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

Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D2concept

Uversky, V. N. (2010) · Expert Review of Proteomics · doi:10.1586/epr.10.36 · Cited by 147

Interaction of p53 with the CCT Complex Promotes Protein Folding and Wild-Type p53 Activity

Trinidad, A. G., Muller, P. A. J., Cuéllar, J., Klejnot, M., Nobis, M., Valpuesta, J., & Vousden, K. H. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.002 · Cited by 147

p53 and stem cells: new developments and new concerns

Zhao, T., & Xu, Y. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.12.004 · Cited by 147

The DNA damage response and immune signaling alliance: Is it good or bad? Nature decides when and where

Pateras, I. S., Havaki, S., Nikitopoulou, X., Vougas, K. N., Townsend, P. A., Panayiotidis, M. I., Georgakilas, A. G., & Gorgoulis, V. G. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.06.011 · Cited by 147

TGF-β1 → SMAD/p53/USF2 → PAI-1 transcriptional axis in ureteral obstruction-induced renal fibrosis

Samarakoon, R., Overstreet, J. M., Higgins, S. P., & Higgins, P. J. (2011) · Cell and Tissue Research · doi:10.1007/s00441-011-1181-y · Cited by 146

An overview of transcriptional regulation in response to toxicological insult

Jennings, P., Limonciel, A., Felice, L., & Leonard, M. O. (2012) · Archives of Toxicology · doi:10.1007/s00204-012-0919-y · Cited by 147

SOCS1 Links Cytokine Signaling to p53 and Senescence

Calabrese, V., Mallette, F. A., Deschênes‐Simard, X., Ramanathan, S., Gagnon, J., Moores, A., Ilangumaran, S., & Ferbeyre, G. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.044 · Cited by 146

Transcriptional Regulation by Wild-Type and Cancer-Related Mutant Forms of p53Preprint

Pfister, N. T., & Prives, C. L. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026054 · Cited by 146

The zebrafish as a model organism for the study of apoptosis

Eimon, P. M., & Ashkenazi, A. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0432-9 · Cited by 145

Gain-of-function mutant p53 downregulates miR-223 contributing to chemoresistance of cultured tumor cells

Masciarelli, S., Fontemaggi, G., Agostino, S. D., Donzelli, S., Carcarino, E., Strano, S., & Blandino, G. (2013) · Oncogene · doi:10.1038/onc.2013.106 · Cited by 144

Distinct Expression Profiles of p63 Variants during Urothelial Development and Bladder Cancer Progression

Karni-Schmidt, O., Castillo-Martín, M., HuaiShen, T., Gladoun, N., Domenech, J. M. D., Sänchez‐Carbayo, M., Li, Y., Lowe, S. W., Prives, C. L., & Cordon‐Cardo, C. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.061 · Cited by 144

Endothelial p53 Deletion Improves Angiogenesis and Prevents Cardiac Fibrosis and Heart Failure Induced by Pressure Overload in Mice

Gogiraju, R., Xu, X., Bochenek, M. L., Steinbrecher, J. H., Lehnart, S. E., Wenzel, P., Kessel, M., Zeisberg, E. M., Dobbelstein, M., & Schäfer, K. (2015) · Journal of the American Heart Association · doi:10.1161/jaha.115.001770 · Cited by 144

PRMT5 is required for lymphomagenesis triggered by multiple oncogenic drivers

Li, Y., Chitnis, N., Nakagawa, H., Kita, Y., Natsugoe, S., Yang, Y., Li, Z., Wasik, M., Klein-Szanto, A. J. P., Rustgi, A. K., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0625 · Cited by 143

Computational tools to model halogen bonds in medicinal chemistry.

Ford, M. C., & Ho, P. S. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00997 · Cited by 143

MicroRNA Control of p53

Liu, J., Zhang, C., Zhao, Y., & Feng, Z. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25609 · Cited by 143

How mutations shape p53 interactions with the genome to promote tumorigenesis and drug resistance

Stiewe, T., & Haran, T. E. (2018) · Drug Resistance Updates · doi:10.1016/j.drup.2018.05.001 · Cited by 143

p53 mutants cooperate with HIF-1 in transcriptional regulation of extracellular matrix components to promote tumor progression

Amelio, I., Mancini, M., Petrova, V., Cairns, R. A., Вихрева, П. Н., Nicolai, S., Marini, A., Antonov, A. A., Quesne, J. P. C. L., Acevedo, J. D. B., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1808314115 · Cited by 143

Myc-induced AMPK-phospho p53 pathway activates Bak to sensitize mitochondrial apoptosis

Nieminen, A. I., Eskelinen, V., Haikala, H. M., Tervonen, T. A., Yan, Y., Partanen, J. I., & Klefström, J. T. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208530110 · Cited by 142

Morpholino artifacts provide pitfalls and reveal a novel role for pro-apoptotic genes in hindbrain boundary development

Gerety, S. S., & Wilkinson, D. G. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.11.030 · Cited by 141

Regulation of p53: a collaboration between Mdm2 and MdmX

Pei, D., Zhang, Y., & Zheng, J. (2012) · Oncotarget · doi:10.18632/oncotarget.443 · Cited by 140

The critical role of catalase in prooxidant and antioxidant function of p53

Kang, M. Y., Kim, H.-B., Piao, C., Lee, K. K., Hyun, J. W., Chang, I.-Y., & You, H. J. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.102 · Cited by 140

E3 ubiquitin ligase TRIM32 negatively regulates tumor suppressor p53 to promote tumorigenesis

Liu, J., Zhang, C., Wang, X. L., Ly, P., Белый, В. А., Xu-Monette, Z. Y., Young, K. H., Hu, W., & Feng, Z. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.121 · Cited by 139

The pro-longevity gene FoxO3 is a direct target of the p53 tumor suppressor

Renault, V. M., Thekkat, P. U., Hoang, K., White, J. L., Brady, C. A., Brož, D. K., Venturelli, O. S., Johnson, T. M., Oskoui, P. R., Xuan, Z., et al. (2011) · Oncogene · doi:10.1038/onc.2011.35 · Cited by 139

MicroRNAs: critical regulators of epithelial to mesenchymal (EMT) and mesenchymal to epithelial transition (MET) in cancer progression

Bullock, M. D., Sayan, A. E., Packham, G., & Mirnezami, A. H. (2011) · Biology of the Cell · doi:10.1111/boc.201100115 · Cited by 138

Inhibition of p53 inhibitors: progress, challenges and perspectives

Sanz, G., Singh, M., Peuget, S., & Selivanova, G. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz075 · Cited by 140

Mechanisms and regulations of ferroptosis

Zhang, X.-D., Liu, Z., Wang, M.-S., Guo, Y.-X., Wang, X., Luo, K., Huang, S., & Li, R. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1269451 · Cited by 138

Targeting of Mutant p53 and the Cellular Redox Balance by APR-246 as a Strategy for Efficient Cancer Therapy

Bykov, V. J. N., Zhang, Q., Zhang, M., Ceder, S., Abrahmsen, L., & Wiman, K. G. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00021 · Cited by 137

Wild-type p53 controls cell motility and invasion by dual regulation of MET expression

Hwang, C., Matoso, A., Corney, D. C., Flesken‐Nikitin, A., Körner, S., Wang, W., Boccaccio, C., Thorgeirsson, S. S., Comoglio, P. M., Hermeking, H., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017536108 · Cited by 137

Immunomodulatory Function of the Tumor Suppressor p53 in Host Immune Response and the Tumor Microenvironment

Cui, Y. R., & Guo, G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111942 · Cited by 137

Luteolin Inhibits Tumorigenesis and Induces Apoptosis of Non-Small Cell Lung Cancer Cells via Regulation of MicroRNA-34a-5p

Jiang, Z., Li, M., Qin, Y.-M., Jiang, H., Zhang, X., & Wu, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19020447 · Cited by 137

Wild-type p53 suppresses the epithelial-mesenchymal transition and stemness in PC-3 prostate cancer cells by modulating miR-145

Ren, D., WANG, M., Guo, W., Zhao, X., Tu, X.-A., Huang, S., Zou, X., & Peng, X. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1825 · Cited by 136

The regulatory roles of p53 in cardiovascular health and disease

Men, H., Cai, H., Cheng, Q., Zhou, W., Wang, X., Huang, S., Zheng, Y., & Cai, L. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03694-6 · Cited by 137

p53 tetramerization: at the center of the dominant-negative effect of mutant p53Preprint

Gencel‐Augusto, J., & Lozano, G. (2020) · Genes & Development · doi:10.1101/gad.340976.120 · Cited by 136

Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation

Burge, S., Kelly, E., Lonsdale, D., Mutowo, P., McAnulla, C., Mitchell, A., Sangrador‐Vegas, A., Yong, S.-Y., Mulder, N., & Hunter, S. (2012) · Database · doi:10.1093/database/bar068 · Cited by 135

The Role of Polo-like Kinase 1 in Carcinogenesis: Cause or Consequence?

Cholewa, B. D., Liu, X., & Ahmad, N. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-2197 · Cited by 134

Eukaryotic transcription factors: paradigms of protein intrinsic disorder

Staby, L., O’Shea, C., Willemoës, M., Theisen, F. F., Kragelund, B. B., & Skriver, K. (2017) · Biochemical Journal · doi:10.1042/bcj20160631 · Cited by 134

The retinoblastoma protein induces apoptosis directly at the mitochondriaPreprint

Hilgendorf, K. I., Leshchiner, E. S., Nedelcu, S., Maynard, M. A., Calo, E., Ianari, A., Walensky, L. D., & Lees, J. A. (2013) · Genes & Development · doi:10.1101/gad.211326.112 · Cited by 134

Deregulation of cell signaling in cancer

Giancotti, F. G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.02.005 · Cited by 133

New insights into p53 activation

Brooks, C. L., & Gu, W. (2010) · Cell Research · doi:10.1038/cr.2010.53 · Cited by 102

RP–MDM2–p53 Pathway: Linking Ribosomal Biogenesis and Tumor Surveillance

Liu, Y., Deisenroth, C., & Zhang, Y. (2016) · Trends in cancer · doi:10.1016/j.trecan.2016.03.002 · Cited by 133

Molecular Mechanisms of Neonatal Brain Injury

Thornton, C., Rousset, C. I., Kichev, A., Miyakuni, Y., Vontell, R., Baburamani, A. A., Fleiss, B., Gressèns, P., & Hagberg, H. (2012) · Neurology Research International · doi:10.1155/2012/506320 · Cited by 132

Tumor suppressor p53 and its gain-of-function mutants in cancer

Liu, J., Zhang, C., & Feng, Z. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt144 · Cited by 133

TP53 status for prediction of sensitivity to taxane versus non-taxane neoadjuvant chemotherapy in breast cancer (EORTC 10994/BIG 1-00): a randomised phase 3 trial

Bonnefoi, H. R., Piccart, M. J., Bogaerts, J., Mauriac, L., Fumoleau, P., Brain, E. G. C., Petit, T., Rouanet, P., Jassem, J., Blot, E., et al. (2011) · The Lancet Oncology · doi:10.1016/s1470-2045(11)70094-8 · Cited by 131

p21 Both Attenuates and Drives Senescence and Aging in BubR1 Progeroid Mice

Baker, D. J., Weaver, R. L., & van Deursen, J. M. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.028 · Cited by 130

The cytoplasmic side of p53's oncosuppressive activities

Comel, A., Sorrentino, G., Capaci, V., & Sal, G. D. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.04.015 · Cited by 130

The Emerging Roles of Long Noncoding RNA ROR (lincRNA-ROR) and its Possible Mechanisms in Human Cancers

Pan, Y., Li, C., Chen, J., Zhang, K., Chu, X., Wang, R., & Chen, L. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000452539 · Cited by 130

p53: emerging roles in stem cells, development and beyond

Jain, A. K., & Barton, M. C. (2018) · Development · doi:10.1242/dev.158360 · Cited by 130

The p53 pathway in hematopoiesis: lessons from mouse models, implications for humans

Pant, V., Quintás-Cardama, A., & Lozano, G. (2012) · Blood · doi:10.1182/blood-2012-05-356014 · Cited by 129

Oct4 Maintains the Pluripotency of Human Embryonic Stem Cells by Inactivating p53 Through Sirt1-Mediated Deacetylation

Zhang, Z., Chung, S., Xu, Z. Q., & Xu, Y. (2013) · Stem Cells · doi:10.1002/stem.1532 · Cited by 129

p53 regulates the cardiac transcriptome

Mak, T. W., Hauck, L., Grothe, D., & Billia, F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1621436114 · Cited by 129

Heterochromatin silencing of p53 target genes by a small viral protein

Soria, C. T., Estermann, F. E., Espantman, K. C., & O’Shea, C. C. (2010) · Nature · doi:10.1038/nature09307 · Cited by 127

The p53 C Terminus Controls Site-Specific DNA Binding and Promotes Structural Changes within the Central DNA Binding Domain

Laptenko, O., Shiff, I., Freed-Pastor, W. A., Zupnick, A., Mattia, M., Freulich, E., Shamir, I., Kadouri, N., Kahan, T., Manfredi, J. J., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.015 · Cited by 127

Double-Edged Sword of Tumour Suppressor Genes in Schizophrenia

Zhuo, C., Wang, D., Zhou, C., Chen, C., Li, J., Tian, H., Li, S., Ji, F., Liu, C., Chen, M., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00001 · Cited by 127

Lipids as Regulators of Cellular Senescence

Hamsanathan, S., & Gurkar, A. U. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.796850 · Cited by 131

Inhibition of Glycolytic Enzymes Mediated by Pharmacologically Activated p53

Zawacka‐Pankau, J., Grinkevich, V. V., Hünten, S., Nikulenkov, F., Gluch, A., Li, H., Enge, M., Kel, A. E., & Selivanova, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.240812 · Cited by 127

p53 -Dependent and -Independent Nucleolar Stress Responses

Olausson, K. H., Nistér, M., & Lindström, M. S. (2012) · Cells · doi:10.3390/cells1040774 · Cited by 127

Translational repression of p53 by RNPC1, a p53 target overexpressed in lymphomasPreprint

Zhang, J., Cho, S.-J., Shu, L., Yan, W., Guerrero, T. A., Kent, M. S., Skorupski, K. A., Chen, H.-W., & Chen, X. (2011) · Genes & Development · doi:10.1101/gad.2069311 · Cited by 127

Mechanisms of estrogen receptor antagonism toward p53 and its implications in breast cancer therapeutic response and stem cell regulation

Konduri, S. D., Medisetty, R., Liu, W., Kaipparettu, B. A., Srivastava, P., Brauch, H. B., Fritz, P., Swetzig, W. M., Gardner, A. E., Khan, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009575107 · Cited by 126

Inositol Pyrophosphates Mediate the DNA-PK/ATM-p53 Cell Death Pathway by Regulating CK2 Phosphorylation of Tti1/Tel2

Rao, F., Cha, J., Xu, J., Xu, R., Vandiver, M. S., Tyagi, R., Tokhunts, R. A., Koldobskiy, M. A., Fu, C., Barrow, R. K., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.020 · Cited by 126

MicroRNAs in colorectal carcinoma - from pathogenesis to therapy

Chi, Y., & Zhou, D. (2016) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-016-0320-4 · Cited by 126

Repeated PM2.5 exposure inhibits BEAS-2B cell P53 expression through ROS-Akt-DNMT3B pathway-mediated promoter hypermethylation

Zhou, W. J., Tian, D., He, J., Wang, Y., Zhang, L., Cui, L., Li, J., Zhang, L., Li, L., Shu, Y., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7842 · Cited by 126

Mutant p53-R273H gains new function in sustained activation of EGFR signaling via suppressing miR-27a expression

Wang, W., Cheng, B., Miao, L., Mei, Y., & Wu, M. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.97 · Cited by 126

Animal models of colorectal cancer

Johnson, R. L., & Fleet, J. C. (2012) · Cancer and Metastasis Reviews · doi:10.1007/s10555-012-9404-6 · Cited by 125

Alterations of metabolic genes and metabolites in cancer

Oermann, E. K., Wu, J., Guan, K., & Xiong, Y. (2012) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2012.01.013 · Cited by 125

Immunogenic cell death in colon cancer prevention and therapy

Ruan, H., Leibowitz, B. J., Zhang, L., & Yu, J. (2020) · Molecular Carcinogenesis · doi:10.1002/mc.23183 · Cited by 125

Li‐Fraumeni syndrome: a paradigm for the understanding of hereditary cancer predisposition

Valdez, J. M., Nichols, K. E., & Kesserwan, C. A. (2016) · British Journal of Haematology · doi:10.1111/bjh.14461 · Cited by 124

Regulation of cellular senescence via the FOXO 4‐p53 axis

Bourgeois, B. M. R., & Madl, T. (2018) · FEBS Letters · doi:10.1002/1873-3468.13057 · Cited by 124

SIRT6 as a key event linking P53 and NRF2 counteracts APAP-induced hepatotoxicity through inhibiting oxidative stress and promoting hepatocyte proliferation

Zhou, Y., Fan, X., Jiao, T., Li, W., Chen, P., Jiang, Y., Sun, J., Chen, Y., Chen, P., Guan, L., et al. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.06.016 · Cited by 124

p53 as a hub in cellular redox regulation and therapeutic target in cancer

Eriksson, S. E., Ceder, S., Bykov, V. J. N., & Wiman, K. G. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz005 · Cited by 123

Pharmacological activation of p53 triggers anticancer innate immune response through induction of ULBP2

Li, H., Lakshmikanth, T., Garofalo, C., Enge, M., Spinnler, C., Anichini, A., Székely, L., Kärre, K., Carbone, E., & Selivanova, G. (2011) · Cell Cycle · doi:10.4161/cc.10.19.17630 · Cited by 123

Uncoupling p53 Functions in Radiation-Induced Intestinal Damage via PUMA and p21

Leibowitz, B. J., Qiu, W., Liu, H., Cheng, T., Zhang, L., & Yu, J. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0052 · Cited by 123

Regulation of necrotic cell death: p53, PARP1 and cyclophilin D-overlapping pathways of regulated necrosis?

Yuan, Y., & Padanilam, B. J. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2202-5 · Cited by 122

Cytoprotective mechanisms of DJ-1 against oxidative stress through modulating ERK1/2 and ASK1 signal transduction

Oh, S. E., & Mouradian, M. M. (2017) · Redox Biology · doi:10.1016/j.redox.2017.09.008 · Cited by 121

MdmX Protein Is Essential for Mdm2 Protein-mediated p53 Polyubiquitination

Wang, X., Wang, J., & Jiang, X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213868 · Cited by 121

The ribosomal protein S26 regulates p53 activity in response to DNA damage

Cui, D., Li, L., Lou, H., Sun, H., Ngai, S. H. O., Shao, G., & Tang, J. (2013) · Oncogene · doi:10.1038/onc.2013.170 · Cited by 121

p53-dependent repression of polo-like kinase-1 (PLK1)

McKenzie, L., King, S., Marcar, L., Nicol, S., Dias, S. S., Schumm, K., Robertson, P., Bourdon, J., Perkins, N. D., Fuller-Pace, F. V., et al. (2010) · Cell Cycle · doi:10.4161/cc.9.20.13532 · Cited by 120

Potential applications of MEG3 in cancer diagnosis and prognosis

He, Y., Luo, Y., Liang, B., Ye, L., Lu, G., & He, W. (2017) · Oncotarget · doi:10.18632/oncotarget.19931 · Cited by 120

Ribosomal Protein L11 Recruits miR-24/miRISC To Repress c-Myc Expression in Response to Ribosomal Stress

Challagundla, K. B., Sun, X., Zhang, X., DeVine, T., Zhang, Q., Sears, R. C., & Dai, M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05810-11 · Cited by 120

miR-221/222: promising biomarkers for breast cancer

Chen, W., Hu, Q., Qiu, M., Zhong, S., Xu, J., Tang, J., & Zhao, J. (2013) · Tumor Biology · doi:10.1007/s13277-013-0750-y · Cited by 119

Tumor Suppressor miR-22 Determines p53-Dependent Cellular Fate through Post-transcriptional Regulation of p21

Tsuchiya, N., Izumiya, M., Ogata‐Kawata, H., Okamoto, K., Fujiwara, Y., Nakai, M., Okabe, A., Schetter, A. J., Bowman, E. D., Midorikawa, Y., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2475 · Cited by 120

2-Sulfonylpyrimidines: Mild alkylating agents with anticancer activity toward p53-compromised cells

Bauer, M. R., Joerger, A. C., & Fersht, A. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610421113 · Cited by 119

Hesperidin induces apoptosis and triggers autophagic markers through inhibition of Aurora-A mediated phosphoinositide-3-kinase/Akt/mammalian target of rapamycin and glycogen synthase kinase-3 beta signalling cascades in experimental colon carcinogenesis

Gowrikumar, S., Palanivel, C., Manikandan, R., & Sudhandiran, G. (2014) · European Journal of Cancer · doi:10.1016/j.ejca.2014.06.013 · Cited by 118

Safety and Efficacy in Advanced Solid Tumors of a Targeted Nanocomplex Carrying the p53 Gene Used in Combination with Docetaxel: A Phase 1b Study

Pirollo, K. F., Nemunaitis, J. J., Leung, P. K., Nunan, R., Adams, J., & Chang, E. H. (2016) · Molecular Therapy · doi:10.1038/mt.2016.135 · Cited by 118

Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases

Tao, Y., & Conn, P. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00029.2016 · Cited by 118

A Small-Molecule Inhibitor of MDMX Activates p53 and Induces Apoptosis

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Mdm2 and MdmX partner to regulate p53

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