The DOI matches its Crossref record; 63 of the 73 references it cites were found in a registry or an index.
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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
Sorted by citations
Items 601–700 of 1,005
Phosphorylation and hsp90 Binding Mediate Heat Shock Stabilization of p53
Wang, C., & Chen, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206697200 · Cited by 75
Homologous Recombination and Its Role in Carcinogenesis
Bishop, A. J. R., & Schiestl, R. H. (2002) · BioMed Research International · doi:10.1155/s1110724302204052 · Cited by 77
Kiyoshima, T., Enoki, N., Kobayashi, I., Sakai, T., Nagata, K., WADA, H., Fujiwara, H., Ookuma, Y., & Sakai, H. (2012) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2012.1102 · Cited by 78
Pecháčková, S., Burdová, K., Benada, J., Kleiblová, P., Jeníková, G., & Macůrek, L. (2016) · Oncotarget · doi:10.18632/oncotarget.7363 · Cited by 76
Activation of p53 Function in Carcinoma Cells by the α6β4 Integrin
Bachelder, R. E., Marchetti, A., Falcioni, R., Soddu, S., & Mercurio, A. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20733 · Cited by 75
Keller, D., Zeng, X., Li, X., Kapoor, M., Iordanov, M. S., Taya, Y., Lozano, G., Magun, B. E., & Lu, H. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1023 · Cited by 75
Self-citationDohoney, K. M., Guillerm, C., Whiteford, C. C., Elbi, C., Lambert, P. F., Hager, G. L., & Brady, J. N. (2004) · Oncogene · doi:10.1038/sj.onc.1207005 · Cited by 77
Homologous recombination as a mechanism of carcinogenesis
Bishop, A. J. R., & Schiestl, R. H. (2001) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(01)00018-x · Cited by 76
Mechanisms of Cr(VI)-induced p53 activation: the role of phosphorylation, mdm2 and ERK
Wang, S. (2001) · Carcinogenesis · doi:10.1093/carcin/22.5.757 · Cited by 75
Atm deficiency causes an increased frequency of intrachromosomal homologous recombination in mice.
Bishop, A. J. R., Barlow, C., Wynshaw-Boris, A. J., & Schiestl, R. H. (2000) · PubMed · Cited by 75
Dumaz, N., Milne, D., Jardine, L., & Meek, D. W. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590459 · Cited by 75
DNA end-independent activation of DNA-PK mediated via association with the DNA-binding protein C1DPreprint
Yavuzer, U., Smith, G. C. M., Bliss, T. M., Werner, D., & Jackson, S. P. (1998) · Genes & Development · doi:10.1101/gad.12.14.2188 · Cited by 75
Alkhalaf, M. (2007) · Pharmacology · doi:10.1159/000103253 · Cited by 74
Mutant TP53 Posttranslational Modifications: Challenges and Opportunities
Nguyen, T., Menéndez, D., Resnick, M. A., & Anderson, C. W. (2014) · Human Mutation · doi:10.1002/humu.22506 · Cited by 77
A TPR Motif Cofactor Contributes to p300 Activity in the p53 Response
Demonacos, C., Krstic–Demonacos, M., & Thangue, N. B. L. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00277-5 · Cited by 76
The p53 tumor suppressor: Critical regulator of life & death in cancer
Fisher, D. E. (2001) · APOPTOSIS · doi:10.1023/a:1009659708549 · Cited by 74
Biasoli, D., Kahn, S. A., Cornélio, T. A., Furtado, M. B., Campanati, L., Chneiweiss, H., Moura‐Neto, V., & Borges, H. L. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.283 · Cited by 74
RNA content in the nucleolus alters p53 acetylation via MYBBP1A
Kuroda, T., Murayama, A., Katagiri, N., Ohta, Y., Fujita, E., Masumoto, H., Ema, M., Takahashi, S., Kimura, K., & Yanagisawa, J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.23 · Cited by 77
Regulation of MDM2 E3 Ligase Activity by Phosphorylation after DNA Damage
Cheng, Q., Cross, B. L., Li, B., Chen, L., Li, Z., & Chen, J. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05553-11 · Cited by 78
USP4 inhibits p53 and NF-κB through deubiquitinating and stabilizing HDAC2
Li, Z., Hao, Q., Luo, J., Xiong, J., Zhang, S., Wang, W., Bai, L., Wang, W., Chen, M., Wang, W., et al. (2015) · Oncogene · doi:10.1038/onc.2015.349 · Cited by 73
Aberrant ubiquitin-mediatedproteolysis of cell cycle regulatory proteins and oncogenesis
Bashir, T., & Pagano, M. (2003) · Advances in cancer research · doi:10.1016/s0065-230x(03)88305-7 · Cited by 73
Role of MAP kinases in UVB-induced phosphorylation of p53 at serine 20
She, Q., Ma, W., & Dong, Z. (2002) · Oncogene · doi:10.1038/sj.onc.1205239 · Cited by 73
Ubiquitous Induction of p53 in Tumor Cells by Antisense Inhibition of MDM2 Expression
Chen, L., Lu, W., Agrawal, S., Zhou, W., Zhang, R., & Chen, J. (1999) · Molecular Medicine · doi:10.1007/bf03402136 · Cited by 73
DNA-dependent Protein Kinase-independent Activation of p53 in Response to DNA Damage
Burma, S., Kurimasa, A., Xie, G., Taya, Y., Araki, R., Abe, M., Crissman, H. A., Ouyang, H., Li, G. C., & Chen, D. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.17139 · Cited by 73
Self-citationInvolvement of Protein Kinase Cε (PKCε) in Thyroid Cell Death
Knauf, J. A., Elisei, R., Mochly‐Rosen, D., Liron, T., Chen, X., Gonsky, R., Korenberg, J. R., & Fagin, J. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23414 · Cited by 73
Revisiting DNA damage repair, p53-mediated apoptosis and cisplatin sensitivity in germ cell tumors
Cavallo, F., Feldman, D. R., & Barchi, M. (2013) · The International Journal of Developmental Biology · doi:10.1387/ijdb.130135mb · Cited by 72
Kim, H. S., Hwang, J. T., Yun, H., Chi, S., Lee, S., Kang, I., Yoon, K., Choe, W.-J., Kim, S. S., & Ha, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704432200 · Cited by 72
RetractedHuh, J., Kang, K., Chae, C., Kim, H., Ahn, K.-S., & Kim, S. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2003.12.025 · Cited by 72
Castillo, J., Frame, F. M., Rogoff, H. A., Pickering, M., Yurochko, A. D., & Kowalik, T. F. (2005) · Journal of Virology · doi:10.1128/jvi.79.17.11467-11475.2005 · Cited by 72
HIF-transcribed p53 chaperones HIF-1α
Madan, E., Parker, T. M., Pelham, C. J., Palma, A. M., Peixoto, M. L., Nagane, M., Chandaria, A., Tomás, A. R., Canas‐Marques, R., Henriques, V., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz766 · Cited by 74
Martin, L. J., Price, A. C., McClendon, K. B., Al‐Abdulla, N. A., Subramaniam, J. R., Wong, P. C., & Liu, Z. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01659.x · Cited by 72
du Toit-Kohn, J.-L., Louw, L., & Engelbrecht, A. (2008) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2007.12.005 · Cited by 72
Melanoma Cells Express Elevated Levels of Phosphorylated Histone H2AX Foci
Warters, R. L., Adamson, P. J., Pond, C. D., & Leachman, S. A. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23674.x · Cited by 77
Stefano, V. D., Soddu, S., Sacchi, A., & D’Orazi, G. (2005) · Oncogene · doi:10.1038/sj.onc.1208717 · Cited by 73
Cytoplasmically “Sequestered” Wild Type p53 Protein Is Resistant to Mdm2-mediated Degradation
Zaika, A. I., Marchenko, N. D., & Moll, U. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.39.27474 · Cited by 72
Wu, H., THOMAS, J. A., & Momand, J. A. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510087 · Cited by 72
p53 Superfamily Proteins in Marine Bivalve Cancer and Stress Biology
Walker, C. W., Beneden, R. J. V., Muttray, A. F., Böttger, S. A., Kelley, M. L., Tucker, A. E., & Thomas, W. K. (2011) · Advances in marine biology · doi:10.1016/b978-0-12-385536-7.00001-7 · Cited by 72
Apoptosis in Parkinson's disease: Is p53 the missing link between genetic and sporadic Parkinsonism?
da Costa, C. A., & Checler, F. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.10.020 · Cited by 75
Mechanistic differences in the transcriptional activation of p53 by 14-3-3 isoforms
Rajagopalan, S., Sade, R. S., Townsley, F. M., & Fersht, A. R. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1041 · Cited by 72
The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A
Luciani, M. G., Hutchins, J. R. A., Zheleva, D. I., & Hupp, T. R. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3830 · Cited by 72
DNA damage, p14ARF, Nucleophosmin (NPM/B23), and cancer
Gjerset, R. A. (2006) · Journal of Molecular Histology · doi:10.1007/s10735-006-9040-y · Cited by 71
Shono, T., Tofilon, P. J., Schaefer, T. S., Parikh, D., Liu, T.-J., & Lang, F. F. (2002) · PubMed · Cited by 71
Autoregulatory control of the p53 response by caspase‐mediated processing of HIPK2
Gresko, E., Roscic, A., Ritterhoff, S., Vichalkovski, A., Sal, G. D., & Schmitz, M. L. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601077 · Cited by 71
p76MDM2 Inhibits the Ability of p90MDM2to Destabilize p53
Perry, M. E., Mendrysa, S. M., Saucedo, L. J., Tannous, P., & Holubar, M. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5733 · Cited by 71
ARF Differentially Modulates Apoptosis Induced by E2F1 and Myc
Russell, J. L., Powers, J. T., Rounbehler, R. J., Rogers, P. M., Conti, C. J., & Johnson, D. G. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1360-1368.2002 · Cited by 72
Requirement of clathrin heavy chain for p53-mediated transcriptionPreprint
Enari, M., Ohmori, K., Kitabayashi, I., & Taya, Y. (2006) · Genes & Development · doi:10.1101/gad.1381906 · Cited by 71
Self-citationRegulation of the Mdm2-p53 signaling axis in the DNA damage response and tumorigenesis
Carr, M. I., & Jones, S. N. (2016) · Translational Cancer Research · doi:10.21037/tcr.2016.11.75 · Cited by 71
ATM&A Key Determinant of Multiple Cellular Responses to Irradiation
Kastan, D.-S. L. M. B. (2001) · Acta Oncologica · doi:10.1080/02841860152619089 · Cited by 70
Tang, H.-Y. J., Zhao, K., Pizzolato, J. F., Fonarev, M., Langer, J., & Manfredi, J. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.44.29156 · Cited by 70
ATR Mutation in Endometrioid Endometrial Cancer Is Associated With Poor Clinical Outcomes
Zighelboim, I., Schmidt, A. P., Gao, F., Thaker, P. H., Powell, M. A., Rader, J. S., Gibb, R. K., Mutch, D. G., & Goodfellow, P. J. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2008.19.9802 · Cited by 69
Kim, T.-S., Kawaguchi, M., Suzuki, M., Jung, C., Asai, K., Shibamoto, Y., Lavin, M. F., Khanna, K. K., & Miura, Y. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.004689 · Cited by 73
Altaf, M., Monim-ul-Mehboob, M., Kawde, A.-N. M., Corona, G., Larcher, R., Ogasawara, M. A., Casagrande, N., Celegato, M., Borghese, C., Siddik, Z. H., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.13448 · Cited by 69
p53 isoforms regulate premature aging in human cells
von Muhlinen, N., Horikawa, I., Alam, F., Isogaya, K., Lissa, D., Vojtesek, B., Lane, D. P., & Harris, C. C. (2018) · Oncogene · doi:10.1038/s41388-017-0101-3 · Cited by 70
Seavey, S. E., Holubar, M. K., Saucedo, L. J., & Perry, M. E. (1999) · Journal of Virology · doi:10.1128/jvi.73.9.7590-7598.1999 · Cited by 69
Ataxia-telangiectasia: chronic activation of damage-responsive functions is reduced by α-lipoic acid
Gatei, M., Shkedy, D., Khanna, K. K., Uziel, T., Shiloh, Y., Pandita, T. K., Lavin, M. F., & Rotman, G. (2001) · Oncogene · doi:10.1038/sj.onc.1204111 · Cited by 68
It’s Getting Complicated—A Fresh Look at p53-MDM2-ARF Triangle in Tumorigenesis and Cancer Therapy
Kung, C.-P., & Weber, J. D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.818744 · Cited by 71
Role of inflammation and oxidative stress in chemotherapy-induced neurotoxicity
Gupta, P., Makkar, T. K., Goel, L., & Pahuja, M. (2022) · Immunologic Research · doi:10.1007/s12026-022-09307-7 · Cited by 71
D’Andrea, F. P., Safwat, A., Kassem, M. S., Gautier, L., Overgaard, J., & Horsman, M. R. (2011) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2011.05.086 · Cited by 69
Synergistic Apoptosis-Inducing Effects on A375 Human Melanoma Cells of Natural Borneol and Curcumin
Chen, J., Li, L., Su, J., Li, B., Chen, T., & Wong, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101277 · Cited by 68
Ichwan, S. J. A., Yamada, S., Sumrejkanchanakij, P., Auerkari, E. I., Eto, K., & Ikeda, M.-A. (2005) · Oncogene · doi:10.1038/sj.onc.1209158 · Cited by 68
Self-citationChromosomal breakage syndromes
Carney, J. P. (1999) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)80074-0 · Cited by 68
Pyrrolidine Dithiocarbamate Prevents p53 Activation and Promotes p53 Cysteine Residue Oxidation
Wu, H., & Momand, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18898 · Cited by 68
Posttranslational Modifications Affect the Interaction of S100 Proteins with Tumor Suppressor p53
van Dieck, J., Teufel, D. P., Jaulent, A. M., Fernández-Fernández, M. R., Rutherford, T. J., Wysłouch‐Cieszyńska, A., & Fersht, A. R. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.10.002 · Cited by 68
Dangerous habits of a security guard: the two faces of p53 as a drug target
Gudkov, A. V., & Komarova, E. A. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm052 · Cited by 67
Stravopodis (2009) · International Journal of Oncology · doi:10.3892/ijo_00000353 · Cited by 67
Ionizing radiation enhances matrix metalloproteinase-2 production in human lung epithelial cells
Araya, J., Maruyama, M., Sassa, K., Fujita, T., Hayashi, R., Matsui, S., Kashii, T., Yamashita, N., Sugiyama, E., & Kobayashi, M. (2001) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2001.280.1.l30 · Cited by 67
Guzman, R. E., Solter, P. F., & Runnegar, M. T. C. (2003) · Toxicon · doi:10.1016/s0041-0101(03)00030-8 · Cited by 67
(2000) · PubMed · Cited by 67
Targeting mutant p53: a key player in breast cancer pathogenesis and beyond
Qayoom, H., Haq, B. U., Sofi, S., Jan, N., Jan, A., & Mir, M. A. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01863-9 · Cited by 68
Wallace, N. A., & Galloway, D. A. (2014) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2013.12.003 · Cited by 68
Muthná, D., Soukup, T., Vávrová, J., Mokrý, J., Ćmielová, J., Víšek, B., Mrkvicová, A., Havelek, R., Suchánek, J., Filip, S., et al. (2010) · Stem Cells and Development · doi:10.1089/scd.2009.0449 · Cited by 66
Lee, H. J., Choi, B. H., Min, B., & Park, S. R. (2007) · Tissue Engineering · doi:10.1089/ten.2006.0346 · Cited by 66
Heat shock factor-1 modulates p53 activity in the transcriptional response to DNA damage
Logan, I. R., McNeill, H. V., Cook, S., Lü, X., Meek, D. W., Fuller-Pace, F. V., Lunec, J., & Robson, C. N. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp180 · Cited by 68
Cooperative actions of p21WAF1 and p53 induce Slug protein degradation and suppress cell invasion
Kim, J., Bae, S., An, S., Park, J. K., Kim, E. M., Hwang, S., Kim, W., & Um, H. (2014) · EMBO Reports · doi:10.15252/embr.201438587 · Cited by 66
HIPK2 neutralizes MDM2 inhibition rescuing p53 transcriptional activity and apoptotic function
Stefano, V. D., Blandino, G., Sacchi, A., Soddu, S., & D’Orazi, G. (2004) · Oncogene · doi:10.1038/sj.onc.1207656 · Cited by 67
Wible, B. A., Wang, L., Kuryshev, Y. A., Basu, A., Haldar, S., & Brown, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201689200 · Cited by 66
Activation of an MDM2-specific Caspase by p53 in the Absence of Apoptosis
Pochampally, R. R., Fodera, B., Chen, L., Lu, W., & Chen, J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.15271 · Cited by 66
Stewart, Z. A., Tang, L. J., & Pietenpol, J. A. (2001) · Oncogene · doi:10.1038/sj.onc.1204060 · Cited by 68
Role of p53 circuitry in tumorigenesis: A brief review
Niazi, S., Purohit, M., & Niazi, J. H. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.08.099 · Cited by 65
DNA-PKcs: A Targetable Protumorigenic Protein Kinase
Dylgjeri, E., & Knudsen, K. E. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-1756 · Cited by 69
Tanel, A., & Averill‐Bates, D. A. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.10.014 · Cited by 65
Peng, L., Yuan, Z., Li, Y., Ling, H., Izumi, V., Fang, B., Fukasawa, K., Koomen, J. M., Chen, J., & Seto, E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.612796 · Cited by 69
PDCD5 interacts with p53 and functions as a positive regulator in the p53 pathway
Xu, L., Hu, J., Zhao, Y., Hu, J. N., Xiao, J., Wang, Y., Ma, D., & Chen, Y. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0754-x · Cited by 65
C/EBPα Is a DNA Damage-Inducible p53-Regulated Mediator of the G 1 Checkpoint in Keratinocytes
Yoon, K., & Smart, R. C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10650-10660.2004 · Cited by 65
Frank, S. K., Menezes, S., Lebreton, C., Oster, M., Dubertret, L., & Coulomb, B. (2005) · Experimental Dermatology · doi:10.1111/j.1600-0625.2005.00397.x · Cited by 65
Fogarty, M. P., Downer, E. J., & Campbell, V. A. (2003) · Biochemical Journal · doi:10.1042/bj20021660 · Cited by 66
Reagan-Shaw, S., Breur, J., & Ahmad, N. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0250 · Cited by 64
Wu, Y., Zhang, C., Xiong, J., Cai, D., Wang, C.-Z., Wang, Y., Liu, Y., Wang, Y., Li, Y., Wu, J. H., et al. (2023) · Cell Research · doi:10.1038/s41422-023-00874-4 · Cited by 68
Huang, X., Choi, J.-K., Park, S. R., Ha, Y. S., Park, H., Yoon, S. H., Park, H. C., Park, J. O., & Choi, B. H. (2007) · Neuroscience Research · doi:10.1016/j.neures.2007.01.015 · Cited by 64
Ali, A., Abedini, M. R., & Tsang, B. K. (2011) · Oncogene · doi:10.1038/onc.2011.399 · Cited by 64
Verma, S. K., Ali, A., Arora, S., & Banerjea, A. C. (2011) · Blood · doi:10.1182/blood-2011-01-333427 · Cited by 64
Feedbacks, Bifurcations, and Cell Fate Decision-Making in the p53 System
Hat, B., Kochańczyk, M., Bogdał, M. N., & Tomasz Lipniacki, B. (2016) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004787 · Cited by 65
Purohit, N. K., Shah, R. G., Adant, S., Hoepfner, M., Shah, G. M., & Beauregard, J. (2018) · Oncotarget · doi:10.18632/oncotarget.25266 · Cited by 67
Liu, X., Kirschenbaum, A. M., Kang, Y., Shen, Y., & Levine, A. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406577200 · Cited by 64
Specific pattern of p53 phosphorylation during nitric oxide-induced cell cycle arrest
Nakaya, N., Lowe, S. W., Taya, Y., Chenchik, A. A., & Enikolopov, G. (2000) · Oncogene · doi:10.1038/sj.onc.1204100 · Cited by 64
Self-citationChromosome translocations in sarcomas and the emergence of oncogenic transcription factors
Xia, S. J., & Barr, F. G. (2005) · European Journal of Cancer · doi:10.1016/j.ejca.2005.08.003 · Cited by 65
Identification of a Sequence Element from p53 That Signals for Mdm2-Targeted Degradation
Gu, J., Chen, D., Lichtenstein, J. H. R., Rubin, R. M., & Yuan, Z.-M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.4.1243-1253.2000 · Cited by 64
Cell cycle‐dependent nuclear retention of p53 by E2F1 requires phosphorylation of p53 at Ser315
Fogal, V., Hsieh, J.-K., Royer, C., Zhong, S., & Lü, X. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600735 · Cited by 64
Thermodynamics of p53 Binding to hdm2(1–126): Effects of Phosphorylation and p53 Peptide Length
Lai, Z., Auger, K. R., Manubay, C. M., & Copeland, R. A. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1998 · Cited by 66
A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model.
Becker, K., Marchenko, N., Palacios, G., & Moll, U. M. (2008) · Cell Cycle · doi:10.4161/cc.7.9.5756 · Cited by 63
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
