The DOI matches its Crossref record; 231 of the 232 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
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
Cited by
Sorted by citations
Items 201–300 of 1,016
The Response to and Repair of RAG-Mediated DNA Double-Strand Breaks
Helmink, B. A., & Sleckman, B. P. (2012) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101320 · Cited by 199
Acetylation-regulated interaction between p53 and SET reveals a widespread regulatory mode
Wang, D., Kon, N., Lasso, G., Jiang, L., Leng, W., Zhu, W., Qin, J., Honig, B. H., & Gu, W. J. (2016) · Nature · doi:10.1038/nature19759 · Cited by 198
The Metabolic Mechanisms of Breast Cancer Metastasis
Wang, L., Zhang, S., & Wang, X. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.602416 · Cited by 200
Uversky, V. N. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111874 · Cited by 196
Mutant p53 Gain-of-Function: Role in Cancer Development, Progression, and Therapeutic Approaches
Alvarado-Ortiz, E., de la Cruz-López, K. G., Becerril-Rico, J., Sarabia-Sánchez, M. Á., Ortíz-Sánchez, E., & García-Carrancá, A. M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607670 · Cited by 203
The link between immunity, autoimmunity and endometriosis: a literature update
Zhang, T., De Carolis, C., Man, G. C. W., & Wang, C. C. (2018) · Autoimmunity Reviews · doi:10.1016/j.autrev.2018.03.017 · Cited by 196
Vascular senescence in cardiovascular and metabolic diseases
Katsuumi, G., Shimizu, I., Yoshida, Y., & Minamino, T. (2018) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2018.00018 · Cited by 196
Chronic inflammation and cancer: the role of the mitochondria.
Kamp, D. W., Shacter, E. B., & Weitzman, S. A. (2011) · PubMed · Cited by 196
Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1
Sun, X., Challagundla, K. B., & Dai, M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.434 · Cited by 195
p53 regulates Period2 expression and the circadian clock
Miki, T., Matsumoto, T., Zhao, Z., & Lee, C. C. (2013) · Nature Communications · doi:10.1038/ncomms3444 · Cited by 195
Tao, R., Vassilopoulos, A., Parisiadou, L., Yan, Y., & Gius, D. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5482 · Cited by 194
Deconstructing p53 transcriptional networks in tumor suppression
Bieging, K. T., & Attardi, L. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.006 · Cited by 194
53BP1 Integrates DNA Repair and p53-Dependent Cell Fate Decisions via Distinct Mechanisms
Cuella-Martin, R., Oliveira, C., Lockstone, H. E., Snellenberg, S., Grolmusova, N., & Chapman, J. R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.002 · Cited by 194
The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo
Huang, L., Yan, Z., Liao, X., Li, Y., Yang, J., Wang, Z.-G., Zuo, Y., Kawai, H., Shadfan, M., Ganapathy, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102309108 · Cited by 193
Shimizu, I., Yoshida, Y., Katsuno, T., Tateno, K., Okada, S., Moriya, J., Yokoyama, M., Nojima, A., Ito, T. K., Zechner, R., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.12.006 · Cited by 192
Recent Advances in p53 Research and Cancer Treatment
Suzuki, K., & Matsubara, H. (2011) · BioMed Research International · doi:10.1155/2011/978312 · Cited by 191
Long non-coding RNAs in the doxorubicin resistance of cancer cells
Ashrafizaveh, S., Ashrafizadeh, M., Zarrabi, A., Husmandi, K., Zabolian, A., Shahinozzaman, M., Aref, A. R., Hamblin, M. R., Nabavi, N., Crea, F., et al. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.03.018 · Cited by 191
The Interferon Stimulated Gene 54 Promotes Apoptosis
Stawowczyk, M., Scoy, S. V., Kumar, K. P., & Reich, N. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.207068 · Cited by 190
Targeting Programmed Cell Death Using Small‐Molecule Compounds to Improve Potential Cancer Therapy
Ke, B., Tian, M., Li, J., Liu, B., & He, G. (2016) · Medicinal Research Reviews · doi:10.1002/med.21398 · Cited by 190
p53-dependent Induction of PVT1 and miR-1204
Barsotti, A. M., Beckerman, R., Laptenko, O., Huppi, K. E., Caplen, N. J., & Prives, C. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.322875 · Cited by 189
Self-citationp53 Regulation of Metabolic PathwaysPreprint
Gottlieb, E., & Vousden, K. H. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001040 · Cited by 189
Self-citationChlorogenic acid effectively treats cancers through induction of cancer cell differentiation
Huang, S., Wang, L.-L., Xue, N., Li, C., Guo, H., Ren, T., Zhan, Y., Li, W., Zhang, J., Chen, X., et al. (2019) · Theranostics · doi:10.7150/thno.34674 · Cited by 188
Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells
Borcherds, W. M., Theillet, F., Katzer, A., Finzel, A., Mishall, K. M., Powell, A. T., Wu, H., Manieri, W., Dieterich, C., Selenko, P., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1668 · Cited by 187
Overview of cyclins D1 function in cancer and the CDK inhibitor landscape: past and present
Casimiro, M. C., Velasco-Velázquez, M. A., Aguirre-Alvarado, C., & Pestell, R. G. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.867017 · Cited by 183
Metabolic Regulation of Apoptosis in Cancer
Matsuura, K., Canfield, K., Feng, W. W., & Kurokawa, M. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.06.006 · Cited by 183
Nikulenkov, F., Spinnler, C., Li, H., Tonelli, C., Shi, Y., Turunen, M. M., Kivioja, T., Ignatiev, I., Kel, A. E., Taipale, J., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.89 · Cited by 181
Mutant p53 mediates survival of breast cancer cells
Lim, L. Y., Vidnovic, N., Ellisen, L. W., & Leong, C.-O. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6605335 · Cited by 181
Mutant p53 reactivation by small molecules makes its way to the clinic
Bykov, V. J. N., & Wiman, K. G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.04.017 · Cited by 181
The role of the p53 tumor suppressor in metabolism and diabetes
Kung, C.-P., & Murphy, M. E. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0324 · Cited by 186
A p53 Super-tumor Suppressor Reveals a Tumor Suppressive p53-Ptpn14-Yap Axis in Pancreatic Cancer
Mello, S. S., Valente, L. J., Raj, N., Seoane, J. A., Flowers, B. M., McClendon, J., Bieging-Rolett, K. T., Lee, J., Ivanochko, D., Kozak, M. M., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.09.007 · Cited by 179
Ribosomal Proteins RPL37, RPS15 and RPS20 Regulate the Mdm2-p53-MdmX Network
Daftuar, L., Zhu, Y. Y., Jacq, X., & Prives, C. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068667 · Cited by 179
Self-citationChen, R., Liu, Y., Zhuang, H., Yang, B., Hei, K., Xiao, M., Hou, C., Gao, H., Zhang, X., Jia, C., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx600 · Cited by 179
Bourougaa, K., Naski, N., Boularan, C., Mlynarczyk, C., Candeias, M. M., Marullo, S., & Fåhræus, R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.041 · Cited by 178
The Transactivation Domains of the p53 ProteinPreprint
Raj, N., & Attardi, L. D. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026047 · Cited by 178
Mammalian DNA repair: HATs and HDACs make their mark through histone acetylation
Gong, F., & Miller, K. M. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.07.002 · Cited by 175
Do Airway Epithelium Air–Liquid Cultures Represent the In Vivo Airway Epithelium Transcriptome?
Dvořák, A., Tilley, A. E., Shaykhiev, R., Wang, R., & Crystal, R. G. (2010) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2009-0453oc · Cited by 175
Role of p53 Serine 46 in p53 Target Gene Regulation
Smeenk, L., van Heeringen, S. J., Koeppel, M., Gilbert, B., Janssen‐Megens, E. M., Stunnenberg, H. G., & Lohrum, M. A. E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017574 · Cited by 174
DNA-Mediated Charge Transport in Redox Sensing and Signaling
Genereux, J. C., Boal, A. K., & Barton, J. K. (2010) · Journal of the American Chemical Society · doi:10.1021/ja907669c · Cited by 174
Senescence in Wound Repair: Emerging Strategies to Target Chronic Healing Wounds
Wilkinson, H. N., & Hardman, M. J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00773 · Cited by 173
Zhu, J., Liu, S., Ye, F., Shen, Y., Tie, Y., Zhu, J., Wei, L., Jin, Y., Fu, H., Wu, Y., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139790 · Cited by 175
The role of DNA damage responses in p53 biology
Speidel, D. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1459-z · Cited by 172
Drug resistance in multiple myeloma: latest findings and new concepts on molecular mechanisms
Abdi, J., Chen, G., & Chang, H. (2013) · Oncotarget · doi:10.18632/oncotarget.1497 · Cited by 172
Tang, Z., Chen, W., Shimada, M., Nguyen, U. T. T., Kim, J., Sun, X., Sengoku, T., McGinty, R. K., Fernandez, J., Muir, T. W., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.027 · Cited by 171
Gong, X., Smith, J., Swanson, H., & Rubin, L. P. (2018) · Molecules · doi:10.3390/molecules23040905 · Cited by 171
GSK-3α is a central regulator of age-related pathologies in mice
Zhou, J., Freeman, T. A., Ahmad, F., Shang, X., Mangano, E. N., Gao, E., Farber, J. L., Wang, Y., Ma, X.-L., Woodgett, J. R., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64398 · Cited by 170
The relationship between the nucleolus and cancer: Current evidence and emerging paradigms
Oršolić, I., Jurada, D., Pullen, N., Oren, M., Eliopoulos, A. G., & Volarević, S. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.12.004 · Cited by 170
Limiting the power of p53 through the ubiquitin proteasome pathwayPreprint
Pant, V., & Lozano, G. (2014) · Genes & Development · doi:10.1101/gad.247452.114 · Cited by 170
FIP200 is required for maintenance and differentiation of postnatal neural stem cells
Wang, C., Liang, C.-C., Bian, Z. C., Zhu, Y., & Guan, J.-L. (2013) · Nature Neuroscience · doi:10.1038/nn.3365 · Cited by 169
Exploring the multiple roles of guardian of the genome: P53
Feroz, W., & Sheikh, A. M. A. (2020) · Egyptian Journal of Medical Human Genetics · doi:10.1186/s43042-020-00089-x · Cited by 172
The role of ubiquitin modification in the regulation of p53
Hock, A. K., & Vousden, K. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.022 · Cited by 168
Self-citationMethods and biomarkers for early detection, prediction, and diagnosis of colorectal cancer
Zhang, Y., Wang, Y., Zhang, B., Li, P., & Zhao, Y. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114786 · Cited by 171
Wang, Y., Li, P., Wang, S., Hu, J., Chen, X. A., Wu, J., Fisher, M., Oshaben, K., Gu, Y., Gu, Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.375725 · Cited by 166
Wang, Q., Zou, Y., Nowotschin, S., Kim, S. Y., Li, Q. V., Soh, C.-L., Su, J., Zhang, C., Shu, W., Xi, Q., et al. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.10.002 · Cited by 166
MOZ increases p53 acetylation and premature senescence through its complex formation with PML
Rokudai, S., Laptenko, O., Arnal, S. M., Taya, Y., Kitabayashi, I., & Prives, C. L. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300490110 · Cited by 165
Self-citationYadavilli, S., Mayo, L. D., Higgins, M., Laı́n, S., Hegde, V. K., & Deutsch, W. A. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.07.003 · Cited by 165
Activation of the tumor suppressor p53 upon impairment of ribosome biogenesis
Bursać, S., Brdovčak, M. C., Donati, G., & Volarević, S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.014 · Cited by 166
Mehta, S. V., Huillard, E., Kesari, S., Maire, C. L., Golebiowski, D., Harrington, E. P., Alberta, J. A., Kane, M., Theisen, M., Ligon, K. L., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.035 · Cited by 165
Tong, X., Zhao, F., Mancuso, A., Gruber, J. J., & Thompson, C. B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911316106 · Cited by 165
Role of Mutagenicity in Asbestos Fiber-Induced Carcinogenicity and Other Diseases
Huang, S. X. L., Jaurand, M.-C., Kamp, D. W., Whysner, J., & Hei, T. K. (2011) · Journal of Toxicology and Environmental Health, Part B · doi:10.1080/10937404.2011.556051 · Cited by 163
Current understanding of the role and targeting of tumor suppressor p53 in glioblastoma multiforme
England, B., Huang, T., & Karsy, M. (2013) · Tumor Biology · doi:10.1007/s13277-013-0871-3 · Cited by 163
Pro-proliferative FoxM1 is a target of p53-mediated repression
Barsotti, A. M., & Prives, C. L. (2009) · Oncogene · doi:10.1038/onc.2009.282 · Cited by 163
Self-citationEpithelial Plasticity, Cancer Stem Cells, and the Tumor-Supportive Stroma in Bladder Carcinoma
van der Horst, G., Bos, L., & van der Pluijm, G. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0274 · Cited by 163
Mage-A Cancer/Testis Antigens Inhibit p53 Function by Blocking Its Interaction with Chromatin
Marcar, L., MacLaine, N. J., Hupp, T. R., & Meek, D. W. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1341 · Cited by 163
Pettitt, A. R., Jackson, R., Carruthers, S., Dodd, J. M., Dodd, S. R., Oates, M., Johnson, G. G., Schuh, A., Matutes, E., Dearden, C. E., et al. (2012) · Journal of Clinical Oncology · doi:10.1200/jco.2011.35.9695 · Cited by 163
Tubular p53 Regulates Multiple Genes to Mediate AKI
Zhang, D., Liu, Y., Wei, Q., Huo, Y., Liu, K., Liu, F., & Dong, Z. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013080902 · Cited by 162
Caught in the cross fire: p53 in inflammation
Cooks, T., Harris, C. C., & Oren, M. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu134 · Cited by 162
p53, Stem Cells, and Reprogramming: Tumor Suppression beyond Guarding the Genome
Spike, B. T., & Wahl, G. M. (2011) · Genes & Cancer · doi:10.1177/1947601911410224 · Cited by 160
p53 Activates the Long Noncoding RNA Pvt1b to Inhibit Myc and Suppress Tumorigenesis
Olivero, C. E., Martínez‐Terroba, E., Zimmer, J. T., Liao, C., Tesfaye, E., Hooshdaran, N., Schofield, J. A., Bendor, J., Fang, D., Simon, M. D., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.014 · Cited by 159
Should mutant TP53 be targeted for cancer therapy?
Wang, Z., Strasser, A., & Kelly, G. L. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00962-9 · Cited by 162
He, Y., Wu, Y., Huang, C., Meng, X., Ma, T., Wu, B., Xu, F., Zhang, L., Lv, X., & Li, J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.08.015 · Cited by 158
Samarakoon, R., Dobberfuhl, A. D., Cooley, C., Overstreet, J. M., Patel, S. P., Goldschmeding, R., Meldrum, K. K., & Higgins, P. J. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.07.007 · Cited by 158
p53 as guardian of the mitochondrial genome
Park, J., Zhuang, J., Li, J., & Hwang, P. M. (2016) · FEBS Letters · doi:10.1002/1873-3468.12061 · Cited by 158
The role of tumor suppressor p53 in the antioxidant defense and metabolism
Budanov, A. V. (2014) · Subcellular Biochemistry · doi:10.1007/978-94-017-9211-0_18 · Cited by 157
p53 activates transcription by directing structural shifts in Mediator
Meyer, K. D., Lin, S., Bernecky, C., Gao, Y., & Taatjes, D. J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1816 · Cited by 157
Integrins in the Spotlight of Cancer
Bianconi, D., Unseld, M., & Prager, G. W. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122037 · Cited by 157
Targeting MDM2-p53 Interaction for Cancer Therapy: Are We There Yet?
Nag, S. A., Zhang, X., Srivenugopal, K. S., Wang, M.-H., Wang, W., & Zhang, R. (2014) · Current Medicinal Chemistry · doi:10.2174/09298673113206660325 · Cited by 156
Crystal Structure of the p53 Core Domain Bound to a Full Consensus Site as a Self-Assembled Tetramer
Chen, Y., Dey, R., & Chen, L. (2010) · Structure · doi:10.1016/j.str.2009.11.011 · Cited by 156
p53 increases MHC class I expression by upregulating the endoplasmic reticulum aminopeptidase ERAP1
Wang, B., Niu, D., Lai, L., & Ren, E. C. (2013) · Nature Communications · doi:10.1038/ncomms3359 · Cited by 156
p53 β-hydroxybutyrylation attenuates p53 activity
Liu, K., Li, F., Sun, Q., Lin, N., Han, H., You, K., Tian, F., Mao, Z., Li, T., Tong, T., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1463-y · Cited by 156
Andrysík, Z., Galbraith, M. D., Guarnieri, A. L., Zaccara, S., Sullivan, K. D., Pandey, A., MacBeth, M. L., Inga, A., & Espinosa, J. M. (2017) · Genome Research · doi:10.1101/gr.220533.117 · Cited by 155
The role of hyperoxia in the pathogenesis of experimental BPD
Buczynski, B. W., Maduekwe, E. T., & O’Reilly, M. A. (2013) · Seminars in Perinatology · doi:10.1053/j.semperi.2013.01.002 · Cited by 154
Regulation of Cellular Metabolism and Hypoxia by p53Preprint
Humpton, T. J., & Vousden, K. H. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026146 · Cited by 154
Self-citationThe transcription factor p53: Not a repressor, solely an activator.
Fischer, M., Steiner, L., & Engeland, K. (2014) · Cell Cycle · doi:10.4161/15384101.2014.949083 · Cited by 153
The C terminus of p53 binds the N-terminal domain of MDM2
Poyurovsky, M. V., Katz, C., Laptenko, O., Beckerman, R., Lokshin, M., Ahn, J., Byeon, I. L., Gabizon, R., Mattia, M., Zupnick, A., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1872 · Cited by 153
Self-citationThe regulation of cellular metabolism by tumor suppressor p53
Liang, Y., Liu, J., & Feng, Z. (2013) · Cell & Bioscience · doi:10.1186/2045-3701-3-9 · Cited by 154
Ferredoxin reductase is critical for p53-dependent tumor suppression via iron regulatory protein 2Preprint
Zhang, Y., Qian, Y., Zhang, J., Yan, W., Jung, Y.-S., Chen, M., Huang, E. C., Lloyd, K. C. K., Duan, Y., Wang, J., et al. (2017) · Genes & Development · doi:10.1101/gad.299388.117 · Cited by 153
Guadagno, J., Swan, P., Shaikh, R., & Cregan, S. P. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.151 · Cited by 152
Melanoma: From Melanocyte to Genetic Alterations and Clinical Options
Bertolotto, C. (2013) · Scientifica · doi:10.1155/2013/635203 · Cited by 152
Carvajal, L. A., Hamard, P.-J., Tonnessen, C., & Manfredi, J. J. (2012) · Genes & Development · doi:10.1101/gad.184911.111 · Cited by 151
Yonemori, K., Kurahara, H., Maemura, K., & Natsugoe, S. (2016) · Journal of Human Genetics · doi:10.1038/jhg.2016.59 · Cited by 151
Osteosarcoma: Molecular Pathogenesis and iPSC Modeling
Lin, Y.-H., Jewell, B. E., Gingold, J., Lu, L., Zhao, R., Wang, L. L., & Lee, D.-F. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.06.004 · Cited by 150
The genetic basis of phenotypic heterogeneity in myelodysplastic syndromes
Raza, A., & Galili, N. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3321 · Cited by 150
The DEAD box proteins DDX5 (p68) and DDX17 (p72): Multi-tasking transcriptional regulators
Fuller-Pace, F. V. (2013) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2013.03.004 · Cited by 150
Another fork in the road—life or death decisions by the tumour suppressor p53
Carvajal, L. A., & Manfredi, J. J. (2013) · The EMBO Reports · doi:10.1038/embor.2013.25 · Cited by 149
ATM-Dependent Downregulation of USP7/HAUSP by PPM1G Activates p53 Response to DNA Damage
Khoronenkova, S. V., Dianova, I. I., Ternette, N., Kessler, B. M., Parsons, J. L., & Dianov, G. L. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.021 · Cited by 149
Massively regulated genes: the example of TP53
Hollstein, M. C., & Hainaut, P. L. (2009) · The Journal of Pathology · doi:10.1002/path.2637 · Cited by 149
Lei, L., Sonabend, A. M., Guarnieri, P., Soderquist, C. R., Ludwig, T. E., Rosenfeld, S. A., Bruce, J. N., & Canoll, P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020041 · Cited by 149
Pfister, N. T., Fomin, V., Regunath, K., Zhou, J. Y., Zhou, W., Silwal‐Pandit, L., Freed-Pastor, W. A., Laptenko, O., Neo, S. P., Bargonetti, J., et al. (2015) · Genes & Development · doi:10.1101/gad.263202.115 · Cited by 149
Self-citationArboleda, V. A., Lee, H., Dorrani, N., Zadeh, N., Willis, M. J. H., Macmurdo, C., Manning, M. A., Hanson‐Kahn, A., Hudgins, L., Barthélémy, F., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.01.017 · Cited by 148
Pharmacological reactivation of mutant p53: from protein structure to the cancer patient
Wiman, K. G. (2010) · Oncogene · doi:10.1038/onc.2010.188 · Cited by 148
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review