chen, Z., Bullock, A. N., & Yamada, K. M. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00448-5 · Cited by 218
Biological functions of p53 isoforms through evolution: lessons from animal and cellular models
Marcel, V., Dichtel-Danjoy, M.-L., Sagne, C., Hafsi, H., Ma, D., Ortiz‐Cuaran, S., Olivier, M., Hall, J. A., Mollereau, B., Hainaut, P. L., et al. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.120 · Cited by 210
Inflammation and p53: A Tale of Two Stresses
Gudkov, A. V., Gurova, K. V., & Komarova, E. A. (2011) · Genes & Cancer · doi:10.1177/1947601911409747 · Cited by 211
Beyond ATM: The protein kinase landscape of the DNA damage response
Bensimon, A., Aebersold, R. H., & Shiloh, Y. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.013 · Cited by 214
Intrinsically disordered regions as affinity tuners in protein–DNA interactions
Vuzman, D., & Levy, Y. (2011) · Molecular BioSystems · doi:10.1039/c1mb05273j · Cited by 202
Li, W., Li, F., Zhang, X., Lin, H., & Xu, C. S. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00825-8 · Cited by 211
p53 genes function to restrain mobile elementsPreprint
Wylie, A., Jones, A. E., D’Brot, A., Lu, W.-J., Kurtz, P., Moran, J. V., Rakheja, D., Chen, K. S.-M., Hammer, R. E., Comerford, S. A., et al. (2015) · Genes & Development · doi:10.1101/gad.266098.115 · Cited by 204
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Metadata
- Authors
- Levine, A. J., & Oren, M.
- Affiliations
- Institute for Advanced Study (US)
- Weizmann Institute of Science (IL)
- Venue
- Nature Reviews Cancer
- Published
- 2009-10
- Volume
- 9
- Issue
- 10
- Pages
- 749-758
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- PMC
- PMC2771725
- OpenAlex
- W1966163762
- Cited by
- 1,967
- References
- 169
- Citations by year
- 2026: 64 · 2025: 111 · 2024: 107 · 2023: 112 · 2022: 114 · 2021: 129 · 2020: 128 · 2019: 111 · 2018: 127 · 2017: 120 · 2016: 144 · 2015: 115 · 2014: 150 · 2013: 113 · 2012: 170
- FWCI
- 9.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (P01CA087497, R37 CA40099, R37CA040099, P01CA87497.)
- 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, TP53, tumour suppressor, SV40 large T antigen, transcription factors, cell cycle arrest, apoptosis, cellular senescence, metabolic regulation, cytokine regulation, embryo implantation
- MeSH terms
- Animals, Humans, Neoplasms, Genes, p53, Tumor Suppressor Protein p53, History, 20th Century, History, 21st Century
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