The DOI matches its Crossref record; 201 of the 201 references it cites were found in a registry or an index.
Transcriptional control of human p53-regulated genes
Abstract
The p53 protein regulates the transcription of many different genes in response to a wide variety of stress signals. Following DNA damage, p53 regulates key processes, including DNA repair, cell-cycle arrest, senescence and apoptosis, in order to suppress cancer. This Analysis article provides an overview of the current knowledge of p53-regulated genes in these pathways and others, and the mechanisms of their regulation. In addition, we present the most comprehensive list so far of human p53-regulated genes and their experimentally validated, functional binding sites that confer p53 regulation.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“The tumor suppressor p53 functions primarily as a transcription factor.”
From Census and evaluation of p53 target genes (2017) · cites this paper as [5]
In the citing paper
“The prevailing function of the p53 tumor suppressor is the transcriptional control of target genes that regulate numerous cellular processes, including cell cycle and apoptosis.5, 6”
From Census and evaluation of p53 target genes (2017) · cites this paper as [5]
In the citing paper
“p53 is an crucial tumor suppressor that is mutated in more than 50% of human cancers”
From USP10 Regulates p53 Localization and Stability by Deubiquitinating p53 (2010) · cites this paper as Riley et al., 2008
Citations
Cites
p53, the cellular gatekeeper for growth and division
Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693
Self-citationVogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“These include several types of DNA damage: telomere shortening, hypoxia, mitotic spindle damage, heat or cold shock, unfolded proteins, improper ribosomal biogenesis, nutritional deprivation in a transformed cell, and even the activation of some oncogenes by mutatio”
BackgroundSelf-citationEddy, S. R. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.9.755 · Cited by 5,515
Sequence logos: a new way to display consensus sequences
Schneider, T. D., & Stephens, R. M. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.20.6097 · Cited by 3,354
Durbin, R. M., Eddy, S. R., Krogh, A., & Mitchison, G. (1998) · Cambridge University Press eBooks · doi:10.1017/cbo9780511790492 · Cited by 3,255
Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
Gu, W., & Roeder, R. G. (1997) · Cell · doi:10.1016/s0092-8674(00)80521-8 · Cited by 2,559
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,559 · cited 1×
“On the basis of X-ray crystallography studies of the p53 DNA-binding core domain bound to a p53-RE DNA sequence, the most important bases for interactions with the p53 protein are the central RCWWGY, which come into close contact with the amino acids from the p53 core domai”
BackgroundHistone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,233
Wild-type p53 induces apoptosis of myeloid leukaemic cells that is inhibited by interleukin-6
Yonish-Rouach, E., Resnftzky, D., Lotem, J., Sachs, L., Kimchi, A., & Oren, M. (1991) · Nature · doi:10.1038/352345a0 · Cited by 2,079
Maximum Entropy Modeling of Short Sequence Motifs with Applications to RNA Splicing Signals
Yeo, G. W.-M., & Burge, C. B. (2004) · Journal of Computational Biology · doi:10.1089/1066527041410418 · Cited by 2,042
Cited by
Sorted by citations
Items 401–500 of 1,000
The roles and mechanisms of G3BP1 in tumour promotion
Zhang, C.-H., Wang, J., Cai, M., Shao, R., Liu, H., & Zhao, W. (2018) · Journal of drug targeting · doi:10.1080/1061186x.2018.1523415 · Cited by 70
The roles of lncRNA in hepatic fibrosis
Peng, H., Wan, L., Liang, J.-J., Zhang, Y., Ai, W., & Wu, J. (2018) · Cell & Bioscience · doi:10.1186/s13578-018-0259-6 · Cited by 71
p53 Superfamily Proteins in Marine Bivalve Cancer and Stress Biology
Walker, C. W., Beneden, R. J. V., Muttray, A. F., Böttger, S. A., Kelley, M. L., Tucker, A. E., & Thomas, W. K. (2011) · Advances in marine biology · doi:10.1016/b978-0-12-385536-7.00001-7 · Cited by 72
TTK/hMps1 Mediates the p53-Dependent Postmitotic Checkpoint by Phosphorylating p53 at Thr18
Huang, Y., Chang, M. D., & Shieh, S.-Y. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01837-08 · Cited by 78
Structures of three distinct activator–TFIID complexesPreprint
Liu, W.-L., Coleman, R. A., Ma, E., Grob, P., Yang, J. L., Zhang, Y., Dailey, G. M., Nogales, E., & Tjian, R. (2009) · Genes & Development · doi:10.1101/gad.1790709 · Cited by 71
Extensive Post-translational Modification of Active and Inactivated Forms of Endogenous p53
DeHart, C. J., Chahal, J. S., Flint, S. J., & Perlman, D. H. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030254 · Cited by 70
The Enteropathogenic Escherichia coli Effector Cif Induces Delayed Apoptosis in Epithelial Cells
Samba‐Louaka, A., Nougayrède, J., Watrin, C., Oswald, É., & Taieb, F. E. (2009) · Infection and Immunity · doi:10.1128/iai.00860-09 · Cited by 70
Alajez, N. M., Shi, W., Hui, A. B., Yue, S., Ng, R., Lo, K. W., Bastianutto, C., O’Sullivan, B., Gullane, P., & Liu, F. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.85 · Cited by 70
Modulation of the DNA damage response during the life cycle of human papillomaviruses
Anacker, D. C., & Moody, C. A. (2016) · Virus Research · doi:10.1016/j.virusres.2016.11.006 · Cited by 70
Glial Cell AMPA Receptors in Nervous System Health, Injury and Disease
Ceprián, M., & Fulton, D. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102450 · Cited by 76
Kucab, J. E., Phillips, D. H., & Arlt, V. M. (2010) · FEBS Journal · doi:10.1111/j.1742-464x.2010.07676.x · Cited by 70
Trinh, D. L. N., Elwi, A. N., & Kim, S.-W. (2010) · Oncotarget · doi:10.18632/oncotarget.174 · Cited by 69
Tanaka, Y., Nakamura, A., Morioka, M. S., Inoue, S., Tamamori‐Adachi, M., Yamada, K., Taketani, K., Kawauchi, J., Tanaka, M., Miyoshi, J., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026848 · Cited by 69
McDade, S. S., Patel, D., Moran, M., Campbell, J., Fenwick, K., Kozarewa, I., Orr, N., Lord, C. J., Ashworth, A., & McCance, D. J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku299 · Cited by 71
Guo, G., Marrero, L., Rodrı́guez, P. C., Valle, L. D., Ochoa, A. C., & Cui, Y. R. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3810 · Cited by 69
Moonlighting proteins in cancer
Min, K., Lee, S., & Baek, S. J. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.09.022 · Cited by 70
Hünten, S., Kaller, M., Drepper, F., Oeljeklaus, S., Bonfert, T., Erhard, F., Dueck, A., Eichner, N., Friedel, C. C., Meister, G., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.050237 · Cited by 70
Radiotherapy-induced salivary dysfunction: Structural changes, pathogenetic mechanisms and therapies
Acauan, M. D., de Figueiredo, M. A. Z., Cherubini, K., Gomes, A. P., & Salum, F. G. (2015) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2015.09.014 · Cited by 71
Sinha, S., Malonia, S. K., Mittal, S. P. K., Singh, K., Sreenath, K., Kamat, R. H., Mukhopadhyaya, R., Pal, J. K., & Chattopadhyay, S. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.395 · Cited by 67
Activation of Wingless Targets Requires Bipartite Recognition of DNA by TCF
Chang, M. V., Chang, J. L., Gangopadhyay, A., Shearer, A. M., & Cadigan, K. M. (2008) · Current Biology · doi:10.1016/j.cub.2008.10.047 · Cited by 68
Zhang, B., Mehrotra, S., Ng, W. L., & Calvi, B. R. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004581 · Cited by 71
Tsuda, M., Toyomitsu, E., Kometani, M., Tozaki‐Saitoh, H., & Inoue, K. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00719.x · Cited by 66
Oxidative stress induced cellular signaling in RPE cells
Klettner, A. (2011) · Frontiers in Bioscience-Scholar · doi:10.2741/275 · Cited by 69
Abl interconnects oncogenic Met and p53 core pathways in cancer cells
Furlan, A., Stagni, V., Hussain, A., Richelme, S., Conti, F., Prodosmo, A., Destro, A., Roncalli, M. G., Barilà, D., & Maina, F. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.23 · Cited by 73
Bergeaud, M., Mathieu, L., Guillaume, A., Moll, U. M., Mignotte, B., Floch, N. L., Vayssière, J., & Rincheval, V. (2013) · Cell Cycle · doi:10.4161/cc.25870 · Cited by 74
Singer, S., Zhao, R., Barsotti, A. M., Ouwehand, A., Fazollahi, M., Coutavas, E. E., Breuhahn, K., Neumann, O., Longerich, T., Pusterla, T., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.020 · Cited by 69
Stravopodis (2009) · International Journal of Oncology · doi:10.3892/ijo_00000353 · Cited by 67
Chillón, I., & Pyle, A. M. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw599 · Cited by 67
Decoding p53 tumor suppression: a crosstalk between genomic stability and epigenetic control?
Janic, A., Abad, E., & Amelio, I. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01259-9 · Cited by 72
Zhao, H. L., Traganos, F., & Darżynkiewicz, Z. (2008) · Cell Cycle · doi:10.4161/cc.7.19.6750 · Cited by 66
USP11 regulates p53 stability by deubiquitinating p53
Ke, J., Dai, C., Wu, W.-L., Gao, J., Xia, A.-J., Liu, G., Lv, K., & Wu, C. (2014) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1400180 · Cited by 69
T-cell intracellular antigens function as tumor suppressor genes
Sánchez-Jiménez, C., Ludeña, M. D., & Izquierdo, J. M. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.43 · Cited by 65
Long non-coding RNAs in Colorectal Cancer: Progression and Future Directions
Yang, Y. P., Peng, J., Sanjun, C., & Ma, Y. (2017) · Journal of Cancer · doi:10.7150/jca.19794 · Cited by 67
The p53/microRNA Network in Cancer: Experimental and Bioinformatics Approaches
Hünten, S., Siemens, H., Kaller, M., & Hermeking, H. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-5590-1_5 · Cited by 66
The p53 tumor suppressor protein is a critical regulator of hematopoietic stem cell behavior
Liu, Y., Elf, S., Asai, T., Miyata, Y., Liu, Y., Sashida, G., Huang, G., Giandomenico, S. D., Koff, A., & Nimer, S. D. (2009) · Cell Cycle · doi:10.4161/cc.8.19.9627 · Cited by 67
Wild type p53 reactivation: From lab bench to clinic
Selivanova, G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.03.049 · Cited by 68
Rong, J., Hu, R., Song, X., Ha, J., Lu, N., Qi, Q., Tao, L., You, Q., & Guo, Q. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.03.016 · Cited by 65
Andrysík, Z., Kim, J., Tan, A. C., & Espinosa, J. M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.014 · Cited by 68
hSSB1 regulates both the stability and the transcriptional activity of p53
Xu, S., Wu, Y., Chen, Q., Cao, J., Hu, K., Tang, J., Sang, Y., Lai, F., Wang, L., Zhang, R., et al. (2012) · Cell Research · doi:10.1038/cr.2012.162 · Cited by 68
GRWD1 negatively regulates p53 via the RPL11–MDM2 pathway and promotes tumorigenesis
Kayama, K., Watanabe, S., Takafuji, T., Tsuji, T., Hironaka, K., Matsumoto, M., Nakayama, K. I., Enari, M., Kohno, T., Shiraishi, K., et al. (2016) · EMBO Reports · doi:10.15252/embr.201642444 · Cited by 65
Mesoporous Silica Nanoparticles as an Antitumoral-Angiogenesis Strategy
Setyawati, M. I., & Leong, D. T. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b12524 · Cited by 65
Fischer, M., Grundke, I., Sohr, S., Quaas, M., Hoffmann, S., Knörck, A., Gumhold, C., & Rother, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063187 · Cited by 64
Mechanical insights into the regulation of programmed cell death by p53 via mitochondria
Yamada, K., & Yoshida, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.02.009 · Cited by 64
Effectiveness of gene delivery systems for pluripotent and differentiated cells
Rapti, K., Stillitano, F., Karakikes, I., Nonnenmacher, M. E., Weber, T., Hulot, J., & Hajjar, R. J. (2015) · Molecular Therapy — Methods & Clinical Development · doi:10.1038/mtm.2014.67 · Cited by 68
Goto, H., Izawa, I., Li, P., & Inagaki, M. (2012) · Cancer Science · doi:10.1111/j.1349-7006.2012.02280.x · Cited by 68
p63 is an alternative p53 repressor in melanoma that confers chemoresistance and a poor prognosis
Matin, R., Chikh, A., Chong, S. L. P., Mesher, D., Graf, M., Sanzà, P., Senatore, V., Scatolini, M., Moretti, F., Leigh, I. M., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20121439 · Cited by 66
Centrosomes in the DNA damage response—the hub outside the centre
Mullee, L. I., & Morrison, C. G. (2015) · Chromosome Research · doi:10.1007/s10577-015-9503-7 · Cited by 63
Structural and Drug Targeting Insights on Mutant p53
Gomes, A. S., Ramos, H., Inga, A., Sousa, E., & Saraiva, L. (2021) · Cancers · doi:10.3390/cancers13133344 · Cited by 63
Overlapping and Non-overlapping Functions of Condensins I and II in Neural Stem Cell Divisions
Nishide, K., & Hirano, T. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004847 · Cited by 63
More targets, more pathways and more clues for mutant p53
Garritano, S., Inga, A., Gemignani, F., & Landi, S. (2013) · Oncogenesis · doi:10.1038/oncsis.2013.15 · Cited by 64
SUMO-specific protease 2 in Mdm2-mediated regulation of p53
Jiang, M., Chiu, S.-Y., & Hsu, W. (2010) · Cell Death and Differentiation · doi:10.1038/cdd.2010.168 · Cited by 65
Ohashi, T., Idogawa, M., Sasaki, Y., Suzuki, H., & Tokino, T. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0330-t · Cited by 63
Bedoya-López, A., Estrada, K., Sánchez‐Flores, A., Ramı́rez, O. T., Altamirano, C., Segovia, L., Miranda‐Ríos, J., Trujillo‐Roldán, M. A., & Valdez‐Cruz, N. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151529 · Cited by 65
Redmer, T., Walz, I., Klinger, B., Khouja, S., Welte, Y., Schäfer, R., & Regenbrecht, C. R. A. (2017) · Oncogenesis · doi:10.1038/oncsis.2016.88 · Cited by 63
Glycogen synthase kinase 3 promotes p53 mRNA translation via phosphorylation of RNPC1Preprint
Zhang, M., Zhang, J., Chen, X., Cho, S.-J., & Chen, X. (2013) · Genes & Development · doi:10.1101/gad.221739.113 · Cited by 65
CerS6 Is a Novel Transcriptional Target of p53 Protein Activated by Non-genotoxic Stress
Fekry, B., Jeffries, K. A., Esmaeilniakooshkghazi, A., Ogretmen, B., Krupenko, S. A., & Krupenko, N. I. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.716902 · Cited by 59
Potential anticancer properties and mechanisms of thymoquinone in osteosarcoma and bone metastasis
Homayoonfal, M., Asemi, Z., & Yousefi, B. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-022-00320-0 · Cited by 64
Licandro, G., Khor, H. L., Beretta, O., Lai, J., Derks, H., Laudisi, F., Conforti‐Andreoni, C., Qian, H. L., Teng, G. G., Ricciardi‐Castagnoli, P., et al. (2013) · European Journal of Immunology · doi:10.1002/eji.201242918 · Cited by 63
Fischer, M., Quaas, M., Wintsche, A., Müller, G. A., & Engeland, K. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt849 · Cited by 66
Aging and vascular dysfunction: beneficial melatonin effects
Rodella, L. F., Favero, G., Rossini, C., Foglio, E., Bonomini, F., Reiter, R. J., & Rezzani, R. (2011) · AGE · doi:10.1007/s11357-011-9336-z · Cited by 62
Guo, H., Liu, Z., Xu, B., Hu, H., Wei, Z., Liu, Q., Zhang, X., Ding, X., Wang, Y., Zhao, M., et al. (2013) · Aging Cell · doi:10.1111/acel.12138 · Cited by 63
Gupta, S., De, S., Srivastava, V. K., Hussain, M., Kumari, J., Muniyappa, K., & Sengupta, S. (2013) · Carcinogenesis · doi:10.1093/carcin/bgt315 · Cited by 65
Idogawa, M., Sasaki, Y., Suzuki, H., Mita, H., Imai, K., Shinomura, Y., & Tokino, T. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2396 · Cited by 62
Pneumococcal Pneumolysin Induces DNA Damage and Cell Cycle Arrest
Rai, P., He, F., Kwang, J., Engelward, B. P., & Chow, V. T. K. (2016) · Scientific Reports · doi:10.1038/srep22972 · Cited by 65
Bai, H., Wu, M., Zhang, H., & Tang, G. (2017) · Oncotarget · doi:10.18632/oncotarget.20891 · Cited by 69
Role and mechanisms of autophagy, ferroptosis, and pyroptosis in sepsis-induced acute lung injury
Shen, Y., He, Y., Pan, Y., Liu, L., Liu, Y., & Jia, J. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1415145 · Cited by 66
Weilbacher, A., Gutekunst, M., Oren, M., Aulitzky, W. E., & van der Kuip, H. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.284 · Cited by 62
p63 the guardian of human reproduction
Amelio, I., Grespi, F., Annicchiarico‐Petruzzelli, M., & Melino, G. (2012) · Cell Cycle · doi:10.4161/cc.22819 · Cited by 61
Graupner, V., Alexander, E., Overkamp, T., Rothfuss, O. C., Laurenzi, V. D., Gillissen, B. F., Daniel, P. T., Schulze‐Osthoff, K., & Eßmann, F. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2010.179 · Cited by 60
Gutekunst, M., Mueller, T., Weilbacher, A., Dengler, M. A., Bedke, J., Kruck, S., Oren, M., Aulitzky, W. E., & van der Kuip, H. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2876 · Cited by 61
Ohtani, N., Yamakoshi, K., Takahashi, A., & Hara, E. (2010) · Cell Division · doi:10.1186/1747-1028-5-1 · Cited by 62
Dziegielewska, B., Brautigan, D. L., Larner, J. M., & Dziegielewski, J. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0485 · Cited by 64
Cellular senescence and protein degradation
Deschênes‐Simard, X., Lessard, F., Gaumont‐Leclerc, M., Bardeesy, N. M., & Ferbeyre, G. (2014) · Cell Cycle · doi:10.4161/cc.29335 · Cited by 66
Targeting the MDM2-p53 pathway in dedifferentiated liposarcoma
Traweek, R. S., Cope, B. M., Roland, C. L., Keung, E. Z.-Y., Nassif, E. F., & Erstad, D. J. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1006959 · Cited by 64
Zhang, W., Borthakur, G. M., Chen, G., Chen, Y., Mu, H., Ruvolo, V. R., Nomoto, K., Zhao, N., Konopleva, M. Y., & Andreeff, M. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-1580 · Cited by 60
Chai, L., Yang, Y., Yang, H., Zhao, Y., & Wang, H. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.124902 · Cited by 60
Mutant p53 Drives Cancer Metastasis via RCP-Mediated Hsp90α Secretion
Zhang, S., Wang, C., Ma, B., Xu, M., Xu, S., Liu, J., Tian, Y., Fu, Y., & Luo, Y. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107879 · Cited by 61
Adrenocortical stem and progenitor cells: Implications for adrenocortical carcinoma
Simon, D. P., & Hammer, G. D. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.12.006 · Cited by 62
Solá, S., Xavier, J. M., dos Santos, D. M., Aranha, M. M., Morgado, A. L., Jepsen, K., & Rodrigues, C. M. P. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018421 · Cited by 61
Making sense of ubiquitin ligases that regulate p53
Jain, A. K., & Barton, M. C. (2010) · Cancer Biology & Therapy · doi:10.4161/cbt.10.7.13445 · Cited by 60
Illuminating p53 function in cancer with genetically engineered mouse models
Garcia, P. B., & Attardi, L. D. (2014) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2013.12.014 · Cited by 65
ARF and p53 Coordinate Tumor Suppression of an Oncogenic IFN-β-STAT1-ISG15 Signaling Axis
Forys, J. T., Kuzmicki, C. E., Saporita, A. J., Winkeler, C. L., Maggi, L. B., & Weber, J. D. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.026 · Cited by 61
Rap2b, a novel p53 target, regulates p53-mediated pro-survival function
Zhang, X., He, Y., Lee, K. H., Dubois, W., Li, Z., Wu, X., Kovalchuk, A. L., Zhang, W., & Huang, J. L. (2013) · Cell Cycle · doi:10.4161/cc.24364 · Cited by 59
Cho, S.-J., Rossi, A., Jung, Y.-S., Yan, W., Liu, G., Zhang, J., Zhang, M., & Chen, X. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221242110 · Cited by 61
Interrogating the Roles of Post-Translational Modifications of Non-Histone Proteins
Buuh, Z. Y., Lyu, Z., & Wang, R. E. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01817 · Cited by 61
Argininosuccinate synthase 1 is an intrinsic Akt repressor transactivated by p53
Miyamoto, T., Lo, P. H. Y., Saichi, N., Ueda, K., Hirata, M., Tanikawa, C., & Matsuda, K. (2017) · Science Advances · doi:10.1126/sciadv.1603204 · Cited by 60
Recent Small-Molecule Inhibitors of the p53–MDM2 Protein–Protein Interaction
Beloglazkina, A. A., Zyk, N. V., Majouga, A. G., & Beloglazkina, E. K. (2020) · Molecules · doi:10.3390/molecules25051211 · Cited by 59
Ferritin binds and activates p53 under oxidative stress
Lee, J., Jang, H., Cho, E., & Youn, H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.08.125 · Cited by 58
MUTYH, an adenine DNA glycosylase, mediates p53 tumor suppression via PARP-dependent cell death
Oka, S., Leon, J., Tsuchimoto, D., Sakumi, K., & Nakabeppu, Y. (2014) · Oncogenesis · doi:10.1038/oncsis.2014.35 · Cited by 61
One Function—Multiple Mechanisms: The Manifold Activities of p53 as a Transcriptional Repressor
Böhlig, L., & Rother, K. (2011) · BioMed Research International · doi:10.1155/2011/464916 · Cited by 58
The mutant p53 mouse as a pre-clinical model
Jackson, J. G., & Lozano, G. (2013) · Oncogene · doi:10.1038/onc.2012.610 · Cited by 57
Lee, J., Kim, H. J., Yoon, N. A., Lee, W. H., Min, Y. J., Ko, B. K., Lee, B. J., Lee, A., Cha, H. J., Cho, W. J., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt222 · Cited by 58
Shahin, S., Banerjee, S., Singh, S. P., & Chaturvedi, C. M. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv205 · Cited by 59
Tanaka, N., Zhao, M., Tang, L., Patel, A. A., Xi, Q., Van, H. T., Takahashi, H., Osman, A. A., Zhang, J., Wang, J., et al. (2017) · Oncogene · doi:10.1038/s41388-017-0032-z · Cited by 60
Bouhaddou, M., Barrette, A. M., Stern, A. D., Koch, R. J., DiStefano, M. S., Riesel, E. A., Santos, L. C., Tan, A. L., Mertz, A. E., & Birtwistle, M. R. (2018) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1005985 · Cited by 58
When the guardian sleeps: Reactivation of the p53 pathway in cancer
Merkel, O., Taylor, N., Prutsch, N., Staber, P. B., Moriggl, R., Turner, S. D., & Kenner, L. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.02.003 · Cited by 56
Targeting the Ubiquitin-Mediated Proteasome Degradation of p53 for Cancer Therapy
DeVine, T., & Dai, M. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319180009 · Cited by 58
Lei, B., Qi, W., Zhao, Y., Li, Y., Liu, S., Xu, X., Chen, Z., Wan, L., & Shen, H. (2014) · Human Pathology · doi:10.1016/j.humpath.2014.07.026 · Cited by 57
Sonabend, A. M., Bansal, M., Guarnieri, P., Lei, L., Amendolara, B., Soderquist, C. R., Leung, R., Yun, J. J., Kennedy, B. C., Sisti, J. S., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-2150 · Cited by 57
Kung, C.-P., Khaku, S., Jennis, M., Zhou, Y., & Murphy, M. E. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0385 · Cited by 58
Metadata
- Authors
- Riley, T., Sontag, E., Chen, P., & Levine, A.
- Affiliations
- Institute for Advanced Study (US)
- Rutgers, The State University of New Jersey (US)
- Corresponding author
- Riley, Todd
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2008-05
- Volume
- 9
- Issue
- 5
- Pages
- 402-412
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W1964719993
- Cited by
- 1,921
- References
- 201
- Citations by year
- 2026: 36 · 2025: 45 · 2024: 56 · 2023: 73 · 2022: 85 · 2021: 97 · 2020: 79 · 2019: 92 · 2018: 110 · 2017: 134 · 2016: 131 · 2015: 115 · 2014: 154 · 2013: 143 · 2012: 153
- FWCI
- 12.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- p53, transcriptional regulation, p53 target genes, DNA damage response, DNA repair, cell cycle arrest, senescence, apoptosis, tumor suppression, transcription factor binding sites, stress signaling
- MeSH terms
- Base Sequence, Binding Sites, Cell Transformation, Neoplastic, DNA Damage, Gene Expression Regulation, Humans, Markov Chains, Molecular Sequence Data, Regulatory Sequences, Nucleic Acid, Transcription, Genetic, Signal Transduction, Genes, p53, Tumor Suppressor Protein p53, Response Elements, Regulatory Elements, Transcriptional
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