Transcriptional regulation by p53: one protein, many possibilities

Surfing the p53 network

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Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations

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DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2

Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100

Mutant p53 gain of function in two mouse models of Li-Fraumeni syndrome

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DNA damage activates p53 through a phosphorylation–acetylation cascade

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p53 isoforms can regulate p53 transcriptional activity

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Regulation of p53 function and stability by phosphorylation.

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A p53 Amino-Terminal Nuclear Export Signal Inhibited by DNA Damage-Induced Phosphorylation

Zhang, Y., & Xiong, Y. (2001) · Science · doi:10.1126/science.1058637 · Cited by 378

Repression of RNA Polymerase I Transcription by the Tumor Suppressor p53

Zhai, W., & Comai, L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.5930-5938.2000 · Cited by 289

A polymorphic microsatellite that mediates induction of PIG3 by p53

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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

Putting p53 in context

Kastenhuber, E. R., & Lowe, S. W. (2017) · Cell · doi:10.1016/j.cell.2017.08.028 · Cited by 1,906

Modes of p53 regulation.

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How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression

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Regulating the p53 pathway: in vitro hypotheses, in vivo veritas

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Mutant p53 disrupts mammary tissue architecture via the mevalonate pathway

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Transcriptional Regulation by P53

Beckerman, R., & Prives, C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000935 · Cited by 569

Distinct Regulatory Mechanisms and Functions for p53-Activated and p53-Repressed DNA Damage Response Genes in Embryonic Stem Cells

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Direct role of nucleotide metabolism in C-MYC-dependent proliferation of melanoma cells

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Characterization of genome-wide p53-binding sites upon stress response

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E2F7, a novel target, is up-regulated by p53 and mediates DNA damage-dependent transcriptional repression

Carvajal, L. A., Hamard, P.-J., Tonnessen, C., & Manfredi, J. J. (2012) · Genes & Development · doi:10.1101/gad.184911.111 · Cited by 151

Diverse stresses dramatically alter genome-wide p53 binding and transactivation landscape in human cancer cells

Menendez, D., Nguyen, T.-A., Freudenberg, J. M., Mathew, V. J., Anderson, C. W., Jothi, R., & Resnick, M. A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt504 · Cited by 154

Noncanonical DNA Motifs as Transactivation Targets by Wild Type and Mutant p53

Jordan, J. J., Menendez, D., Inga, A., Nourredine, M., Bell, D., & Resnick, M. A. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000104 · Cited by 103

Transcriptional modulation induced by ionizing radiation: p53 remains a central player

Rashi‐Elkeles, S., Elkon, R., Shavit, S., Lerenthal, Y., Linhart, C., Kupershtein, A., Amariglio, N., Rechavi, G., Shamir, R., & Shiloh, Y. (2011) · Molecular Oncology · doi:10.1016/j.molonc.2011.06.004 · Cited by 95

A Gain-of-Function p53-Mutant Oncogene Promotes Cell Fate Plasticity and Myeloid Leukemia through the Pluripotency Factor FOXH1

Loizou, E., Banito, A., Livshits, G., Ho, Y.-J., Koche, R. P., Sánchez-Rivera, F. J., Mayle, A., Chen, C.-C., Kinalis, S., Bagger, F. O., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1391 · Cited by 88

Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase

Okamoto, K., Taya, Y., & Nakagama, H. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.07.021 · Cited by 76

DNA damage-induced cellular senescence is sufficient to suppress tumorigenesis: a mouse model

Van Nguyen, T., Puebla-Osorio, N., Pang, H., Dujka, M. E., & Zhu, C. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062453 · Cited by 72

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

Induction of PPM1D following DNA-damaging treatments through a conserved p53 response element coincides with a shift in the use of transcription initiation sites

Rossi, M., Demidov, O. N., Anderson, C. W., Appella, E., & Mazur, S. J. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn888 · Cited by 57

Insights into regulators of p53 acetylation

Nagasaka, M., Miyajima, C., Aoki, H., Aoyama, M., Morishita, D., Inoue, Y., & Hayashi, H. (2022) · Cells · doi:10.3390/cells11233825 · Cited by 45

Aging: What We Can Learn From Elephants

Chusyd, D. E., Ackermans, N. L., Austad, S. N., Hof, P. R., Mielke, M. M., Sherwood, C. C., & Allison, D. B. (2021) · Frontiers in Aging · doi:10.3389/fragi.2021.726714 · Cited by 23