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Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
Open accessAbstract
We have demonstrated previously that the oncoprotein Mdm2 has a ubiquitin ligase activity for the tumor suppressor p53 protein. In the present study, we characterize this ubiquitin ligase activity of Mdm2. We first demonstrate the ubiquitination of several p53 point mutants and deletion mutants by Mdm2. The point mutants, which cannot bind to Mdm2, are not ubiquitinated by Mdm2. The ubiquitination of the C-terminal deletion mutants, which contain so-called Mdm2-binding sites, is markedly decreased, compared with that of wild-type p53. The binding of Mdm2 to p53 is essential for ubiquitination, but p53's tertiary structure and/or C-terminal region may also be important for this reaction. DNA-dependent protein kinase is known to phosphorylate p53 on Mdm2-binding sites, where DNA damage induces phosphorylation, and p53 phosphorylated by this kinase is not a good substrate for Mdm2. This suggests that DNA damage-induced phosphorylation stabilizes p53 by inhibiting its ubiquitination by Mdm2. We further investigated whether the tumor suppressor p19(ARF) affects the ubiquitin ligase activity of Mdm2 for p53. The activity of p19(ARF)-bound Mdm2 was found to be lower than that of free Mdm2, suggesting that p19(ARF) promotes the stabilization of p53 by inactivating Mdm2.
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In the citing paper
“the tumor suppressor genes that stabilize p53 (Trp53) via inactivation of Mdm2 in response to a variety of oncogenic stresses (Honda and Yasuda, 1999;Brummelkamp et al., 2002;Lingbeek et al., 2002;Kim and Sharpless, 2006).”
From Tbx3 controls the fate of hepatic progenitor cells in liver development by suppressing p19ARF expression (2008) · cites this paper as Honda and Yasuda, 1999
Experimental — accuracy not yet measuredThe check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Tbx3 is known as a transcriptional repressor for p19 ARF (Cdkn2a -Mouse Genome Informatics) and p14 ARF (the human ortholog of p19 ARF )”
From Tbx3 controls the fate of hepatic progenitor cells in liver development by suppressing p19ARF expression (2008) · cites this paper as Honda and Yasuda, 1999
Experimental — accuracy not yet measuredIn the citing paper
“These data suggested that transfected GFP-Mdm2 is a labile protein that is a target for degradation (20,21) and, furthermore, that PKB phosphorylation is required for protecting Mdm2 from proteasome-dependent destruction, thus increasing Mdm2 stability.”
From Stabilization of Mdm2 via Decreased Ubiquitination Is Mediated by Protein Kinase B/Akt-dependent Phosphorylation (2004) · cites this paper as [20]
In the citing paper
“Mdm2 harbors a self-and p53specific E3 ubiquitin ligase activity within its evolutionarily conserved C-terminal RING finger domain, which mediates p53 ubiquitination and rapid degradation by the 26 S proteasome (20,21).”
From Stabilization of Mdm2 via Decreased Ubiquitination Is Mediated by Protein Kinase B/Akt-dependent Phosphorylation (2004) · cites this paper as [20]
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Cites
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321
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
Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
Toshiyuki, M., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90412-3 · Cited by 4,063
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 · cited 1×
“When Mdm2 cDNA is transfected into human cells, p53 degradation is accelerated (Haupt et al., 1997; Kubbutat et al., 1997).”
BackgroundKastan, 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
The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,416
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
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
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
Cited by
Sorted by citations
Mechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
The p53 pathway: positive and negative feedback loops
Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967
Malignant astrocytic glioma: genetics, biology, and paths to treatment
Furnari, F. B., Fenton, T., Bachoo, R. M., Mukasa, A., Stommel, J. M., Stegh, A., Hahn, W. C., Ligon, K. L., Louis, D. N., Brennan, C., et al. (2007) · Genes & Development · doi:10.1101/gad.1596707 · Cited by 2,316
Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507
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
The Pezcoller lecture: cancer cell cycles revisited.
Sherr, C. J. (2000) · PubMed · Cited by 1,193
RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
Lorick, K. L., Jensen, J. P., Fang, S., Ong, A. M., Hatakeyama, S., & Weissman, A. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11364 · Cited by 1,151
Mdm2 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
The INK4a/ARF network in tumour suppression
Sherr, C. J. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096061 · Cited by 1,001
HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
Zhou, B. P., Liao, Y., Xia, W., Zou, Y., Spohn, B., & Hung, M.-C. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-973 · Cited by 951
Nucleolar 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
Disruption of the ARF-Mdm2-p53 tumor suppressor pathway in Myc-induced lymphomagenesis
Eischen, C. M., Weber, J. D., Roussel, M. F., Sherr, C. J., & Cleveland, J. L. (1999) · Genes & Development · doi:10.1101/gad.13.20.2658 · Cited by 819
Moll, U. M., & Petrenko, O. (2003) · PubMed · Cited by 778
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
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
“The ability of Mdm2 to ubiquinate p53 is negatively regulated by ARF (Pomerantz et al. 1998; Honda and Yasuda 1999; Zhang and Xiong 1999; Fang et al. 2000), suggesting that modifications affecting ARF binding might also modulate Mdm2 function.”
BackgroundInfluentialERK promotes tumorigenesis by inhibiting FOXO3a via MDM2-mediated degradation
Yang, J.-Y., Zong, C. S., Xia, W., Yamaguchi, H., Ding, Q., Xie, X., Lang, J.-Y., Lai, C., Chang, C. J., Huang, W., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1676 · Cited by 720
Sherr, C. J., & Weber, J. D. (2000) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)00038-6 · Cited by 654
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
Regulation of HDM2 activity by the ribosomal protein L11
Lohrum, M. A. E., Ludwig, R. L., Kubbutat, M. H. G., Hanlon, M., & Vousden, K. H. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00134-x · Cited by 626
Tumour suppression by p53: a role for the DNA damage response?
Meek, D. W. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2716 · Cited by 625
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
Update on adenovirus and its vectors
Russell, W. C. (2000) · Journal of General Virology · doi:10.1099/0022-1317-81-11-2573 · Cited by 605
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
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
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
Regulation of the p53 Tumor Suppressor Protein
Oren, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.51.36031 · Cited by 567
Molecular Interaction Map of the Mammalian Cell Cycle Control and DNA Repair Systems
Kohn, K. W. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.8.2703 · Cited by 561
Role of iron in carcinogenesis: cancer as a ferrotoxic disease
Toyokuni, S. (2009) · Cancer Science · doi:10.1111/j.1349-7006.2008.01001.x · Cited by 552
ARF-BP1/Mule Is a Critical Mediator of the ARF Tumor Suppressor
Chen, D., Kon, N., Li, M., Zhang, W., Qin, J., & Gu, W. J. (2005) · Cell · doi:10.1016/j.cell.2005.03.037 · Cited by 551
Ubiquitination: RING for destruction?
Freemont, P. S. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00287-6 · Cited by 522
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
Šulić, S., Panić, L., Barkić, M., Merćep, M., Uzelac, M., & Volarević, S. (2005) · Genes & Development · doi:10.1101/gad.359305 · Cited by 510
Dai, M., Zeng, S. X., Jin, Y., Sun, X., David, L. L., & Lu, H. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.17.7654-7668.2004 · Cited by 495
Myc pathways provoking cell suicide and cancer
Nilsson, J. A., & Cleveland, J. L. (2003) · Oncogene · doi:10.1038/sj.onc.1207261 · Cited by 470
Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage
Khosravi, R., Maya, R., Gottlieb, T., Oren, M., Shiloh, Y., & Shkedy, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14973 · Cited by 461
The role of the E6-p53 interaction in the molecular pathogenesis of HPV
Thomas, M., Pim, D., & Banks, L. (1999) · Oncogene · doi:10.1038/sj.onc.1202953 · Cited by 448
The ubiquitin‐proteasome pathway and proteasome inhibitors
Myung, J., Kim, K. B., & Crews, C. M. (2001) · Medicinal Research Reviews · doi:10.1002/med.1009 · Cited by 453
Itahana, K., Bhat, K., Jin, A., Itahana, Y., Hawke, D. H., Kobayashi, R., & Zhang, Y. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00431-3 · Cited by 431
Bmi1, stem cells, and senescence regulation
Park, I.-K., Morrison, S. J., & Clarke, M. F. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420800 · Cited by 495
The MDM2-p53 pathway revisited
Nag, S. A., Jiangjiang, Q., Kalkunte, S. S., Ming-hai, W., & Zhang, R. (2013) · Journal of Biomedical Research · doi:10.7555/jbr.27.20130030 · Cited by 438
Ashcroft, M. A., & Vousden, K. H. (1999) · Oncogene · doi:10.1038/sj.onc.1203012 · Cited by 411
COP9 signalosome‐specific phosphorylation targets p53 to degradation by the ubiquitin system
Bech‐Otschir, D., Kraft, R., Huang, X., Henklein, P., Kapelari, B., Pollmann, C., & Dubiel, W. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1630 · Cited by 396
Multiple C-Terminal Lysine Residues Target p53 for Ubiquitin-Proteasome-Mediated Degradation
Rodríguez, M. S., Desterro, J. M. P., Laı́n, S., Lane, D. P., & Hay, R. T. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8458-8467.2000 · Cited by 386
Iwakuma, T., & Lozano, G. (2003) · PubMed · Cited by 390
Honda, R., & Yasuda, H. (2000) · Oncogene · doi:10.1038/sj.onc.1203464 · Cited by 376
Self-citationCircumventing tolerance to a human MDM2-derived tumor antigen by TCR gene transfer
Stanislawski, T., Voss, R.-H., Lotz, C., Sadovnikova, E., Willemsen, R. A., Kuball, J. H. E., Ruppert, T., Bolhuis, R. L. H., Melief, C. J. M., Huber, C., et al. (2001) · Nature Immunology · doi:10.1038/ni1001-962 · Cited by 362
The MDM2 RING-finger domain is required to promote p53 nuclear export
Geyer, R. K., Yu, Z. K., & Maki, C. G. (2000) · Nature Cell Biology · doi:10.1038/35023507 · Cited by 361
Opposing Effects of Ras on p53
Ries, S., Biederer, C., Woods, D., Shifman, O., Shirasawa, S., Sasazuki, T., McMahon, M., Oren, M., & McCormick, F. (2000) · Cell · doi:10.1016/s0092-8674(00)00123-9 · Cited by 357
Efp targets 14-3-3σ for proteolysis and promotes breast tumour growth
Urano, T., Saito, T., Tsukui, T., Fujita, M., Hosoi, T., Muramatsu, M., Ouchi, Y., & Inoue, S. (2002) · Nature · doi:10.1038/nature00826 · Cited by 357
A plausible model for the digital response of p53 to DNA damage
Ma, L., Wagner, J., Rice, J. J., Hu, W., Levine, A. J., & Stolovitzky, G. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501352102 · Cited by 351
Stress Signals Utilize Multiple Pathways To Stabilize p53
Ashcroft, M. A., Taya, Y., & Vousden, K. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.9.3224-3233.2000 · Cited by 360
p53-independent functions of the p19ARF tumor suppressorPreprint
Weber, J. D., Jeffers, J. R., Rehg, J. E., Randle, D. H., Lozano, G., Roussel, M. F., Sherr, C. J., & Zambetti, G. P. (2000) · Genes & Development · doi:10.1101/gad.827300 · Cited by 361
Regulation of transcription factor function by phosphorylation
Whitmarsh, A. J., & Davis, R. J. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000757 · Cited by 345
An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
Boyd, S. D., Tsai, K. Y., & Jacks, T. (2000) · Nature Cell Biology · doi:10.1038/35023500 · Cited by 334
MDM2 interacts with MDMX through their RING finger domains
Tanimura, S., Ohtsuka, S., Mitsui, K., Shirouzu, K., Yoshimura, A., & Ohtsubo, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00254-9 · Cited by 324
Cyclin-Dependent Kinase Inhibitors: Useful Targets in Cell Cycle Regulation
Sielecki, T. M., Boylan, J. F., Benfield, P. A., & Trainor, G. L. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990256j · Cited by 322
Clinical Overview of MDM2/X-Targeted Therapies
Burgess, A., Chia, K. M., Haupt, S., Thomas, D., Haupt, Y., & Lim, E. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00007 · Cited by 315
Pattern formation by local self-activation and lateral inhibition
Meinhardt, H., & Gierer, A. (2000) · BioEssays · doi:10.1002/1521-1878(200008)22:8 · Cited by 629
Woods, D. B., & Vousden, K. H. (2001) · Experimental Cell Research · doi:10.1006/excr.2000.5141 · Cited by 323
Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1
Asher, G., Lotem, J., Cohen, B., Sachs, L., & Shaul, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1188 · Cited by 317
Activation and activities of the p53 tumour suppressor protein
Bálint, É., & Vousden, K. H. (2001) · British Journal of Cancer · doi:10.1054/bjoc.2001.2128 · Cited by 315
p53 stabilization is decreased upon NFκB activation
Tergaonkar, V., Pando, M. P., Vafa, O., Wahl, G. M., & Verma, I. M. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00068-5 · Cited by 319
MDM2 is a Central Node in the p53 Pathway: 12 Years and Counting
Bond, G. L., Hu, W., & Levine, A. J. (2005) · Current Cancer Drug Targets · doi:10.2174/1568009053332627 · Cited by 310
de Bie, P., & Ciechanover, A. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.16 · Cited by 296
Sakaguchi, K., Saito, S., Higashimoto, Y., Roy, S., Anderson, C. W., & Appella, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9278 · Cited by 293
Feng, J., Tamaskovic, R., Yang, Z., Brazil, D. P., Merlo, A., Hess, D., & Hemmings, B. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404936200 · Cited by 294
The evolution of diverse biological responses to DNA damage: insights from yeast and p53
Wahl, G. M., & Carr, A. M. (2001) · Nature Cell Biology · doi:10.1038/ncb1201-e277 · Cited by 376
The multiple levels of regulation by p53 ubiquitination
Lee, J. T., & Gu, W. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.77 · Cited by 289
Nucleophosmin (B23) Targets ARF to Nucleoli and Inhibits Its Function
Korgaonkar, C. K., Hagen, J., Tompkins, V. S., Frazier, A. A., Allamargot, C., Quelle, F. W., & Quelle, D. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1258-1271.2005 · Cited by 294
The Origins and Evolution of the p53 Family of GenesPreprint
Белый, В. А., Ak, P., Markert, E. K., Wang, H., Hu, W., Puzio‐Kuter, A. M., & Levine, A. J. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001198 · Cited by 310
Stabilization of the MDM2 Oncoprotein by Interaction with the Structurally Related MDMX Protein
Sharp, D. A., Kratowicz, S. A., Sank, M. J., & George, D. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38189 · Cited by 286
Cell cycle regulation by long non-coding RNAs
Kitagawa, M., Kitagawa, K., Kotake, Y., Niida, H., & Ohhata, T. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1423-0 · Cited by 280
Cooperative Signals Governing ARF-Mdm2 Interaction and Nucleolar Localization of the Complex
Weber, J. D., Kuo, M.-L., Bothner, B. B., DiGiammarino, E. L., Kriwacki, R. W., Roussel, M. F., & Sherr, C. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2517-2528.2000 · Cited by 275
Nucleolar Arf Tumor Suppressor Inhibits Ribosomal RNA Processing
Sugimoto, M., Kuo, M.-L., Roussel, M. F., & Sherr, C. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00057-1 · Cited by 273
Buschmann, T., Fuchs, S. Y., Lee, C.-G., Pan, Z., & Ronai, Z. A. (2000) · Cell · doi:10.1016/s0092-8674(00)80887-9 · Cited by 267
RetractedMyc Requires Distinct E2F Activities to Induce S Phase and Apoptosis
Leone, G. W., Sears, R. C., Huang, E. S., Rempel, R. E., Nuckolls, F., Park, C., Giangrande, P. H., Wu, L., Saavedra, H. I., Field, S. J., et al. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00275-1 · Cited by 265
Rayburn, E., Zhang, R., He, J., & Wang, H. (2005) · Current Cancer Drug Targets · doi:10.2174/1568009053332636 · Cited by 265
U-box proteins as a new family of ubiquitin ligases
Hatakeyama, S., & Nakayama, K. I. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00245-6 · Cited by 270
MDM2 interaction with nuclear corepressor KAP1 contributes to p53 inactivation
Wang, C., Ivanov, A. V., Chen, L., Fredericks, W. J., Seto, E., Rauscher, F. J., & Chen, J. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600791 · Cited by 263
Stabilization of p53 by p14ARF without relocation of MDM2 to the nucleolus
Llanos, S., Clark, P. A., Rowe, J., & Peters, G. G. (2001) · Nature Cell Biology · doi:10.1038/35074506 · Cited by 252
Toward a Molecular Classification of Melanoma
Fecher, L. A., Cummings, S. D., Keefe, M. J., & Alani, R. M. (2007) · Journal of Clinical Oncology · doi:10.1200/jco.2006.06.0442 · Cited by 255
Midgley, C., Desterro, J. M. P., Saville, M. K., Howard, S. F., Sparks, A., Hay, R. T., & Lane, D. P. (2000) · Oncogene · doi:10.1038/sj.onc.1203593 · Cited by 250
Development of novel targeted therapies in the treatment of malignant glioma
Rich, J. N., & Bigner, D. D. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1380 · Cited by 250
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Metadata
- Authors
- Honda, R., & Yasuda, H.
- Affiliations
- Tokyo University of Pharmacy and Life Sciences (JP)
- Corresponding author
- Yasuda, Hideyo
- Venue
- The EMBO Journal
- Published
- 1999-01-04
- Volume
- 18
- Issue
- 1
- Pages
- 22-27
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1171098
- OpenAlex
- W2028210102
- Cited by
- 724
- References
- 43
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 12 · 2022: 12 · 2021: 3 · 2020: 10 · 2019: 4 · 2018: 11 · 2017: 5 · 2016: 14 · 2015: 19 · 2014: 20 · 2013: 24 · 2012: 20
- FWCI
- 33.88
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Molecular Biology Organization
- Institute of Genetics
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- p19ARF, MDM2, p53, ubiquitin ligase activity, p53 ubiquitination, p53 stabilization, DNA-dependent protein kinase, p53 phosphorylation, DNA damage response, tumor suppressor proteins, protein-protein interaction
- MeSH terms
- Animals, Cell Line, Cloning, Molecular, DNA-Binding Proteins, HeLa Cells, Humans, Ligases, Mutation, Nuclear Proteins, Phosphorylation, Proteins, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Ubiquitins, Tumor Suppressor Protein p53, Protein Serine-Threonine Kinases, Spodoptera, Tumor Suppressor Protein p14ARF, Ubiquitin-Protein Ligases, Proto-Oncogene Proteins c-mdm2, DNA-Activated Protein Kinase, In Vitro Techniques
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