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DNA Damage-Induced Phosphorylation of p53 Alleviates Inhibition by MDM2
Open accessAbstract
DNA-damaging agents signal to p53 through as yet unidentified posttranscriptional mechanisms. Here we show that phosphorylation of human p53 at serine 15 occurs after DNA damage and that this leads to reduced interaction of p53 with its negative regulator, the oncoprotein MDM2, in vivo and in vitro. Furthermore, using purified DNA-dependent protein kinase (DNA-PK), we demonstrate that phosphorylation of p53 at serines 15 and 37 impairs the ability of MDM2 to inhibit p53-dependent transactivation. We present evidence that these effects are most likely due to a conformational change induced upon phosphorylation of p53. Our studies provide a plausible mechanism by which the induction of p53 can be modulated by DNA-PK (or other protein kinases with similar specificity) in response to DNA damage.
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In the citing paper
“Doxorubicin treatment of early passage tumor cell lines revealed that five of five early generation mTerc Ink4a / Arf -/ -tumors maintained intact p53 response evidenced by p53 Ser-18 phosphorylation (37, 38) and associated induction of p21 CIP1 .”
From Ink4a / Arf tumor suppressor does not modulate the degenerative conditions or tumor spectrum of the telomerase-deficient mouse (2007) · cites this paper as [37]
In the citing paper
“Induction of double strand breaks in DNA by ionizing radiation or genotoxic chemotherapy leads to the rapid stabilization of p53 through phosphorylation of its N terminus (Shieh et al. 1997; Siliciano et al. 1997”
From p53 Deficiency Rescues the Adverse Effects of Telomere Loss and Cooperates with Telomere Dysfunction to Accelerate Carcinogenesis (1999) · cites this paper as Shieh et al. 1997
In the citing paper
“ATM also activates Chk2, which in turn phosphorylates p53 on serine 20 and inhibits MDM2 binding (Shieh et al, 1997;Banin et al, 1998;Chehab et al, 2000;Shieh et al, 2000).”
From ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage (2005) · cites this paper as Shieh et al, 1997
In the citing paper
“ATM also activates Chk2, which in turn phosphorylates p53 on S20, which is a part of the MDM2-binding site (Shieh et al, 1997(Shieh et al, , 2000;;Banin et al, 1998;Chehab et al, 2000).”
From ATM activates p53 by regulating MDM2 oligomerization and E3 processivity (2009) · cites this paper as Shieh et al, 1997
In the citing paper
“Several landmark studies showed that DNA double strand breaks induce phosphorylation of p53 S15 by DNA-PK and ATM (Mayo et al, 1997;Shieh et al, 1997;Banin et al, 1998;Prives and Hall, 1999).”
From ATM activates p53 by regulating MDM2 oligomerization and E3 processivity (2009) · cites this paper as Shieh et al, 1997
Citations
Cites
p53, the cellular gatekeeper for growth and division
Levine, A. J. (1997) · Cell · doi:10.1016/s0092-8674(00)81871-1 · Cited by 7,693
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
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312
Momand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
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
A Single Ataxia Telangiectasia Gene with a Product Similar to PI-3 Kinase
Savitsky, K., Bar-Shira, A., Gilad, S., Rotman, G., Ziv, Y., Vanagaite, L., Tagle, D. A., Smith, S., Uziel, T., Sfez, S., et al. (1995) · Science · doi:10.1126/science.7792600 · Cited by 2,785
p53: puzzle and paradigm.Preprint
Ko, L. J., & Prives, C. L. (1996) · Genes & Development · doi:10.1101/gad.10.9.1054 · Cited by 2,346
Self-citationStructure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
The p53-mdm-2 autoregulatory feedback loop.
Wu, X., Bayle, J. H., Olson, D., & Levine, A. J. (1993) · Genes & Development · doi:10.1101/gad.7.7a.1126 · Cited by 1,801
Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53
Oliner, J. D., Pietenpol, J. A., Thiagalingam, S., Gyuris, J., Kinzler, K. W., & Vogelstein, B. (1993) · Nature · doi:10.1038/362857a0 · Cited by 1,474
Research works printed but not linked: 3
- Hawley, 1996, Stange bedfellows in even stranger places, Genes Dev., 10, 1383
- Meek, 1994, Posttranslational modification of p53, Semin. Cancer Biol., 5, 203
- Nelson, 1994, DNA strand breaks, Mol. Cell. Biol., 14, 1815
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Negative Control of p53 by Sir2α Promotes Cell Survival under Stress
Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081
Activation of the ATM Kinase by Ionizing Radiation and Phosphorylation of p53
Canman, C. E., Lim, D.-S., Cimprich, K. A., Taya, Y., Tamai, K., Sakaguchi, K., Appella, E., Kastan, M. B., & Siliciano, J. D. (1998) · Science · doi:10.1126/science.281.5383.1677 · Cited by 2,042
Self-citationATM, ATR, and DNA-PK: The Trinity at the Heart of the DNA Damage Response
Blackford, A. N., & Jackson, S. P. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.015 · Cited by 2,050
Kastenhuber, E. R., & Lowe, S. W. (2017) · Cell · doi:10.1016/j.cell.2017.08.028 · Cited by 1,906
Enhanced Phosphorylation of p53 by ATM in Response to DNA Damage
Banin, S., Moyal, L., Shieh, S.-Y., Taya, Y., Anderson, C. W., Chessa, L., Smorodinsky, N. I., Prives, C., Reiss, Y., Shiloh, Y., et al. (1998) · Science · doi:10.1126/science.281.5383.1674 · Cited by 1,797
Self-citationZhang, Y., Xiong, Y., & Yarbrough, W. G. (1998) · Cell · doi:10.1016/s0092-8674(00)81401-4 · Cited by 1,626
AMP-activated protein kinase induces a p53-dependent metabolic checkpoint
Jones, R. G., Plas, D. R., Kubek, S., Buzzai, M., Mu, J., Xu, Y., Birnbaum, M. J., & Thompson, C. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.027 · Cited by 1,619
Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610
A Matter of Life and Cell Death
Evan, G. I., & Littlewood, T. D. (1998) · Science · doi:10.1126/science.281.5381.1317 · Cited by 1,528
Metabolism pathways of arachidonic acids: mechanisms and potential therapeutic targets
Wang, B., Wu, L., Chen, J., Dong, L., Chen, C., Zheng, W., Hu, J., Fleming, I., & Wang, D. W. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00443-w · Cited by 1,538
Fridman, J. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1207116 · Cited by 1,401
How does p53 induce apoptosis and how does this relate to p53-mediated tumour suppression
Aubrey, B. J., Kelly, G. L., Janic, A., Herold, M. J., & Strasser, A. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.169 · Cited by 1,395
Unravelling mechanisms of p53-mediated tumour suppression
Bieging-Rolett, K. T., Mello, S. S., & Attardi, L. D. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3711 · Cited by 1,459
Multiple Ras-dependent phosphorylation pathways regulate Myc protein stabilityPreprint
Sears, R. C., Nuckolls, F., Haura, E. B., Taya, Y., Tamai, K., & Nevins, J. R. (2000) · Genes & Development · doi:10.1101/gad.836800 · Cited by 1,411
Self-citationThe complexity of p53 modulation: emerging patterns from divergent signalsPreprint
Giaccia, A. J., & Kastan, M. B. (1998) · Genes & Development · doi:10.1101/gad.12.19.2973 · Cited by 1,315
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
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Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204
Oda, K., Arakawa, H., Tanaka, T., Matsuda, K., Tanikawa, C., Mori, T., Nishimori, H., Tamai, K., Tokino, T., Nakamura, Y., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00073-8 · Cited by 1,162
Self-citationThe multiple mechanisms that regulate p53 activity and cell fate
Hafner, A., Bulyk, M. L., Jambhekar, A., & Lahav, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0110-x · Cited by 1,129
Role of cell cycle in mediating sensitivity to radiotherapy
Pawlik, T. M., & Keyomarsi, K. (2004) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2004.03.005 · Cited by 1,155
Post‐translational modifications and activation of p53 by genotoxic stresses
Appella, E., & Anderson, C. W. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02225.x · Cited by 1,095
A role for ATR in the DNA damage-induced phosphorylation of p53
Tibbetts, R. S., Brumbaugh, K. M., Williams, J. M., Sarkaria, J. N., Cliby, W. A., Shieh, S.-Y., Taya, Y., Prives, C., & Abraham, R. T. (1999) · Genes & Development · doi:10.1101/gad.13.2.152 · Cited by 1,046
Self-citationMdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53
Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044
(1999) · PubMed · Cited by 1,030
Self-citationDeubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,048
Regulation of p53 in response to DNA damage
Lakin, N. D., & Jackson, S. P. (1999) · Oncogene · doi:10.1038/sj.onc.1203015 · Cited by 987
p53 and Human Cancer: The First Ten Thousand Mutations
Hainaut, P. L., & Hollstein, M. C. (1999) · Advances in cancer research · doi:10.1016/s0065-230x(08)60785-x · Cited by 999
Chin, L., Artandi, S. E., Shen, Q., Tam, A., Lee, S.-L., Gottlieb, G. J., Greider, C. W., & DePinho, R. A. (1999) · Cell · doi:10.1016/s0092-8674(00)80762-x · Cited by 979
Shieh, S.-Y., Ahn, J., Tamai, K., Taya, Y., & Prives, C. (2000) · Genes & Development · doi:10.1101/gad.14.3.289 · Cited by 972
Self-citationNucleolar Arf sequesters Mdm2 and activates p53
Weber, J. D., Taylor, L. J., Roussel, M. F., Sherr, C. J., & Bar-Sagi, D. (1999) · Nature Cell Biology · doi:10.1038/8991 · Cited by 940
Functional and physical interactions of the ARF tumor suppressor with p53 and Mdm2
Kamijo, T., Weber, J. D., Zambetti, G., Zindy, F., Roussel, M. F., & Sherr, C. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.14.8292 · Cited by 899
The DNA-dependent protein kinasePreprint
Smith, G. C. M., & Jackson, S. P. (1999) · Genes & Development · doi:10.1101/gad.13.8.916 · Cited by 903
Takaoka, A., Hayakawa, S., Yanai, H., Stoiber, D., Negishi, H., Kikuchi, H., Sasaki, S., Imai, K., Shibue, T., Honda, K., et al. (2003) · Nature · doi:10.1038/nature01850 · Cited by 847
Regulation of p53 activity through lysine methylation
Chuikov, S., Kurash, J. K., Wilson, J. R., Xiao, B., Justin, N., Ivanov, G. S., McKinney, K. M., Tempst, P., Prives, C. L., Gamblin, S. J., et al. (2004) · Nature · doi:10.1038/nature03117 · Cited by 846
Self-citationDNA damage induces phosphorylation of the amino terminus of p53
Siliciano, J. D., Canman, C. E., Taya, Y., Sakaguchi, K., Appella, E., & Kastan, M. B. (1997) · Genes & Development · doi:10.1101/gad.11.24.3471 · Cited by 818
Self-citationChk2/hCds1 functions as a DNA damage checkpoint in G1by stabilizing p53
Chehab, N. H., Malikzay, A., Appel, M., & Halazonetis, T. D. (2000) · Genes & Development · doi:10.1101/gad.14.3.278 · Cited by 805
Regulation ofp53downstream genes
El‐Deiry, W. S. (1998) · Seminars in Cancer Biology · doi:10.1006/scbi.1998.0097 · Cited by 805
The many substrates and functions of ATM.
Kastan, M. B., & Lim, D.-S. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35043058 · Cited by 779
Moll, U. M., & Petrenko, O. (2003) · PubMed · Cited by 778
p53 Sites Acetylated In Vitro by PCAF and p300 Are Acetylated In Vivo in Response to DNA Damage
Liu, L., Scolnick, D. M., Trievel, R. C., Zhang, H. B., Marmorstein, R., Halazonetis, T. D., & Berger, S. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1202 · Cited by 776
Tumor suppressor p53: Biology, signaling pathways, and therapeutic targeting
Borrero, L. J. H., & El‐Deiry, W. S. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188556 · Cited by 805
Direct Activation of the ATM Protein Kinase by the Mre11/Rad50/Nbs1 Complex
Lee, J.-H., & Paull, T. T. (2004) · Science · doi:10.1126/science.1091496 · Cited by 762
The p53–Mdm2 module and the ubiquitin system
Michael, D., & Oren, M. (2002) · Seminars in Cancer Biology · doi:10.1016/s1044-579x(02)00099-8 · Cited by 772
Stommel, J. M., Marchenko, N. D., Jimenez, G. S., Moll, U. M., Hope, T. J., & Wahl, G. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1660 · Cited by 738
Cytokine Stimulation of Energy Expenditure through p38 MAP Kinase Activation of PPARγ Coactivator-1
Puigserver, P., Rhee, J., Lin, J., Wu, Z., Yoon, J. C., Zhang, C.-Y., Krauss, S., Mootha, V. K., Lowell, B. B., & Spiegelman, B. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00390-2 · Cited by 732
Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
Honda, R., & Yasuda, H. (1999) · The EMBO Journal · doi:10.1093/emboj/18.1.22 · Cited by 724
ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
Maya, R., Balass, M., Kim, S.-T., Shkedy, D., Leal, J.-F. M., Shifman, O., Moas, M., Buschmann, T., Ronai, Z., Shiloh, Y., et al. (2001) · Genes & Development · doi:10.1101/gad.886901 · Cited by 731
“…by ATM on serine 15 (Siliciano et al. 1997; Banin et al. 1998; Canman et al. 1998; Khanna et al. 1998), which may render p53 more resistant to the inhibitory effects of Mdm2 (Shieh et al. 1997), as well as enhance its transcriptional activity (Lambert et al. 1998; Dumaz and Meek 1999).”
BackgroundBarlev, N. A., Liu, L., Chehab, N. H., Mansfield, K., Harris, K. G., Halazonetis, T. D., & Berger, S. L. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00414-2 · Cited by 710
Bulavin, D. V., Saito, S., Hollander, M. C., Sakaguchi, K., Anderson, C. W., Appella, E., & Fornace, A. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.23.6845 · Cited by 716
p53 polymorphisms: cancer implications
Whibley, C., Pharoah, P. D. P., & Hollstein, M. C. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2584 · Cited by 677
Regulation of p53 Translation and Induction after DNA Damage by Ribosomal Protein L26 and Nucleolin
Takagi, M., Absalon, M. J., McLure, K. G., & Kastan, M. B. (2005) · Cell · doi:10.1016/j.cell.2005.07.034 · Cited by 677
MDM2 — master regulator of the p53 tumor suppressor protein
Momand, J., Wu, H.-H., & Dasgupta, G. (2000) · Gene · doi:10.1016/s0378-1119(99)00487-4 · Cited by 641
SUMO‐1 modification activates the transcriptional response of p53
Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Midgley, C., Lane, D. P., & Hay, R. T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6455 · Cited by 639
USP10 Regulates p53 Localization and Stability by Deubiquitinating p53
Yuan, J., Luo, K., Zhang, L., Cheville, J. C., & Lou, Z. (2010) · Cell · doi:10.1016/j.cell.2009.12.032 · Cited by 637
“The phosphorylation of p53 by ATM or Chk2 has been shown to inhibit Mdm2 binding (Banin et al., 1998; Chehab et al., 2000; Shieh et al., 2000; Shieh et al., 1997).”
Mechanisms of Early Brain Injury after Subarachnoid Hemorrhage
Cahill, J., Calvert, J. H., & Zhang, J. H. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600283 · Cited by 634
Prives, C. (1998) · Cell · doi:10.1016/s0092-8674(00)81774-2 · Cited by 623
Self-citationDrug discovery in the ubiquitin–proteasome system
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E1A signaling to p53 involves the p19ARFtumor suppressorPreprint
de Stanchina, E., McCurrach, M. E., Zindy, F., Shieh, S.-Y., Ferbeyre, G., Samuelson, A. V., Prives, C. L., Roussel, M. F., Sherr, C. J., & Lowe, S. W. (1998) · Genes & Development · doi:10.1101/gad.12.15.2434 · Cited by 611
Self-citationTumour suppression by p53: a role for the DNA damage response?
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p53 signaling in cancer progression and therapy
Marei, H. E. S., Thani, A. A. A., Afifi, N. M., Hasan, A., Caceci, T., Pozzoli, G., Morrione, A., Giordano, A., & Cenciarelli, C. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02396-8 · Cited by 628
The casein kinase 1 family: participation in multiple cellular processes in eukaryotes
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The cellular response to p53: the decision between life and death
Sionov, R. V., & Haupt, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1203130 · Cited by 608
Divorcing ARF and p53: an unsettled case
Sherr, C. J. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1954 · Cited by 595
Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2
Hofmann, T. G., Möller, A., Sirma, H., Zentgraf, H., Taya, Y., Dröge, W., Will, H., & Schmitz, M. L. (2001) · Nature Cell Biology · doi:10.1038/ncb715 · Cited by 591
Self-citationPhosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53
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Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage.
Chehab, N. H., Malikzay, A., Stavridi, E. S., & Halazonetis, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13777 · Cited by 583
p300/CBP‐mediated p53 acetylation is commonly induced by p53‐activating agents and inhibited by MDM2
Ito, A., Lai, C.-H., Zhao, X., Saito, S., Hamilton, M. H., Appella, E., & Yao, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1331 · Cited by 597
Generation of oscillations by the p53-Mdm2 feedback loop: A theoretical and experimental study
Bar‐Or, R. L., Maya, R. B.-Y., Segel, L. A., Alon, U., Levine, A. J., & Oren, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.210171597 · Cited by 579
Functions of the MDM2 oncoprotein
Freedman, D. A., Wu, L., & Levine, A. J. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050273 · Cited by 573
MDM2–HDAC1-mediated deacetylation of p53 is required for its degradation
Ito, A., Kawaguchi, Y., Lai, C., Kovacs, J. J., Higashimoto, Y., Appella, E., & Yao, T. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf616 · Cited by 570
Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341
Hideshima, T., Mitsiades, C. S., Akiyama, M., Hayashi, T., Chauhan, D., Richardson, P. G. G., Schlossman, R. L., Podar, K., Munshi, N. C., Mitsiades, N., et al. (2003) · Blood · doi:10.1182/blood-2002-08-2543 · Cited by 570
Regulation of the p53 Tumor Suppressor Protein
Oren, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.51.36031 · Cited by 567
Zhang, Y., Wolf, G. W., Bhat, K., Jin, A., Allio, T., Burkhart, W., & Xiong, Y. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8902-8912.2003 · Cited by 556
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PML is induced by oncogenic ras and promotes premature senescence
Ferbeyre, G., de Stanchina, E., Querido, E., Baptiste, N., Prives, C., & Lowe, S. W. (2000) · Genes & Development · doi:10.1101/gad.14.16.2015 · Cited by 536
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Bernstein, C. (2002) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(02)00009-1 · Cited by 527
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MEKK1/JNK signaling stabilizes and activates p53
Fuchs, S. Y., Adler, V., Pincus, M. R., & Ronai, Z. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10541 · Cited by 521
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twist is a potential oncogene that inhibits apoptosis
Maestro, R., Tos, A. P. D., Hamamori, Y., Krasnokutsky, S., Sartorelli, V., Kedes, L., Doglioni, C., Beach, D. H., & Hannon, G. J. (1999) · Genes & Development · doi:10.1101/gad.13.17.2207 · Cited by 516
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Li, M., Luo, J., Brooks, C. L., & Gu, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200578200 · Cited by 503
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Khanna, K. K., Keating, K. E., Kozlov, S., Scott, S. P., Gatei, M. H., Hobson, K., Taya, Y., Gabrielli, B. G., Chan, D. W., Lees‐Miller, S. P., et al. (1998) · Nature Genetics · doi:10.1038/3882 · Cited by 481
Self-citationReversible centriole depletion with an inhibitor of Polo-like kinase 4
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Dumaz, N., & Meek, D. W. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.7002 · Cited by 455
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Metadata
- Authors
- Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C.
- Affiliations
- Columbia University (US)
- Medical & Biological Laboratories (Japan) (JP)
- National Cancer Center Research Institute (JP)
- Corresponding author
- Prives, Carol
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-10
- Volume
- 91
- Issue
- 3
- Pages
- 325-334
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1978518304
- Cited by
- 2,100
- References
- 73
- Citations by year
- 2026: 15 · 2025: 25 · 2024: 40 · 2023: 53 · 2022: 72 · 2021: 53 · 2020: 49 · 2019: 45 · 2018: 47 · 2017: 72 · 2016: 50 · 2015: 55 · 2014: 74 · 2013: 86 · 2012: 84
- FWCI
- 45.42
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 58316)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- p53, MDM2, DNA damage response, DNA-dependent protein kinase, p53-MDM2 interaction, protein conformational change
- MeSH terms
- Binding Sites, DNA Damage, DNA-Binding Proteins, Humans, Nuclear Proteins, Phosphorylation, Proto-Oncogene Proteins, Serine, Tumor Cells, Cultured, Transcriptional Activation, Down-Regulation, Tumor Suppressor Protein p53, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Proto-Oncogene Proteins c-mdm2, DNA-Activated Protein Kinase
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