Blinded by the Light: The Growing Complexity of p53

In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2

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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

p53 in health and disease

Vousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,351

TIGAR, 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

Transactivation 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

A phosphorylation-dependent switch in the disordered p53 transactivation domain regulates DNA binding

Sun, X., Dyson, H. J., & Wright, P. E. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2021456118 · Cited by 80

HIPK2 restricts SIRT1 activity upon severe DNA damage by a phosphorylation-controlled mechanism

Conrad, E., Polonio-Vallon, T., Meister, M. T., Matt, S., Bitomsky, N., Herbel, C., Liebl, M. C., Greiner, V., Križnik, B., Schumacher, S. D., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.75 · Cited by 80

Violacein induces apoptosis in human breast cancer cells through up regulation of BAX, p53 and down regulation of MDM2

Alshatwi, A. A., Subash‐Babu, P., & Antonisamy, P. (2015) · Experimental and Toxicologic Pathology · doi:10.1016/j.etp.2015.10.002 · Cited by 80

Ser46 phosphorylation and prolyl-isomerase Pin1-mediated isomerization of p53 are key events in p53-dependent apoptosis induced by mutant huntingtin

Grison, A., Mantovani, F., Comel, A., Agostoni, E., Gustincich, S., Persichetti, F., & Sal, G. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106198108 · Cited by 80

An Ultrahigh Affinity d -Peptide Antagonist Of MDM2

Zhan, C., Zhao, L., Wei, X., Wu, X., Chen, X., Yuan, W., Lu, W., Pazgier, M., & Lu, W. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3005465 · Cited by 80

BAG2 promotes tumorigenesis through enhancing mutant p53 protein levels and function

Yue, X., Zhao, Y., Liu, J., Zhang, C., Yu, H., Wang, J., Zheng, T., Liu, L., Li, J., Feng, Z., et al. (2015) · eLife · doi:10.7554/elife.08401 · Cited by 81

Integrin α5β1 and p53 convergent pathways in the control of anti-apoptotic proteins PEA-15 and survivin in high-grade glioma

Renner, G., Janoušková, H., Noulet, F., Koenig, V., Guérin, É., Bär, S., Nüesch, J. P. F., Rechenmacher, F., Neubauer, S., Kessler, H., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.131 · Cited by 80

Functions of p53 in pluripotent stem cells

Fu, X., Wu, S., Li, B., Xu, Y., & Liu, J. (2019) · Protein & Cell · doi:10.1007/s13238-019-00665-x · Cited by 80

The Mdm network and its regulation of p53 activities: a rheostat of cancer risk

Eischen, C. M., & Lozano, G. (2014) · Human Mutation · doi:10.1002/humu.22524 · Cited by 79

Roles of HAUSP-mediated p53 regulation in central nervous system development

Kon, N., Zhong, J., Kobayashi, Y., Li, M., Szabolcs, M., Ludwig, T., Canoll, P. D., & Gu, W. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.12 · Cited by 79

Rescue of the apoptotic-inducing function of mutant p53 by small molecule RITA

Zhao, C. Y., Grinkevich, V., Nikulenkov, F., Bao, W., & Selivanova, G. (2010) · Cell Cycle · doi:10.4161/cc.9.9.11545 · Cited by 79

p53 promotes the expression of gluconeogenesis-related genes and enhances hepatic glucose production

Goldstein, I., Yizhak, K., Madar, S., Goldfinger, N., Ruppin, E., & Rotter, V. (2013) · Cancer & Metabolism · doi:10.1186/2049-3002-1-9 · Cited by 79

The Ubiquitin-Proteasome System Is Indispensable for the Maintenance of Muscle Stem Cells

Kitajima, Y., Suzuki, N., Nunomiya, A., Osana, S., Yoshioka, K., Tashiro, Y., Takahashi, R., Ono, Y., Aoki, M., & Nagatomi, R. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.10.009 · Cited by 79

Pharmacologically blocking p53-dependent apoptosis protects intestinal stem cells and mice from radiation

Wang, X., Liang, W., Cramer, J. M., Leibowitz, B. J., Judge-Golden, C. P., Epperly, M. W., Greenberger, J. S., Wang, F., Li, L., Stelzner, M. G., et al. (2015) · Scientific Reports · doi:10.1038/srep08566 · Cited by 79

LncRNA H19 promotes triple-negative breast cancer cells invasion and metastasis through the p53/TNFAIP8 pathway

Li, Y., Ma, H., Hu, X., Qu, Y., Wen, X., Zhang, Y., & Xu, Q. (2020) · Cancer Cell International · doi:10.1186/s12935-020-01261-4 · Cited by 79

The C terminus of p53 regulates gene expression by multiple mechanisms in a target- and tissue-specific manner in vivoPreprint

Hamard, P.-J., Barthelery, N. J., Hogstad, B., Mungamuri, S. K., Tonnessen-Murray, C. A., Carvajal, L. A., Senturk, E., Gillespie, V., Aaronson, S. A., Mérad, M., et al. (2013) · Genes & Development · doi:10.1101/gad.224386.113 · Cited by 79

Expanding the p53 regulatory network: LncRNAs take up the challenge

Grossi, E., Sánchez, Y., & Huarte, M. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.07.011 · Cited by 78

Oxidative stress-induced p53 activity is enhanced by a redox-sensitive TP53INP1 SUMOylation

Peuget, S., Bonacci, T., Soubeyran, P., Iovanna, J., & Dusetti, N. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.28 · Cited by 78

p53-mediated transcriptional regulation and activation of the actin cytoskeleton regulatory RhoC to LIMK2 signaling pathway promotes cell survival

Croft, D. R., Crighton, D., Samuel, M. S., Lourenço, F. C., Munro, J., Wood, J. M., Bensaad, K., Vousden, K. H., Sansom, O. J., Ryan, K. M., et al. (2010) · Cell Research · doi:10.1038/cr.2010.154 · Cited by 78

Muscle ankyrin repeat proteins: their role in striated muscle function in health and disease

Kojić, S., Radojkovic, D. P., & Faulkner, G. (2011) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408363.2011.643857 · Cited by 78

Essential Roles of E3 Ubiquitin Ligases in p53 Regulation

Sane, S., & Rezvani, K. S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020442 · Cited by 78

Supramolecular pseudo-block gene carriers based on bioreducible star polycations

Hu, Y., Yuan, W., Zhao, N., Ma, J., Yang, W., & Xu, F. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.03.092 · Cited by 77

PYCR1 and PYCR2 Interact and Collaborate with RRM2B to Protect Cells from Overt Oxidative Stress

Kuo, M.-L., Lee, M. B.-E., Tang, M., den Besten, W., Hu, S., Sweredoski, M. J., Hess, S. Y., Chou, C., Changou, C. A., Su, M., et al. (2016) · Scientific Reports · doi:10.1038/srep18846 · Cited by 77

The Mettl3 epitranscriptomic writer amplifies p53 stress responses

Raj, N., Wang, M., Seoane, J. A., Zhao, R. L., Kaiser, A. M., Moonie, N. A., Demeter, J., Boutelle, A. M., Kerr, C. H., Mulligan, A. S., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.010 · Cited by 77

Mutant TP53 Posttranslational Modifications: Challenges and Opportunities

Nguyen, T., Menéndez, D., Resnick, M. A., & Anderson, C. W. (2014) · Human Mutation · doi:10.1002/humu.22506 · Cited by 77

miR-128 exerts pro-apoptotic effect in a p53 transcription-dependent and -independent manner via PUMA-Bak axis

Adlakha, Y. K., & Saini, N. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.46 · Cited by 77

Growth hormone is a cellular senescence target in pituitary and nonpituitary cells

Chesnokova, V., Zhou, C., Ben-Shlomo, A., Zonis, S., Tani, Y., Ren, S.-G., & Melmed, S. K. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310589110 · Cited by 77

SIRT3 and SIRT4 are mitochondrial tumor suppressor proteins that connect mitochondrial metabolism and carcinogenesis

Zhu, Y., Yan, Y., Principe, D. R., Zou, X., Vassilopoulos, A., & Gius, D. R. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-15 · Cited by 77

Putting the pieces together: How is the mitochondrial pathway of apoptosis regulated in cancer and chemotherapy?

Elkholi, R., Renault, T. T., Serasinghe, M. N., & Chipuk, J. E. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-16 · Cited by 77

RNA content in the nucleolus alters p53 acetylation via MYBBP1A

Kuroda, T., Murayama, A., Katagiri, N., Ohta, Y., Fujita, E., Masumoto, H., Ema, M., Takahashi, S., Kimura, K., & Yanagisawa, J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.23 · Cited by 77

Downregulation of core clock gene Bmal1 attenuates expression of progesterone and prostaglandin biosynthesis-related genes in rat luteinizing granulosa cells

Chen, H., Zhao, L., Kumazawa, M., Yamauchi, N., Shigeyoshi, Y., Hashimoto, S., & Hattori, M. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00008.2013 · Cited by 77

High and Low LET Radiation Differentially Induce Normal Tissue Damage Signals

Niemantsverdriet, M., van Goethem, M., Bron, R., Hogewerf, W., Brandenburg, S., Langendijk, J. A., van Luijk, P., & Coppes, R. P. (2012) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2011.09.057 · Cited by 77

Regulatory module involving FGF13, miR-504, and p53 regulates ribosomal biogenesis and supports cancer cell survival

Bublik, D. R., Bursać, S., Sheffer, M., Oršolić, I., Shalit, T., Tarcic, O., Kotler, E., Mouhadeb, O., Hoffman, Y., Fuchs, G., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614876114 · Cited by 77

Progerin-Induced Replication Stress Facilitates Premature Senescence in Hutchinson-Gilford Progeria Syndrome

Wheaton, K., Campuzano, D., Ma, W., Sheinis, M., Ho, B., Brown, G. W., & Benchimol, S. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00659-16 · Cited by 77

Non-Coding RNAs in Cancer Radiosensitivity: MicroRNAs and lncRNAs as Regulators of Radiation-Induced Signaling Pathways

Podralska, M., Ciesielska, S., Kluiver, J. L., van den Berg, A., Dzikiewicz‐Krawczyk, A., & Ślęzak-Prochazka, I. (2020) · Cancers · doi:10.3390/cancers12061662 · Cited by 76

Multiple transcriptomic profiling: p53 signaling pathway is involved in DEHP-induced prepubertal testicular injury via promoting cell apoptosis and inhibiting cell proliferation of Leydig cells

Wang, J., Zhao, T., Chen, J., Kang, L., Wei, Y., Wu, Y., Han, L., Shen, L., Long, C., Wu, S., et al. (2020) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2020.124316 · Cited by 76

Ubiquitin ligases in cancer: Functions and clinical potentials

Duan, S., & Pagano, M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.008 · Cited by 77

The E3 Ligase Smurf1 Regulates Wolfram Syndrome Protein Stability at the Endoplasmic Reticulum

Guo, X. L., Shen, S., Song, S., He, S., Cui, Y., Xing, G., Wang, J., Yin, Y., Fan, L., He, F., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225615 · Cited by 76

p53 promotes inflammation-associated hepatocarcinogenesis by inducing HMGB1 release

Yan, H., Wu, H., Zhang, H., Ashton, C., Tong, C., Wu, H., Qian, Q., Wang, H.-Y., & Ying, Q. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.05.029 · Cited by 76

Hypersensitivity of Primordial Germ Cells to Compromised Replication-Associated DNA Repair Involves ATM-p53-p21 Signaling

Luo, Y., Hartford, S. A., Zeng, R., Southard, T. L., Shima, N., & Schimenti, J. C. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004471 · Cited by 76

Dnmt3a regulates both proliferation and differentiation of mouse neural stem cells

Wu, Z., Huang, K. Y., Yu, J., Le, T. T., Namihira, M., Liu, Y., Zhang, J., Xue, Z., Cheng, L., & Fan, G. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.23077 · Cited by 76

Reactivation of mutant p53 by capsaicin, the major constituent of peppers

Garufi, A., Pistritto, G., Cirone, M., & D’Orazi, G. (2016) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-016-0417-9 · Cited by 76

Geometric deep learning of protein–DNA binding specificity

Mitra, R., Li, J., Sagendorf, J. M., Jiang, Y., Cohen, A. S., Chiu, T.-P., Glasscock, C. J., & Rohs, R. (2024) · Nature Methods · doi:10.1038/s41592-024-02372-w · Cited by 75

Policing Cancer: Vitamin D Arrests the Cell Cycle

Bhoora, S., & Punchoo, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239296 · Cited by 75

Restoration of the Tumor Suppressor Function of Y220C-Mutant p53 by Rezatapopt, a Small-Molecule Reactivator

Puzio‐Kuter, A. M., Xu, L., McBrayer, M. K., Dominique, R., Li, H. H., Fahr, B. J., Brown, A. M., Wiebesiek, A. E., Russo, B. M., Mulligan, C. L., et al. (2025) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-1421 · Cited by 75

Autophagy regulation in cancer development and therapy.

White, E. J., Martín, V., Liu, J.-L., Klein, S. R., Piya, S., Gomez‐Manzano, C., Fueyo-Margareto, J., & Jiang, H. (2011) · Europe PMC (PubMed Central) · Cited by 76

Analysis of p53 Transactivation Domain Mutants Reveals Acad11 as a Metabolic Target Important for p53 Pro-Survival Function

Jiang, D., LaGory, E. L., Brož, D. K., Bieging-Rolett, K. T., Brady, C. A., Link, N., Abrams, J., Giaccia, A. J., & Attardi, L. D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.043 · Cited by 75

Role of the transcription factor Bcl11b in development and lymphomagenesis

Kominami, R. (2012) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.88.72 · Cited by 75

ATF4 Gene Network Mediates Cellular Response to the Anticancer PAD Inhibitor YW3-56 in Triple-Negative Breast Cancer Cells

Wang, S., Chen, X. A., Hu, J., Jiang, J.-K., Li, Y., Chan-Salis, K. Y., Gu, Y., Chen, G., Thomas, C. J., Pugh, B. F., et al. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-1093-t · Cited by 75

Radioprotection: smart games with death

Gudkov, A. V., & Komarova, E. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43794 · Cited by 75

A microRNA-dependent program controls p53-independent survival and chemosensitivity in human and murine squamous cell carcinoma

Ory, B., Ramsey, M. R., Wilson, C., Vadysirisack, D. D., Forster, N., Rocco, J. W., Rothenberg, S. M., & Ellisen, L. W. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43897 · Cited by 75

Electrocatalytic Monitoring of Metal Binding and Mutation-Induced Conformational Changes in p53 at Picomole Level

Paleček, E., Ostatná, V., Černocká, H., Joerger, A. C., & Fersht, A. R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja201006s · Cited by 75

Metabolomic Profiling of the Synergistic Effects of Melittin in Combination with Cisplatin on Ovarian Cancer Cells

Alonezi, S., Tusiimire, J., Wallace, J., Dufton, M. J., Parkinson, J. A., Young, L., Clements, C. J., Park, J., Jeon, J.-W., Ferro, V. A., et al. (2017) · Metabolites · doi:10.3390/metabo7020014 · Cited by 75

Mitochondrial uncoupling reveals a novel therapeutic opportunity for p53-defective cancers

Kumar, R., Coronel, L., Somalanka, B., Raju, A., Aning, O. A., An, Ö., Ho, Y. S., Chen, S., Mak, S. Y., Hor, P. Y., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05805-1 · Cited by 75

Significance of TP53 mutation in bladder cancer disease progression and drug selection

Wu, G., Wang, F., Li, K., shu-gen, L., Zhao, C., Fan, C., & Wang, J. (2019) · PeerJ · doi:10.7717/peerj.8261 · Cited by 75

Down-regulation of LATS kinases alters p53 to promote cell migrationPreprint

Furth, N., Moshe, N. B. B., Pozniak, Y., Porat, Z., Geiger, T., Domany, E., Aylon, Y., & Oren, M. (2015) · Genes & Development · doi:10.1101/gad.268185.115 · Cited by 75

p53 regulates mitochondrial dynamics by inhibiting Drp1 translocation into mitochondria during cellular senescence

Kim, Y. Y., Um, J., Yoon, J.-H., Lee, D., Lee, Y. J., Kim, D. H., Park, J., & Yun, J. (2019) · The FASEB Journal · doi:10.1096/fj.201901747rr · Cited by 74

Association of the circadian factor Period 2 to p53 influences p53's function in DNA-damage signaling

Gotoh, T., Vila-Caballer, M., Liu, J., Schiffhauer, S., & Finkielstein, C. V. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-05-0994 · Cited by 74

Mitochondrial p53 mediates a transcription-independent regulation of cell respiration and interacts with the mitochondrial F₁F₀-ATP synthase

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

The E3 Ubiquitin Protein Ligase HERC2 Modulates the Activity of Tumor Protein p53 by Regulating Its Oligomerization

Cubillos‐Rojas, M., Amair‐Pinedo, F., Peiró‐Jordán, R., Bartrons, R., Ventura, F., & Rosa, J. L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.527978 · Cited by 74

Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2

Vogel, S., Bauer, M. R., Joerger, A. C., Wilcken, R., Brandt, T., Veprintsev, D. B., Rutherford, T. J., Fersht, A. R., & Boeckler, F. M. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215060109 · Cited by 74

Regulation of tumor suppressor p53 at the RNA level

Vilborg, A., Wilhelm, M., & Wiman, K. G. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-010-0609-2 · Cited by 74

Dysregulation of Mdm2 and Mdm4 alternative splicing underlies motor neuron death in spinal muscular atrophyPreprint

Alstyne, M. V., Simon, C. M., Sardi, S. P., Shihabuddin, L. S., Mentis, G. Z., & Pellizzoni, L. (2018) · Genes & Development · doi:10.1101/gad.316059.118 · Cited by 75

YPEL3, a p53-Regulated Gene that Induces Cellular Senescence

Kelley, K. D., Miller, K. R., Todd, A., Kelley, A. R., Tuttle, R., & Berberich, S. J. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3219 · Cited by 73

A Comprehensive and High-Resolution Genome-wide Response of p53 to Stress

Chang, G. S., Chen, X. A., Park, B., Rhee, H. S., Li, P., Han, K. H., Mishra, T., Chan-Salis, K. Y., Li, Y., Hardison, R. C., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.030 · Cited by 73

Mechanisms involved in alternariol-induced cell cycle arrest

Solhaug, A., Vines, L. L., Ivanova, L., Spilsberg, B., Holme, J. A., Pestka, J. J., Collins, A. R., & Eriksen, G. S. (2012) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2012.09.001 · Cited by 73

Degradation of p53 by Human Alphapapillomavirus E6 Proteins Shows a Stronger Correlation with Phylogeny than Oncogenicity

Fu, L., Doorslaer, K. V., Chen, Z., Ristriani, T., Masson, M., Travé, G., & Burk, R. D. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012816 · Cited by 73

Auto-ubiquitination of Mdm2 Enhances Its Substrate Ubiquitin Ligase Activity

Ranaweera, R. S., & Yang, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.454470 · Cited by 73

Involvement of S100A14 Protein in Cell Invasion by Affecting Expression and Function of Matrix Metalloproteinase (MMP)-2 via p53-dependent Transcriptional Regulation

Chen, H., Yuan, Y., Zhang, C., Luo, A., Ding, F., Ma, J., Yang, S., Tian, Y., Tong, T., Zhan, Q., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.326975 · Cited by 73

Spatio-temporal modelling of the Hes1 and p53-Mdm2 intracellular signalling pathways

Sturrock, M., Terry, A. J., Xirodimas, D. P., Thompson, A. M., & Chaplain, M. A. J. (2010) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2010.12.016 · Cited by 73

Ribosomal protein L4 is a novel regulator of the MDM2-p53 loop

He, X., Li, Y., Dai, M., & Sun, X. (2016) · Oncotarget · doi:10.18632/oncotarget.7479 · Cited by 73

The Ovarian Cycle

Richards, J. S. (2018) · Vitamins and hormones · doi:10.1016/bs.vh.2018.01.009 · Cited by 73

Oncogenic Intra-p53 Family Member Interactions in Human Cancers

Ferraiuolo, M. A., Agostino, S. D., Blandino, G., & Strano, S. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00077 · Cited by 72

Triphala Extract Suppresses Proliferation and Induces Apoptosis in Human Colon Cancer Stem Cells via Suppressing c-Myc/Cyclin D1 and Elevation of Bax/Bcl-2 Ratio

Vadde, R., Radhakrishnan, S., Reddivari, L., & Vanamala, J. (2015) · BioMed Research International · doi:10.1155/2015/649263 · Cited by 72

The clinical development candidate CCT245737 is an orally active CHK1 inhibitor with preclinical activity in RAS mutant NSCLC and Eμ-MYC driven B-cell lymphoma

Walton, M. I., Eve, P. D., Hayes, A., Henley, A. T., Valenti, M. R., Brandon, A. K. D. H., Box, G., Boxall, K. J., Tall, M., Swales, K. E., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4919 · Cited by 72

Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA

Melero, R., Rajagopalan, S., Lázaro, M., Joerger, A. C., Brandt, T., Veprintsev, D. B., Lasso, G., Gil‐Carton, D., Scheres, S. H. W., Carazo, J. M., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015520107 · Cited by 72

The Prognostic Value of the Apoptosis Pathway in Colorectal Cancer: A Review of the Literature on Biomarkers Identified by Immunohistochemistry

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p53 negatively regulates Aurora A via both transcriptional and posttranslational regulation

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