The expanding universe of p53 targets

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890

WebLogo: A Sequence Logo Generator: Figure 1Preprint

Crooks, G. E., Hon, G. C., Chandonia, J., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,418

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

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

Live or let die: the cell's response to p53

Vousden, K. H., & Lü, X. (2002) · Nature reviews. Cancer · doi:10.1038/nrc864 · Cited by 3,231

Blinded by the Light: The Growing Complexity of p53

Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163

A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia

Kastan, M. B., Zhan, Q., El-Deiry, W. S., Carrier, F., Jacks, T., Walsh, W. V., Plunkett, B. S., Vogelstein, B., & Fornace, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90593-2 · Cited by 3,047

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

Definition of a consensus binding site for p53

El-Deiry, W. S., Kern, S. E., Pietenpol, J. A., Kinzler, K. W., & Vogelstein, B. (1992) · Nature Genetics · doi:10.1038/ng0492-45 · Cited by 1,985

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

Two p53 tetramers bind one consensus DNA response element

Kearns, S., Lurz, R., Orlova, E. V., & Okorokov, A. L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw215 · Cited by 37

Discovery of Mieap‐regulated mitochondrial quality control as a new function of tumor suppressor p53

Nakamura, Y., & Arakawa, H. (2017) · Cancer Science · doi:10.1111/cas.13208 · Cited by 36

Emerging roles of long non-coding RNAs in the p53 network

Jain, A. K. (2020) · RNA Biology · doi:10.1080/15476286.2020.1770981 · Cited by 35

The NAD+synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT-2) is a p53 downstream target

Pan, L.-Z., Ahn, D., Sharif, T., Clements, D. R., Gujar, S. A., & Lee, P. W. K. (2014) · Cell Cycle · doi:10.4161/cc.28128 · Cited by 37

Tumor Suppressor WWOX and p53 Alterations and Drug Resistance in Glioblastomas

Chiang, M., Chou, P., Wang, W., Sze, C., & Chang, N. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00043 · Cited by 34

Tumor Suppressor Protein p53 Negatively Regulates Human Pregnane X Receptor Activity

Elias, A., Wu, J., & Chen, T. (2013) · Molecular Pharmacology · doi:10.1124/mol.113.085092 · Cited by 35

A p53 enhancer region regulates target genes through chromatin conformations in cis and in transPreprint

Link, N., Kurtz, P., O’Neal, M. A., Garcia-Hughes, G., & Abrams, J. (2013) · Genes & Development · doi:10.1101/gad.225565.113 · Cited by 37

Chemotherapy-mediated p53-dependent DNA damage response in clear cell renal cell carcinoma: role of the mTORC1/2 and hypoxia-inducible factor pathways

Selvarajah, J., Nathawat, K., Moumen, A., Ashcroft, M. A., & Carroll, V. A. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.395 · Cited by 34

Sulfuretin inhibits 6-hydroxydopamine-induced neuronal cell death via reactive oxygen species-dependent mechanisms in human neuroblastoma SH-SY5Y cells

Kwon, S., Ma, S., Lee, S., & Jang, C. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.04.016 · Cited by 34

Gene-specific transcription activation via long-range allosteric shape-shifting

Tsai, C., & Nussinov, R. (2011) · Biochemical Journal · doi:10.1042/bj20110972 · Cited by 35

Recognition of Local DNA Structures by p53 Protein

Brázda, V., & Coufal, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020375 · Cited by 41

Coumarin-chalcone hybrid instigates DNA damage by minor groove binding and stabilizes p53 through post translational modifications

Ashraf, R., Hamidullah, Hasanain, M., Pandey, P., Maheshwari, M., Singh, L., Siddiqui, M. Q., Konwar, R., Sashidhara, K. V., & Sarkar, J. (2017) · Scientific Reports · doi:10.1038/srep45287 · Cited by 33

Construction and validation of a TP53-associated immune prognostic model for gastric cancer

Nie, K., Zheng, Z., Wen, Y., Shi, L., Xu, S., Wang, X., Zhou, Y., Fu, B., Li, X., Deng, Z., et al. (2020) · Genomics · doi:10.1016/j.ygeno.2020.08.026 · Cited by 34

The Complete Loss of p53 Expression Uniquely Predicts Worse Prognosis in Colorectal Cancer

Nagao, K., Koshino, A., Sugimura‐Nagata, A., Nagano, A., Komura, M., Ueki, A., Ebi, M., Ogasawara, N., Tsuzuki, T., Kasai, K., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23063252 · Cited by 34

RB and p53 Cooperate to Prevent Liver Tumorigenesis in Response to Tissue Damage

McClendon, A. K., Dean, J. L., Ertel, A., Fu, Z., Rivadeneira, D. B., Reed, C. A., Bourgo, R. J., Witkiewicz, A. K., Addya, S., Mayhew, C. N., et al. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.06.046 · Cited by 33

p53-responsive TLR8 SNP enhances human innate immune response to respiratory syncytial virus

Menéndez, D., Snipe, J. R., Marzec, J. M., Innes, C. L., Polack, F. P., Caballero, M. T., Schurman, S. H., Kleeberger, S. R., & Resnick, M. A. (2019) · Journal of Clinical Investigation · doi:10.1172/jci128626 · Cited by 35

Low-level p53 expression changes transactivation rules and reveals superactivating sequences

Jordan, J. J., Menéndez, D., Sharav, J., Beno, I., Rosenthal, K., Resnick, M. A., & Haran, T. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205971109 · Cited by 33

Structural Basis for p53 Lys120-Acetylation-Dependent DNA-Binding Mode

Vainer, R., Cohen, S., Shahar, A., Zarivach, R., & Arbely, E. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.06.009 · Cited by 33

Construction and Validation of an Immune-Related Prognostic Model Based on TP53 Status in Colorectal Cancer

Zhao, X., Liu, J., Liu, S., Yang, F., & Chen, E. (2019) · Cancers · doi:10.3390/cancers11111722 · Cited by 32

Short-term magnesium deficiency upregulates ceramide synthase in cardiovascular tissues and cells: cross-talk among cytokines, Mg2+, NF-κB, and de novo ceramide

Altura, B. M., Shah, N. C., Shah, G. J., Zhang, A., Li, W., Zheng, T., Perez-Albela, J. L., & Altura, B. T. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00453.2011 · Cited by 33

Nonsense mutation-dependent reinitiation of translation in mammalian cells

Cohen, S., Kramarski, L., Levi, S., Deshe, N., David, O. B., & Arbely, E. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz319 · Cited by 35

P53 Family Members Modulate the Expression of PRODH, but Not PRODH2, via Intronic p53 Response Elements

Raimondi, I., Ciribilli, Y., Monti, P., Bisio, A., Pollegioni, L., Fronza, G., Inga, A., & Campomenosi, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069152 · Cited by 32

Modifications of p53 and the DNA Damage Response in Cells Expressing Mutant Form of the Protein Huntingtin

Illuzzi, J. L., Vickers, C. A., & Kmiec, E. B. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9516-4 · Cited by 32

Transglutaminase 2 contributes to a TP53-induced autophagy program to prevent oncogenic transformation

Yeo, S. Y., Itahana, Y., Guo, A. K., Han, R., Iwamoto, K., Nguyen, T., Bao, Y., Kleiber, K., Wu, Y., Bay, B., et al. (2016) · eLife · doi:10.7554/elife.07101 · Cited by 32

Tumor suppressor protein p53 exerts negative transcriptional regulation on human sodium iodide symporter gene expression in breast cancer

Kelkar, M. G., Thakur, B. L., Derle, A., Chatterjee, S., Ray, P., & De, A. (2017) · Breast Cancer Research and Treatment · doi:10.1007/s10549-017-4297-2 · Cited by 31

Complex Regulation of p73 Isoforms after Alteration of Amyloid Precursor Polypeptide (APP) Function and DNA Damage in Neurons

Benosman, S., Meng, X., von Grabowiecki, Y., Palamiuc, L., Hriţcu, L., Groß, I., Mellitzer, G., Taya, Y., Loeffler, J., & Gaiddon, C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.261271 · Cited by 39

Igf2 pathway dependency of the Trp53 developmental and tumour phenotypes

Haley, V., Barnes, D., Sandovici, I., Constância, M., Graham, C. F., Pezzella, F., Bühnemann, C., Carter, E. J., & Hassan, A. B. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201101105 · Cited by 30

5-Lipoxygenase is a direct p53 target gene in humans

Gilbert, B., Ahmad, K. A., Roos, J., Lehmann, C., Chiba, T., Ulrich-Rückert, S., Smeenk, L., van Heeringen, S. J., Maier, T. J., Groner, B., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.06.004 · Cited by 31

Expression of MYSM1 is associated with tumor progression in colorectal cancer

Li, Y., Li, J., He, L., Liu, Y., & Cui, B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177235 · Cited by 30

Fuzzy Tandem Repeats Containing p53 Response Elements May Define Species-Specific p53 Target Genes

Simeonova, I., Lejour, V., Bardot, B., Bouarich-Bourimi, R., Morin, A., Fang, M., Charbonnier, L., & Toledo, F. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002731 · Cited by 34

DRAGO (KIAA0247), a New DNA Damage–Responsive, p53-Inducible Gene That Cooperates With p53 as Oncosuppressor

Polato, F., Rusconi, P., Zangrossi, S., Morelli, F., Boeri, M., Musi, A., Marchini, S., Castiglioni, V., Scanziani, E., Torri, V., et al. (2014) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dju053 · Cited by 30

Global re‐wiring of p53 transcription regulation by the hepatitis B virus X protein

Chan, C. S. C., Thurnherr, T., Wang, J., Gallart‐Palau, X., Sze, S. K., Rozen, S., & Lee, C. G. L. (2016) · Molecular Oncology · doi:10.1016/j.molonc.2016.05.006 · Cited by 30

The PRR11-SKA2 Bidirectional Transcription Unit Is Negatively Regulated by p53 through NF-Y in Lung Cancer Cells

Wang, S., Weng, H., Zhang, Y., Long, Y., Li, Y., Niu, Y., Song, F., & Bu, Y. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18030534 · Cited by 31

ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes

Grimaldi, G., & Corda, D. (2019) · Biochemical Society Transactions · doi:10.1042/bst20180416 · Cited by 30

The Role of p53/p21/p16 in DNA-Damage Signaling and DNA Repair

Kulaberoglu, Y., Gündoğdu, R., & Hergovich, A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803309-8.00015-x · Cited by 30

ERK1/2 activation mediated by the nutlin-3-induced mitochondrial translocation of p53

Lee, S., Shin, S. J., & Kim, H. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1764 · Cited by 29

Specific Recognition of p53 Tetramers by Peptides Derived from p53 Interacting Proteins

Gabizon, R., Brandt, T., Sukenik, S., Lahav, N., Lebendiker, M., Shalev, D. E., Veprintsev, D. B., & Friedler, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038060 · Cited by 29

Modulation of immune responses by the tumor suppressor p53

Lowe, J. M., Shatz, M., Resnick, M. A., & Menéndez, D. (2013) · Biodiscovery · doi:10.7750/biodiscovery.2013.8.2 · Cited by 30

p53 Acts as a Co-Repressor to Regulate Keratin 14 Expression during Epidermal Cell Differentiation

Cai, B., Hsu, P.-C., Hsin, I., Chao, C., Lu, M., Lin, H.-C., Chiou, S., Tao, P., & Chen, J.-Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041742 · Cited by 31

Short-term magnesium deficiency upregulates sphingomyelin synthase and p53 in cardiovascular tissues and cells: relevance to the de novo synthesis of ceramide

Altura, B. M., Shah, N. C., Li, Z., Jiang, X., Zhang, A., Li, W., Zheng, T., Perez-Albela, J. L., & Altura, B. T. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00671.2010 · Cited by 29

Phosphorylation of Daxx by ATM contributes to DNA damage-induced p53 activation.

Tang, J., Agrawal, T., Cheng, Q., Qu, L., Brewer, M. D., Chen, J., & Yang, X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055813 · Cited by 28

The function, mechanisms, and role of the genes PTEN and TP53 and the effects of asbestos in the development of malignant mesothelioma: a review focused on the genes' molecular mechanisms

de Assis, L. V. M., & Isoldi, M. C. (2013) · Tumor Biology · doi:10.1007/s13277-013-1210-4 · Cited by 27

The use of genetically modified mice in cancer risk assessment: Challenges and limitations

Eastmond, D. A., Vulimiri, S. V., French, J. E., & Sonawane, B. R. (2013) · Critical Reviews in Toxicology · doi:10.3109/10408444.2013.822844 · Cited by 28

Rad is a p53 direct transcriptional target that inhibits cell migration and is frequently silenced in lung carcinoma cells

Hsiao, B.-Y., Chen, C.-C., Hsieh, P.-C., Chang, T.-K., Yeh, Y., Wu, Y., Hsu, H., Wang, F.-F., & Chou, T. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0717-z · Cited by 28

A label-free electrochemical test for DNA-binding activities of tumor suppressor protein p53 using immunoprecipitation at magnetic beads

Němcová, K., Havran, L., Šebest, P., Brázdová, M., Pivoňková, H., & Fojta, M. (2010) · Analytica Chimica Acta · doi:10.1016/j.aca.2010.04.018 · Cited by 27

Cooperative interactions between p53 and NFκB enhance cell plasticity

Bisio, A., Zámborszky, J., Zaccara, S., Lion, M., Tebaldi, T., Sharma, V., Raimondi, I., Alessandrini, F., Ciribilli, Y., & Inga, A. (2014) · Oncotarget · doi:10.18632/oncotarget.2545 · Cited by 27

Erythropoietin inhibits chemotherapy-induced cell death and promotes a senescence-like state in leukemia cells

Pham, T.-N. D., Ma, W., Miller, D., Kazakova, L., & Benchimol, S. (2019) · Cell Death and Disease · doi:10.1038/s41419-018-1274-6 · Cited by 27

Salvation of the fallen angel: Reactivating mutant p53

Yang, L., Wang, Z., Chen, Y., Petersen, R. B., Zheng, L., & Huang, K. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14572 · Cited by 27

Elevated transcription of the p53 gene in early S-phase leads to a rapid DNA-damage response during S-phase of the cell cycle

Takahashi, P., Polson, A., & Reisman, D. (2011) · APOPTOSIS · doi:10.1007/s10495-011-0623-z · Cited by 27

p53 Is a Direct Transcriptional Repressor of Keratin 17: Lessons from a Rat Model of Radiation Dermatitis

Liao, C., Xie, G., Zhu, L., Chen, X., Li, X., Lu, H., Xu, B., Ramot, Y., Paus, R., & Yue, Z. (2015) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2015.12.021 · Cited by 27

Interaction of p53 with prolyl isomerases: Healthy and unhealthy relationships

Mantovani, F., Zannini, A., Rustighi, A., & Sal, G. D. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.01.013 · Cited by 30

Mutations in exon 8 of TP53 are associated with shorter survival in patients with advanced lung cancer

Liu, Y., Xu, F., Wang, Y., Wu, Q., Wang, B., Yao, Y., Zhang, Y., Han‐Zhang, H., Ye, J., Zhang, L., et al. (2019) · Oncology Letters · doi:10.3892/ol.2019.10625 · Cited by 26

Chitinase 3 like 1 suppresses the stability and activity of p53 to promote lung tumorigenesis

Park, K., Yun, H., Yoo, K., Ham, Y. W., Han, S., & Hong, J. T. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-019-0503-7 · Cited by 26

NEK10 tyrosine phosphorylates p53 and controls its transcriptional activity

Haider, N., Dutt, P., van de Kooij, B., Ho, J., Palomero, L., Pujana, M. Á., Yaffe, M. B., & Stambolic, V. (2020) · Oncogene · doi:10.1038/s41388-020-1361-x · Cited by 26

The Coordinated P53 and Estrogen Receptor Cis-Regulation at an FLT1 Promoter SNP Is Specific to Genotoxic Stress and Estrogenic Compound

Ciribilli, Y., Andreotti, V., Menéndez, D., Langen, J.-S., Schönfelder, G., Resnick, M. A., & Inga, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010236 · Cited by 26

Tumor-suppressive p53 Signaling Empowers Metastatic Inhibitor KLF17-dependent Transcription to Overcome Tumorigenesis in Non-small Cell Lung Cancer

Ali, A., Bhatti, M. Z., Shah, A. S., Duong, H., Alkreathy, H. M., Mohammad, S. F., Khan, R. A., & Ahmad, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.635730 · Cited by 26

ΔN-P63α and TA-P63α exhibit intrinsic differences in transactivation specificities that depend on distinct features of DNA target sites

Monti, P., Ciribilli, Y., Bisio, A., Foggetti, G., Raimondi, I., Campomenosi, P., Menichini, P., Fronza, G., & Inga, A. (2014) · Oncotarget · doi:10.18632/oncotarget.1845 · Cited by 26

Ultraviolet irradiation promotes FOXP3 transcription via p53 in psoriasis

Zhang, D., Chen, Y., Chen, L., Yang, R., Wang, L., Liu, W., Zhai, Z., & Shen, Z. (2016) · Experimental Dermatology · doi:10.1111/exd.12942 · Cited by 26

Study of Arsenic Sulfide in Solid Tumor Cells Reveals Regulation of Nuclear Factors of Activated T-cells by PML and p53

Ding, W., Tong, Y., Zhang, X., Pan, M., & Chen, S. (2016) · Scientific Reports · doi:10.1038/srep19793 · Cited by 25

Bimodal regulation of p21waf1protein as function of DNA damage levels

Buscemi, G., Ricci, C., Zannini, L., Fontanella, E., Plevani, P., & Delia, D. (2014) · Cell Cycle · doi:10.4161/15384101.2014.946852 · Cited by 25

The role of acetylation sites in the regulation of p53 activity

Wang, Y., Chen, Y., Chen, Q., Zhang, X., Wang, H., Wang, Z., Wang, J., & Tian, C. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-05141-7 · Cited by 27

The complex architecture of p53 binding sites

Senitzki, A., Safieh, J., Sharma, V., Golovenko, D., Danin‐Poleg, Y., Inga, A., & Haran, T. E. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1283 · Cited by 25

An Updated View of the Roles of p53 in Embryonic Stem Cells

Ayaz, G., Yan, H., Malik, N., & Huang, J. L. (2022) · Stem Cells · doi:10.1093/stmcls/sxac051 · Cited by 26

Exploiting the MDM2-CK1α Protein-Protein Interface to Develop Novel Biologics That Induce UBL-Kinase-Modification and Inhibit Cell Growth

Huart, A.-S., MacLaine, N. J., Narayan, V., & Hupp, T. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043391 · Cited by 27

Gene expression profiling of mouse p53-deficient epidermal carcinoma defines molecular determinants of human cancer malignancy

García‐Escudero, R., Martínez‐Cruz, A. B., Santos, M., Lorz, C., Segrelles, C., Garaulet, G., Sáiz-Ladera, C., Costa, C., Buitrago-Pérez, Á., Dueñas, M., et al. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-193 · Cited by 26

Crystal Structures of the DNA-binding Domain Tetramer of the p53 Tumor Suppressor Family Member p73 Bound to Different Full-site Response Elements

Ethayathulla, A. S., Nguyen, H. T., & Viadiu, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.408039 · Cited by 25

Limited cell-autonomous anticancer mechanisms in long-lived bats

Athar, F., Zheng, Z., Riquier, S., Zacher, M., Lu, J. Y., Zhao, Y., Volobaev, V. P., Alcock, D., Galazyuk, A. V., Cooper, L. N., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59403-z · Cited by 26

Context is key: Understanding the regulation, functional control, and activities of the p53 tumour suppressor

Moxley, A. H., & Reisman, D. (2020) · Cell Biochemistry and Function · doi:10.1002/cbf.3590 · Cited by 25

Targeting tumor-stroma communication by blocking endothelin-1 receptors sensitizes high-grade serous ovarian cancer to PARP inhibition

Tocci, P., Román, C., Sestito, R., Castro, V. D., Sacconi, A., Molineris, I., Paolini, F., Carosi, M., Tonon, G., Blandino, G., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-022-05538-6 · Cited by 26

MAP/ERK Kinase Kinase 1 (MEKK1) Mediates Transcriptional Repression by Interacting with Polycystic Kidney Disease-1 (PKD1) Promoter-bound p53 Tumor Suppressor Protein

Islam, M. R., Jiménez, T., Pelham, C. J., Rodova, M., Puri, S., Magenheimer, B. S., Maser, R. L., Widmann, C., & Calvet, J. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145284 · Cited by 25

Relevance of TP53 for CLL diagnostics

Catherwood, M. A., de Castro, D. G., Donaldson, D. M., Clifford, R. M., Mills, K., & Thornton, P. D. (2019) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2018-205622 · Cited by 24

The REGγ-Proteasome Regulates Spermatogenesis Partially by P53-PLZF Signaling

Gao, X. C., Chen, H., Liu, J., Shen, S., Wang, Q., Clement, T. M., Deskin, B., Chen, C., Zhao, D., Wang, L., et al. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.07.010 · Cited by 28

Irreversible Transitions, Bistability and Checkpoint Controls in the Eukaryotic Cell Cycle

Tyson, J. J., & Novák, B. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-385944-0.00014-9 · Cited by 24

Estrogens, regulation of p53 and breast cancer risk: a balancing act

Jerry, D. J., Dunphy, K. A., & Hagen, M. J. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0244-7 · Cited by 23

p53 alters intracellular Ca2+ signaling through regulation of TRPM4

Kappel, S., Ross‐Kaschitza, D., Hauert, B., Rother, K., & Peinelt, C. (2022) · Cell Calcium · doi:10.1016/j.ceca.2022.102591 · Cited by 23

A novel oncoprotein Pirh2: rising from the shadow of MDM2

Wang, Z., Yang, B. R., Dong, L., Peng, B., He, X., & Liu, W. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.01899.x · Cited by 24

Toca-1 is suppressed by p53 to limit breast cancer cell invasion and tumor metastasis

Chander, H., Brien, C. D., Truesdell, P. F., Watt, K., Meens, J., Schick, C., Germain, D., & Craig, A. W. (2014) · Breast Cancer Research · doi:10.1186/s13058-014-0503-x · Cited by 23

In vitro binding properties of tumor suppressor p53 with PUMA and NOXA

Park, M.-J., Jeong, M. S., & Jang, S. B. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.03.001 · Cited by 25

Transcriptome and Molecular Endocrinology Aspects of Epicardial Adipose Tissue in Cardiovascular Diseases: A Systematic Review and Meta-Analysis of Observational Studies

Maghbooli, Z., & Hossein‐Nezhad, A. (2015) · BioMed Research International · doi:10.1155/2015/926567 · Cited by 22

Selective binding of tumor suppressor p53 protein to topologically constrained DNA: Modulation by intercalative drugs

Pivoňková, H., Šebest, P., Pečínka, P., Tichá, O., Němcová, K., Brázdová, M., Jagelská, E. B., Brázda, V., & Fojta, M. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.02.120 · Cited by 22

p53 controls CDC7 levels to reinforce G1 cell cycle arrest upon genotoxic stress

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