Cited by 3,192

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

Vousden, Karen H., Lu, Xin·2002·Nature Reviews Cancer

DOI 10.1038/nrc864

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Surfing the p53 network
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“Although far from complete, these examples illustrate that many of the genes that are induced by p53 can be divided into groups that might mediate a specific p53 function, such as inhibition of cell growth, DNA repair, activation of apoptosis or regulation of angiogenesi”
Background
Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis
Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
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Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
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“cgi?l=4194">MDMX (MDM4) — have crucial roles in regulating p53 activity to allow normal growth and developmen”
Background
A Chemical Inhibitor of p53 That Protects Mice from the Side Effects of Cancer Therapy
Komarov, P. G., Komarova, E. A., Kondratov, R. V., Christov-Tselkov, K., Coon, J. S., Chernov, M. V., & Gudkov, A. V. (1999) · Science · doi:10.1126/science.285.5434.1733 · Cited by 1,270
DNA damage activates p53 through a phosphorylation–acetylation cascade
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Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067
A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage
Tanaka, H., Arakawa, H., Yamaguchi, T., Shiraishi, K., Fukuda, S., Matsui, K., Takei, Y., & Nakamura, Y. (2000) · Nature · doi:10.1038/35003506 · Cited by 904
ASPP Proteins Specifically Stimulate the Apoptotic Function of p53
Samuels-Lev, Y., O'Connor, D. J., Bergamaschi, D., Trigiante, G., Hsieh, J.-K., Zhong, S., Campargue, I., Naumovski, L., Crook, T., & Lu, X. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00367-7 · Cited by 664
Mechanisms of p53-dependent apoptosis
Schuler, M., & Green, D. R. (2001) · Biochemical Society Transactions · doi:10.1042/bst0290684 · Cited by 641

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Items 101–141 of 141

Core domain interactions in full-length p53 in solution
Veprintsev, D. B., Freund, S. M. V., Andreeva, A., Rutledge, S. E., Tidow, H., Cañadillas, J. M. P., Blair, C. M., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511130103 · Cited by 95
Tumor suppressor protein (p)53, is a regulator of NF-κB repression by the glucocorticoid receptor
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USP15-dependent lysosomal pathway controls p53-R175H turnover in ovarian cancer cells
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Mdm2–p53 signaling regulates epidermal stem cell senescence and premature aging phenotypes in mouse skin
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MDM2 Antagonist Nutlin-3 Displays Antiproliferative and Proapoptotic Activity in Mantle Cell Lymphoma
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The biological impact of the human master regulator p53 can be altered by mutations that change the spectrum and expression of its target genes
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Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ)
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Increased Radioresistance and Accelerated B Cell Lymphomas in Mice with Mdmx Mutations that Prevent Modifications by DNA-Damage-Activated Kinases
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p53 Regulates the Ras circuit to inhibit the expression of a cancer-related gene signature by various molecular pathways
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Mdmx enhances p53 ubiquitination by altering the substrate preference of the Mdm2 ubiquitin ligase
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Tumor Suppressor Protein Pdcd4 Inhibits Translation of p53 mRNA
Wedeken, L., Singh, P., & Klempnauer, K.-H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.269456 · Cited by 75
Watching the watcher: Regulation of p53 by mitochondria
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Redox-Dependent Translocation of p53 to Mitochondria or Nucleus in Human Melanocytes after UVA- and UVB-Induced Apoptosis
Wäster, P. K., & Öllinger, K. M. (2009) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.421 · Cited by 72
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De novo N-palmitoylsphingosine synthesis is the major biochemical mechanism of ceramide accumulation following p53 up-regulation
Panjarian, S., Kozhaya, L., Arayssi, S., Yehia, M., Bielawski, J., Bielawska, A., Usta, J., Hannun, Y. A., Obeid, L. M., & Dbaibo, G. S. (2008) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2008.02.004 · Cited by 69
DNA-dependent protein kinase catalytic subunit mediates T-cell loss in rheumatoid arthritis.
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p53 pathway is involved in cell competition during mouse embryogenesis
Zhang, G., Xie, Y., Zhou, Y., Xiang, C., Chen, L., Zhang, C., Hou, X., Chen, J., Zong, H., & Liu, G. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617414114 · Cited by 69
PRIMA-1MET inhibits growth of mouse tumors carrying mutant p53.
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Transient ATM Kinase Inhibition Disrupts DNA Damage–Induced Sister Chromatid Exchange
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ATM and MET kinases are synthetic lethal with nongenotoxic activation of p53
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Distinct roles of Mdm2 and Mdm4 in red cell production
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p21 does not protect cancer cells from apoptosis induced by nongenotoxic p53 activation
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Molecular epidemiology of adrenocortical tumors in southern Brazil
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Identification and Characterization of the Cytoplasmic Protein TRAF4 as a p53-regulated Proapoptotic Gene
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Protein Kinase CK1δ Phosphorylates Key Sites in the Acidic Domain of Murine Double-Minute Clone 2 Protein (MDM2) That Regulate p53 Turnover
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Authors: Vousden, K. H., & Lu, X.
Venue: Nature Reviews Cancer
Publisher: Springer Science and Business Media LLC
Published: 2002-08-01
Volume: 2
Issue: 8
Pages: 594-604
ISSN: 1474-175X (ISSN-L)
1474-1768
DOI: 10.1038/nrc864
OpenAlex: W2063669247
Cited by: 3,192
References: 16
FWCI: 7.49
Type: journal article
Language: en
Open access: closed

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

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