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 201–300 of 1,005
Regulation of p53 localization
Liang, S., & Clarke, M. F. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02227.x · Cited by 224
Relevance of the p53–MDM2 axis to aging
Wu, D., & Prives, C. (2018) · Cell Death & Differentiation · doi:10.1038/cdd.2017.187 · Cited by 215
Self-citationHall-Jackson, C. A., Cross, D. A. E., MORRICE, N. A., & Smythe, C. (1999) · Oncogene · doi:10.1038/sj.onc.1203077 · Cited by 214
Skeletal muscle gene expression profiles in 20–29 year old and 65–71 year old women
Welle, S., Brooks, A. I., Delehanty, J. M., Needler, N., Bhatt, K., Shah, B., & Thornton, C. A. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2003.11.011 · Cited by 210
Functional activation of p53 via phosphorylation following DNA damage by UV but not γ radiation
Kapoor, M., & Lozano, G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2834 · Cited by 209
Mitochondrial and Cell Death Mechanisms in Neurodegenerative Diseases
Martin, L. J. (2010) · Pharmaceuticals · doi:10.3390/ph3040839 · Cited by 213
The role of p53 in hypoxia-induced apoptosis
Hammond, E. M., & Giaccia, A. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.154 · Cited by 213
The importance of p53 location: nuclear or cytoplasmic zip code?
O’Brate, A., & Giannakakou, P. (2003) · Drug Resistance Updates · doi:10.1016/j.drup.2003.10.004 · Cited by 214
Martin, L. J. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31816ff780 · Cited by 213
MDM2 promotes p21waf1/cip1 proteasomal turnover independently of ubiquitylation
Jin, Y., Lee, H., Zeng, S. X., Dai, M., & Lu, H. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg600 · Cited by 206
DNA Damage Caused by Metal Nanoparticles: Involvement of Oxidative Stress and Activation of ATM
Wan, R., Mo, Y., Feng, L., Chien, S., Tollerud, D. J., & Zhang, Q. (2012) · Chemical Research in Toxicology · doi:10.1021/tx200513t · Cited by 209
Chk2 Activation Dependence on Nbs1 after DNA Damage
Buscemi, G., Savio, C., Zannini, L., Miccichè, F., Masnada, D., Nakanishi, M., Tauchi, H., Komatsu, K., Mizutani, S., Khanna, K., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.15.5214-5222.2001 · Cited by 201
Olsson, A., Manzl, C., Strasser, A., & Villunger, A. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402196 · Cited by 204
Tyrosine phosphorylation of Mdm2 by c‐Abl: implications for p53 regulation
Goldberg, Z., Sionov, R. V., Berger, M., Zwang, Y., Perets, R., Etten, R. A. V., Oren, M., Taya, Y., & Haupt, Y. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf384 · Cited by 200
Self-citationp53 Signaling and Cell Cycle Checkpoints
Stewart, Z. A., & Pietenpol, J. A. (2001) · Chemical Research in Toxicology · doi:10.1021/tx000199t · Cited by 204
Thomas, M. C., & Chiang, C. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.016 · Cited by 198
Nakamura, S., Roth, J. A., & Mukhopadhyay, T. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9391-9398.2000 · Cited by 198
Cancer Risk and the ATM Gene: a Continuing Debate
Khanna, K. K. (2000) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/92.10.795 · Cited by 200
Ou, Y.-H., Chung, P.-H., Sun, T.-P., & Shieh, S.-Y. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0689 · Cited by 211
Self-citationAlternative and aberrant splicing of MDM2 mRNA in human cancer
Bartel, F., Taubert, H. W., & Harris, L. C. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00091-0 · Cited by 196
The nucleolus: the magician’s hat for cell cycle tricks
Visintin, R., & Amon, A. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00102-2 · Cited by 196
Stark, G. R., & Taylor, W. R. (2004) · Humana Press eBooks · doi:10.1385/1-59259-788-2:051 · Cited by 203
Regulation of Mdm2-Directed Degradation by the C Terminus of p53
Kubbutat, M. H. G., Ludwig, R. L., Ashcroft, M. A., & Vousden, K. H. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.10.5690 · Cited by 193
Kobet, E., Zeng, X., Zhu, Y., Keller, D., & Lu, H. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.23.12547 · Cited by 193
Juven‐Gershon, T., & Oren, M. (1999) · Molecular Medicine · doi:10.1007/bf03402141 · Cited by 193
Webley, K., Bond, J. A., Jones, C. J., Blaydes, J. P., Craig, A., Hupp, T., & Wynford-Thomas, D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2803-2808.2000 · Cited by 192
Escrivà, M., Peiró, S., Herranz, N., Villagrasa, P., Dave, N., Montserrat-Sentís, B., Murray, S. A., Francı́, C., Gridley, T., Virtanen, I., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02061-07 · Cited by 190
Mutations in serines 15 and 20 of human p53 impair its apoptotic activity
Unger, T., Sionov, R. V., Moallem, E., Yee, C., Howley, P. M., Oren, M., & Haupt, Y. (1999) · Oncogene · doi:10.1038/sj.onc.1202656 · Cited by 190
Comparative study of the p53-mdm2 and p53-MDMX interfaces
Böttger, V., Böttger, A., Garcia-Echeverria, C., Ramos, Y. F., van der Eb, A. J., Jochemsen, A. G., & Lane, D. P. (1999) · Oncogene · doi:10.1038/sj.onc.1202281 · Cited by 189
DNA-PK as an Emerging Therapeutic Target in Cancer
Mohiuddin, I. S., & Kang, M. H. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00635 · Cited by 188
Hyperosmolality in the form of elevated NaCl but not urea causes DNA damage in murine kidney cells
Kültz, D., & Chakravarty, D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1999 · Cited by 190
Liu, Y. (2001) · Carcinogenesis · doi:10.1093/carcin/22.6.851 · Cited by 187
DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53
Nagashima, M., Shiseki, M., Miura, K., Hagiwara, K., Linke, S. P., Pedeux, R., Wang, X. W., Yokota, J., Riabowol, K. T., & Harris, C. C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161151798 · Cited by 183
Adachi, M., & Brenner, D. A. (2008) · Hepatology · doi:10.1002/hep.21991 · Cited by 188
Quaternary structures of tumor suppressor p53 and a specific p53–DNA complex
Tidow, H., Melero, R., Mylonas, E., Freund, S. M. V., Großmann, J., Carazo, J. M., Svergun, D. I., Valle, M., & Fersht, A. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705069104 · Cited by 185
Maintenance of genomic integrity by p53: complementary roles for activated and non-activated p53
Albrechtsen, N., Dornreiter, I., Große, F., Kim, E. L., Wiesmüller, L., & Deppert, W. (1999) · Oncogene · doi:10.1038/sj.onc.1202952 · Cited by 183
Regulation of p53 stability and activity in response to genotoxic stress
Colman, M. S., Afshari, C. A., & Barrett, J. C. (2000) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(00)00035-1 · Cited by 182
Inhibition of MDM2 by hsp90 Contributes to Mutant p53 Stabilization
Peng, Y., Chen, L., Li, C., Lu, W., & Chen, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102817200 · Cited by 180
Kinetics of p53 Binding to Promoter Sites In Vivo
Szak, S. T., Mays, D. J., & Pietenpol, J. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3375-3386.2001 · Cited by 178
hMutSα- and hMutLα-dependent phosphorylation of p53 in response to DNA methylator damage
Duckett, D. R., Bronstein, S. M., Taya, Y., & Modrich, P. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12384 · Cited by 178
Self-citationThe ATM protein is required for sustained activation of NF-κB following DNA damage
Piret, B., Schoonbroodt, S., & Piette, J. (1999) · Oncogene · doi:10.1038/sj.onc.1202541 · Cited by 176
Jimenez, G. S., Khan, S. H., Stommel, J. M., & Wahl, G. M. (1999) · Oncogene · doi:10.1038/sj.onc.1203013 · Cited by 177
Radiation-Induced Senescence-like Growth Arrest Requires TP53 Function but not Telomere Shortening
Suzuki, K., Mori, I., Nakayama, Y., Miyakoda, M., Kodama, S., & Watanabe, M. (2001) · Radiation Research · doi:10.1667/0033-7587(2001)155[0248:rislga]2.0.co;2 · Cited by 177
Fraser, M. E., Bai, T., & Tsang, B. K. (2007) · International Journal of Cancer · doi:10.1002/ijc.23086 · Cited by 180
DNA Damage Response in Plants: Conserved and Variable Response Compared to Animals
Yoshiyama, K., Sakaguchi, K., & Kimura, S. (2013) · Biology · doi:10.3390/biology2041338 · Cited by 182
p53 Down-Regulates CHK1 through p21 and the Retinoblastoma Protein
Gottifredi, V., Karni-Schmidt, O., Shieh, S.-Y., & Prives, C. L. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.4.1066-1076.2001 · Cited by 174
Self-citationCandidate protein biodosimeters of human exposure to ionizing radiation
Marchetti, F., Coleman, M. A., Jones, I. M., & Wyrobek, A. J. (2006) · International Journal of Radiation Biology · doi:10.1080/09553000600930103 · Cited by 176
The role of p53 in neuronal cell death
Morrison, R. S., & Kinoshita, Y. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400741 · Cited by 175
Corbière, C., Liagre, B., Terro, F., & Beneytout, J. (2004) · Cell Research · doi:10.1038/sj.cr.7290219 · Cited by 172
Blagosklonny, M. V. (2000) · The FASEB Journal · doi:10.1096/fj.99-1078rev · Cited by 170
Genotoxic and non-genotoxic pathways of p53 induction
Pluquet, O., & Hainaut, P. L. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00698-x · Cited by 177
Stress-Dependent Nucleolin Mobilization Mediated by p53-Nucleolin Complex Formation
Daniely, Y., Dimitrova, D. D., & Borowiec, J. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.6014-6022.2002 · Cited by 174
The role of ubiquitin modification in the regulation of p53
Hock, A. K., & Vousden, K. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.022 · Cited by 168
Gajjar, M. K., Candeias, M. M., Malbert-Colas, L., Mazars, A., Fujita, J., Olivares‐Illana, V., & Fåhræus, R. (2012) · Cancer Cell · doi:10.1016/j.ccr.2011.11.016 · Cited by 177
Roy, A. M., Baliga, M. S., & Katiyar, S. K. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.81.4.1 · Cited by 168
Phosphorylation of murine p53 at Ser-18 regulates the p53 responses to DNA damage
Chao, C., Saito, S., Anderson, C. W., Appella, E., & Xu, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220252297 · Cited by 168
ATM activates p53 by regulating MDM2 oligomerization and E3 processivity
Cheng, Q., Chen, L., Li, Z., Lane, W. S., & Chen, J. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.294 · Cited by 165
The role of DNA damage responses in p53 biology
Speidel, D. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1459-z · Cited by 172
Reactive Oxygen Species Induced p53 Activation: DNA Damage, Redox Signaling, or Both?
Shi, T., & Dansen, T. B. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8074 · Cited by 173
Apoptosis in amyotrophic lateral sclerosis: a review of the evidence
Sathasivam, S., Ince, P. G., & Shaw, P. J. (2001) · Neuropathology and Applied Neurobiology · doi:10.1046/j.0305-1846.2001.00332.x · Cited by 172
Redox signalling and transition metals in the control of the p53 pathway
Méplan, C., Richard, M., & Hainaut, P. L. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00297-x · Cited by 164
Shukla, S., & Gupta, S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.02.007 · Cited by 163
The 400 kDa Subunit of the PCAF Histone Acetylase Complex Belongs to the ATM Superfamily
Vassilev, A. P., Yamauchi, J., Kotani, T., Prives, C. L., Avantaggiati, M. L., Qin, J., & Nakatani, Y. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80301-9 · Cited by 164
Self-citationEischen, C. M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026096 · Cited by 161
CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53
Shi, D., Pop, M. S., Kulikov, R., Love, I. M., Kung, A. L., & Grossman, S. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904305106 · Cited by 165
p53 at the crossroad of DNA replication and ribosome biogenesis stress pathways
Lindström, M. S., Bártek, J., & Maya‐Mendoza, A. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00999-w · Cited by 177
Identification of a Novel Protein Kinase Mediating Akt Survival Signaling to the ATM Protein
Suzuki, A., Kusakai, G.-I., Kishimoto, A., Lu, J., Ogura, T., Lavin, M. F., & Esumi, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206025200 · Cited by 161
Sankala, H. M., Hait, N. C., Paugh, S. W., Shida, D., Lépine, S., Elmore, L. W., Dent, P., Milstien, S., & Spiegel, S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2090 · Cited by 166
Effect of zinc oxide nanomaterials-induced oxidative stress on the p53 pathway
Setyawati, M. I., Tay, C. Y., & Leong, D. T. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.09.024 · Cited by 158
López-Borges, S., & Lazo, P. A. (2000) · Oncogene · doi:10.1038/sj.onc.1203709 · Cited by 158
Pifithrin-α protects against doxorubicin-induced apoptosis and acute cardiotoxicity in mice
Liu, X., Chua, C. C., Gao, J., Chen, Z., Landy, C., Hamdy, R. C., & Chua, B. H. L. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00759.2003 · Cited by 162
Ronen, A., & Glickman, B. W. (2001) · Environmental and Molecular Mutagenesis · doi:10.1002/em.1033 · Cited by 161
Role of Type 2C Protein Phosphatases in Growth Regulation and in Cellular Stress Signaling
Lammers, T., & Lavi, S. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701693342 · Cited by 165
Lee, Y., Kuo, H., Chu, C.-Y., Wang, C., Lin, W.-C., & Tseng, T. (2003) · Biochemical Pharmacology · doi:10.1016/j.bcp.2003.07.014 · Cited by 159
Mingo-Sion, A. M., Marietta, P. M., Koller, E., Wolf, D. M., & Berg, C. L. V. D. (2004) · Oncogene · doi:10.1038/sj.onc.1207147 · Cited by 156
Havrilesky, L. J., Darcy, K. M., Hamdan, H. B., Priore, R. L., Leon, J., Bell, J., & Berchuck, A. (2003) · Journal of Clinical Oncology · doi:10.1200/jco.2003.11.052 · Cited by 156
Life and death decisions: regulation of apoptosis by proteolysis of signaling molecules
Utz, P. J., & Anderson, P. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400696 · Cited by 155
Therapeutics targeting p53-MDM2 interaction to induce cancer cell death
Koo, N., Sharma, A. K., & Narayan, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095005 · Cited by 153
Hsp90 Chaperones Wild-type p53 Tumor Suppressor Protein
Walerych, D., Kudla, G., Gutkowska, M., Wawrzynów, B., Muller, L., King, F. W., Helwak, A., Boros, J., Żylicz, M., & Żylicz, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407601200 · Cited by 154
Zinc-finger protein-targeted gene regulation: Genomewide single-gene specificity
Tan, S., Guschin, D. Y., Davalos, A. R., Lee, Y.-L., Snowden, A. W., Jouvenot, Y., Zhang, H. S., Howes, K., McNamara, A. R., Lai, A., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2035056100 · Cited by 154
Su, F., Overholtzer, M., Besser, D., & Levine, A. J. (2002) · Genes & Development · doi:10.1101/gad.942902 · Cited by 153
Phosphorylation of Serine 18 Regulates Distinct p53 Functions in Mice
Sluss, H. K., Armata, H., Gallant, J., & Jones, S. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.976-984.2004 · Cited by 152
Sabirzhanov, B. E., Zhao, Z., Stoica, B. A., Loane, D. J., Wu, J., Borroto, C., Dorsey, S. G., & Faden, A. I. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1260-14.2014 · Cited by 152
Harms, K. L., & Chen, X. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4397 · Cited by 156
Tumor suppressor p53: regulation and function
Somasundaram, K. (2000) · Frontiers in bioscience · doi:10.2741/somasund · Cited by 155
DNA damage induced p53 stabilization: no indication for an involvement of p53 phosphorylation
Blattner, C., Tobiasch, E., Litfen, M., Rahmsdorf, H. J., & Herrlich, P. (1999) · Oncogene · doi:10.1038/sj.onc.1202480 · Cited by 151
A DNA damage and stress inducible G protein-coupled receptor blocks cells in G 2 /M
Weng, Z., Fluckiger, A.-C., Nisitani, S., Wahl, M. I., Le, L. Q., Hunter, C. A., Fernal, A. A., Beau, M. M. L., & Witte, O. N. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12334 · Cited by 151
Structural Details on mdm2-p53 Interaction
Chi, S., Lee, S., Kim, D., Ahn, M.-J., Js, K., Woo, J.-Y., Torizawa, T., Kainosho, M., & Han, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508578200 · Cited by 152
Another fork in the road—life or death decisions by the tumour suppressor p53
Carvajal, L. A., & Manfredi, J. J. (2013) · The EMBO Reports · doi:10.1038/embor.2013.25 · Cited by 149
E2F1 Uses the ATM Signaling Pathway to Induce p53 and Chk2 Phosphorylation and Apoptosis
Powers, J. T., Hong, S., Mayhew, C. N., Rogers, P. M., Knudsen, E. S., & Johnson, D. G. (2004) · Molecular Cancer Research · doi:10.1158/1541-7786.203.2.4 · Cited by 152
The dual role model for p53 in maintaining genomic integrity
Janus, F., Albrechtsen, N. J. W., Dornreiter, I., Wiesmüller, L., Große, F., & Deppert, W. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050266 · Cited by 154
p53 accumulates but is functionally impaired when DNA synthesis is blocked
Gottifredi, V., Shieh, S.-Y., Taya, Y., & Prives, C. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1036 · Cited by 147
Self-citationThe C terminus of p53 binds the N-terminal domain of MDM2
Poyurovsky, M. V., Katz, C., Laptenko, O., Beckerman, R., Lokshin, M., Ahn, J., Byeon, I. L., Gabizon, R., Mattia, M., Zupnick, A., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1872 · Cited by 153
Self-citationRate of environmental change determines stress response specificity
Young, J. W., Locke, J. C. W., & Elowitz, M. B. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1213060110 · Cited by 150
Strategies for manipulating the p53 pathway in the treatment of human cancer
Hupp, T. R., Lane, D. P., & Ball, K. L. (2000) · Biochemical Journal · doi:10.1042/bj3520001 · Cited by 148
5-Aza-2′-deoxycytidine Activates the p53/p21Waf1/Cip1 Pathway to Inhibit Cell Proliferation
Zhu, W., Hileman, T., Ke, Y., Wang, P., Lu, S., Duan, W., Dai, Z., Tong, T., Villalona-Calero, M. A., Plass, C., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311703200 · Cited by 148
Breaking Bad: How Viruses Subvert the Cell Cycle
Fan, Y., Sanyal, S., & Bruzzone, R. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00396 · Cited by 150
Zhang, H.-Y., Han, Q.-W., Xu, Y.-F., Fan, Y.-R., Dai, Q.-M., Zhu, H.-W., Rong, Z.-G., Wang, J.-J., & Xu, G.-X. (2005) · Cancer Biology & Therapy · doi:10.4161/cbt.4.2.1442 · Cited by 147
HIF‐1‐dependent transcriptional activity is required for oxygen‐mediated HIF‐1α degradation
Berra, E., Richard, D. E., Gothié, E., & Pouysségur, J. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02159-7 · Cited by 147
Craig, A. L., Burch, L. R., VOJTESEK, B., MIKUTOWSKA, J., Thompson, A. M., & Hupp, T. R. (1999) · Biochemical Journal · doi:10.1042/bj3420133 · Cited by 146
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
