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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
Cited by
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Items 801–900 of 1,005
Abraham, J., Kelly, J. F., Thibault, P., & Benchimol, S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3415 · Cited by 54
Multiple Signaling Pathways Involving ATMPreprint
Kastan, M., Lim, D., KIM, S.-T., Xu, B., & Canman, C. E. (2000) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2000.65.521 · Cited by 53
Khoo, C. M., Carrasco, D. R., Bosenberg, M. W., Paik, J.-H., & DePinho, R. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700093104 · Cited by 52
p53 gene mutations are uncommon but p53 is commonly expressed in anaplastic large-cell lymphoma
Rassidakis, G. Z., Thomaides, A. X., Wang, S., Jiang, Y., Fourtouna, A., Lai, R., & Medeiros, L. J. (2005) · Leukemia · doi:10.1038/sj.leu.2403840 · Cited by 56
Stathmin regulates mutant p53 stability and transcriptional activity in ovarian cancer
Sonego, M., Schiappacassi, M., Lovisa, S., Dall’Acqua, A., Bagnoli, M., Lovat, F., Libra, M., D’Andrea, S., Canzonieri, V., Militello, L., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201201504 · Cited by 53
Ghosh (2010) · International Journal of Oncology · doi:10.3892/ijo_00000627 · Cited by 52
Imiquimod activates p53-dependent apoptosis in a human basal cell carcinoma cell line
Huang, S., Chang, S.-H., Mu, S.-W., Jiang, H.-Y., Wang, S.-T., Kao, J., Huang, J.-L., Wu, C., Chen, Y., & Shieh, J. (2015) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2015.12.011 · Cited by 53
Sun, Y., Xiao, L., Wang, D., Ji, Y., Yang, Y., Ma, R., & Chen, X. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.3850 · Cited by 52
Deciphering the PTM codes of the tumor suppressor p53
Wen, J., & Wang, D. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab047 · Cited by 55
The vaccinia virus B1R kinase induces p53 downregulation by an Mdm2-dependent mechanism
Santos, C. R., Vega, F. M. D. L., Blanco, S., Barcia, R., & Lazo, P. A. (2004) · Virology · doi:10.1016/j.virol.2004.08.013 · Cited by 52
Umannová, L., Machala, M., Topinka, J., Nováková, Z. V., Milcová, A., Kozubı́k, A., & Vondráček, J. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.02.001 · Cited by 52
Robles, A. I., Wang, X. W., & Harris, C. C. (1999) · Oncogene · doi:10.1038/sj.onc.1202862 · Cited by 52
The N Terminus of p53 Regulates Its Dissociation from DNA
Cain, C. R., Miller, S., Ahn, J., & Prives, C. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002509200 · Cited by 53
Self-citationp73 competes with p53 and attenuates its response in a human ovarian cancer cell line
Vikhanskaya, F. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.2.513 · Cited by 52
Post-translational modifications of p53 tumor suppressor: determinants of its functional targets.
Taira, N., & Yoshida, K. (2012) · PubMed · doi:10.14670/hh-27.437 · Cited by 51
Sarbia, M., Ott, N. L., Pühringer-Oppermann, F., & Brücher, B. L. D. M. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6604037 · Cited by 51
Melnikova, V. O., Santamaria, A. B., Bolshakov, S. V., & Ananthaswamy, H. N. (2003) · Oncogene · doi:10.1038/sj.onc.1206595 · Cited by 52
Modulation of p53 Cellular Function and Cell Death by African Swine Fever Virus
Granja, A. G., Nogal, M. L., Hurtado, C., Salas, J., Salas, M. L., Carrascosa, Á. L., & Revilla, Y. (2004) · Journal of Virology · doi:10.1128/jvi.78.13.7165-7174.2004 · Cited by 52
Angiogenin functionally interacts with p53 and regulates p53-mediated apoptosis and cell survival
Sadagopan, S., Veettil, M. V., Chakraborty, S., Sharma-Walia, N., Paudel, N., Bottero, V., & Chandran, B. (2012) · Oncogene · doi:10.1038/onc.2011.648 · Cited by 53
Functional Cooperation of RKTG with p53 in Tumorigenesis and Epithelial–Mesenchymal Transition
Jiang, Y., Xie, X., Li, Z., Wang, Z., Zhang, Y., Ling, Z., Pan, Y., Wang, Z., & Chen, Y. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-4077 · Cited by 51
Regulation of cytotoxic T-cell responses by p53 in cancer
Braun, M. W., & Iwakuma, T. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.11.76 · Cited by 51
Li, S., Zhao, J., Shang, D., Kass, D. J., & Zhao, Y. (2018) · JCI Insight · doi:10.1172/jci.insight.120362 · Cited by 52
Zhang, S., Yuan, H., Guo, Y., Wang, K., Wang, X., & Guo, Z. (2018) · Chemical Communications · doi:10.1039/c8cc06576d · Cited by 51
Cytolethal distending toxin generates cell death by inducing a bottleneck in the cell cycle
Ceelen, L. M., Decostere, A., Ducatelle, R., & Haesebrouck, F. (2005) · Microbiological Research · doi:10.1016/j.micres.2005.04.002 · Cited by 51
A DNA damage signal is required for p53 to activate gadd45.
Xiao, G., Chicas, A., Olivier, M., Taya, Y., Tyagi, S., Kramer, F. R., & Bargonetti, J. (2000) · PubMed · Cited by 51
Self-citationZhu, H., & Gooderham, N. J. (2006) · Toxicological Sciences · doi:10.1093/toxsci/kfj146 · Cited by 52
Mazière, C., Meignotte, A., Dantin, F., Conte, M.-A., & Mazière, J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3528 · Cited by 51
Hu, W., Ge, Y., Ojcius, D. M., Sun, D. Y., Dong, H., Yang, X., & Yan, J. (2013) · Cellular Microbiology · doi:10.1111/cmi.12141 · Cited by 53
Lou, S., Luo, Y., Cheng, F., Huang, Q., Shen, W., Kleiboeker, S. B., Tisdale, J. F., Liu, Z., & Qiu, J. (2012) · Journal of Virology · doi:10.1128/jvi.01007-12 · Cited by 50
Gamma rays induce a p53-independent mitochondrial biogenesis that is counter-regulated by HIF1α
Bartoletti‐Stella, A., Mariani, E., Kurelac, I., Maresca, A., Caratozzolo, M. F., Iommarini, L., Carelli, V., Eusebi, L. H., Guido, A., Cenacchi, G., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.187 · Cited by 52
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Busso, C. S., Lake, M. W., & Izumi, T. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0487-3 · Cited by 54
Verschuren, E. W., Ban, K. H.-K., Masek, M. A., Lehman, N. L., & Jackson, P. K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00908-07 · Cited by 52
Yung, H. W., Bal‐Price, A., Brown, G. C., & Tolkovsky, A. M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02395.x · Cited by 50
Nakashima, N., Kuwano, K., Maeyama, T., Hagimoto, N., Yoshimi, M., Hamada, N., Yamada, M., & Nakanishi, Y. (2005) · Journal of Clinical Pathology · doi:10.1136/jcp.2004.022632 · Cited by 50
Lee, B. S., Oh, J., Kang, S. K., Park, S., Lee, S., Choi, D., Chung, J. H., Chung, Y. W., & Kang, S.-M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135438 · Cited by 50
Ghosh, C., Nandi, A., & Basu, S. (2019) · Nanoscale · doi:10.1039/c8nr08682f · Cited by 50
Zerbini, L. F., Wang, Y., Correa, R. G., Cho, J., & Libermann, T. A. (2005) · Cell Cycle · doi:10.4161/cc.4.9.1966 · Cited by 50
Regulation of p53 Expression in Response to 5-Fluorouracil in Human Cancer RKO Cells
Ju, J., Schmitz, J. C., Song, B., Kudo, K., & Chu, E. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2890 · Cited by 50
Marsit, C. J., Hasegawa, M., Hirao, T., Kim, D., Aldape, K., Hinds, P. W., Wiencke, J. K., Nelson, H. H., & Kelsey, K. T. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2558 · Cited by 50
Burch, L. R., Scott, M. T., Pöhler, E., Meek, D. W., & Hupp, T. R. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.081 · Cited by 50
Novoselova, E. G., Lunin, S. M., Khrenov, M. O., Parfenyuk, S. B., Novoselova, T. V., Shenkman, B. S., & Fesenko, E. E. (2014) · Immunobiology · doi:10.1016/j.imbio.2014.10.021 · Cited by 52
Sen, N., Kumari, R., Singh, M. I., & Das, S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.003 · Cited by 49
Ye, W., Gong, X., Xie, J., Wu, J., Zhang, X., Ouyang, Q., Zhao, X., Shi, Y., & Zhang, X. (2010) · APOPTOSIS · doi:10.1007/s10495-009-0438-3 · Cited by 49
Nutlins and Ionizing Radiation in Cancer Therapy
Impicciatore, G. G., Sancilio, S., Miscia, S., & Pietro, R. D. (2010) · Current Pharmaceutical Design · doi:10.2174/138161210791033932 · Cited by 50
Eleftheriadis, T., Pissas, G., Antoniadi, G., Spanoulis, A., Liakopoulos, V., & Stefanidis, I. (2014) · International Immunology · doi:10.1093/intimm/dxu077 · Cited by 50
Angelis, P. D. (2011) · International Journal of Oncology · doi:10.3892/ijo.2011.1080 · Cited by 50
Jaiswal, A. S., & Narayan, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101298200 · Cited by 50
Zhan, C., Varney, K. M., Yuan, W., Zhao, L., & Lu, W. (2012) · Journal of the American Chemical Society · doi:10.1021/ja301255n · Cited by 50
Lagranha, C. J., Hirabara, S. M., Curi, R., & Pithon‐Curi, T. C. (2007) · Cell Biochemistry and Function · doi:10.1002/cbf.1421 · Cited by 49
Lyakhovich, A., & Shekhar, M. P. V. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.7.2463-2475.2003 · Cited by 49
Chang, C.-Y., Shen, C.-Y., Kang, C.-K., Sher, Y., Sheu, W. H., Chang, C., & Lee, T. (2014) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2014.06.029 · Cited by 49
IKEO, Y., Sakurai, A., Suzuki, R., Mu-xia, Z., Koizumi, S., Takeuchi, Y., Yumita, W., Nakayama, J., & Hashizume, K. (2000) · Laboratory Investigation · doi:10.1038/labinvest.3780084 · Cited by 49
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Hu, J., Yao, H., Gan, F., Tokarski, A. T., & Wang, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043362 · Cited by 49
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Kodama, M., Otsubo, C., Hirota, T., Yokota, J., Enari, M., & Taya, Y. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00810-09 · Cited by 49
Self-citationPirh2 E3 Ubiquitin Ligase Modulates Keratinocyte Differentiation through p63
Jung, Y.-S., Qian, Y., Yan, W., & Chen, X. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2012.466 · Cited by 48
Li, L., Gu, B., Zhou, F., Chi, J., Wang, F., Peng, G., Xie, F., Qing, J., Feng, D., Lu, S., et al. (2011) · Journal of Virology · doi:10.1128/jvi.02577-10 · Cited by 48
Hsieh, T., Liu, T., Chern, C., Tsao, D., Lu, F., Syu, Y.-H., Hsieh, P.-Y., Hu, H.-S., Chang, T.-T., & Chen, C. (2005) · Food and Chemical Toxicology · doi:10.1016/j.fct.2005.03.002 · Cited by 48
Anderson, C. W., & Appella, E. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00264-3 · Cited by 49
Casein Kinase 1α Regulates an MDMX Intramolecular Interaction To Stimulate p53 Binding
Wu, S., Chen, L., Becker, A., Schönbrunn, E., & Chen, J. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00851-12 · Cited by 48
Namwan, N., Senawong, G., Phaosiri, C., Kumboonma, P., Somsakeesit, L., Samankul, A., Leerat, C., & Senawong, T. (2022) · Molecules · doi:10.3390/molecules27134014 · Cited by 47
Wolfrum, P., Fietz, A., Schnichels, S., & Hurst, J. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.1029473 · Cited by 49
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Oh, S.-M., Liu, Z., Okada, M., Jang, S.-W., Liu, X., Chan, C.-B., Luo, H., & Ye, K.-N. (2009) · Oncogene · doi:10.1038/onc.2009.411 · Cited by 47
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Hong, C., Huang, S. C., Lin, S., Lee, J. J., Chueh, L.-L., Lee, C.-H. K., Lin, J.-H., & Hsiao, M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3341 · Cited by 47
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Deng, Z., Manz, D. H., Torti, S. V., & Torti, F. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7023 · Cited by 47
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Moyer, S. M., Wasylishen, A. R., Qi, Y., Fowlkes, N. W., Su, X., & Lozano, G. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2008474117 · Cited by 47
Delayed reactivation of p53 in the progeny of cells surviving ionizing radiation.
Suzuki, K., Yokoyama, S., Waseda, S., Kodama, S., & Watanabe, M. (2003) · PubMed · Cited by 47
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Ling, H. Y., Zhou, L., Jia, X., Gapter, L. A., Agarwal, R., & Ng, K. (2008) · Molecular Carcinogenesis · doi:10.1002/mc.20487 · Cited by 47
Ohkubo, S., Tanaka, T., Taya, Y., Kitazato, K., & Prives, C. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601388200 · Cited by 47
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Jones, D. L., Thompson, D. A., Suh‐Burgmann, E., Grace, M. R., & Münger, K. (1999) · Virology · doi:10.1006/viro.1999.9733 · Cited by 47
Siddik, Z. H. (2005) · Wiley eBooks · doi:10.1002/0470025077.chap84b · Cited by 50
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Heiber, J. F., & Barber, G. N. (2011) · Journal of Virology · doi:10.1128/jvi.05408-11 · Cited by 48
Gadéa, G., Roger, L., Anguille, C., de Toledo, M., Gire, V., & Roux, P. (2004) · Journal of Cell Science · doi:10.1242/jcs.01566 · Cited by 49
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Wang, F., Chen, S., Jiang, Y., Zhao, Y., Sun, L., Zheng, B., Chen, L., Liu, Z., Zheng, X., Yi, K., et al. (2018) · Mutagenesis · doi:10.1093/mutage/gey023 · Cited by 46
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Shao, J., Lu, J., Zhu, W., Yu, H. T., Jing, X., Wang, Y., Wang, X., & Wang, X. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0293-x · Cited by 49
Ho, C. ‐., Yang, X., Lee, T. ‐., Liao, P., Yang, S. ‐., Tsai, C. ‐., & Chou, M. (2003) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2003.01240.x · Cited by 46
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Lutzker, S. G., Mathew, R., & Taller, D. R. (2001) · Oncogene · doi:10.1038/sj.onc.1204394 · Cited by 46
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Negative control elements of the cell cycle in human tumors
Adams, P. D., & Kaelin, W. G. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80123-3 · Cited by 46
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Lee, J. (2024) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2024.102808 · Cited by 50
Westin, E. R., Aykin‐Burns, N., Buckingham, E. M., Spitz, D. R., Goldman, F. D., & Klingelhutz, A. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3444 · Cited by 45
Oct4 Interaction with Hmgb2 Regulates Akt Signaling and Pluripotency
Campbell, P. A., & Rudnicki, M. A. (2013) · Stem Cells · doi:10.1002/stem.1365 · Cited by 46
Yuan, F., Chen, X., Liu, J., Feng, W., Wu, X., & Chen, S. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1746-3 · Cited by 45
Madan, E., Parker, T. M., Bauer, M. R., Dhiman, A., Pelham, C. J., Nagane, M., Kuppusamy, M. L., Holmes, M., Holmes, T. R., Shaik, K., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000950 · Cited by 45
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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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