The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Live or let die: the cell's response to p53
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“Although far from complete, these examples illustrate that many of the genes that are induced by p53 can be divided into groups that might mediate a specific p53 function, such as inhibition of cell growth, DNA repair, activation of apoptosis or regulation of angiogenesi”
BackgroundNoxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis
Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420
Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · cited 1×
“cgi?l=4194">MDMX (MDM4) — have crucial roles in regulating p53 activity to allow normal growth and developmen”
BackgroundA Chemical Inhibitor of p53 That Protects Mice from the Side Effects of Cancer Therapy
Komarov, P. G., Komarova, E. A., Kondratov, R. V., Christov-Tselkov, K., Coon, J. S., Chernov, M. V., & Gudkov, A. V. (1999) · Science · doi:10.1126/science.285.5434.1733 · Cited by 1,270
DNA damage activates p53 through a phosphorylation–acetylation cascade
Sakaguchi, K., Herrera, J. E., Saito, S., Miki, T., Bustin, M., Vassilev, A., Anderson, C. W., & Appella, E. (1998) · Genes & Development · doi:10.1101/gad.12.18.2831 · Cited by 1,204
Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067
A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage
Tanaka, H., Arakawa, H., Yamaguchi, T., Shiraishi, K., Fukuda, S., Matsui, K., Takei, Y., & Nakamura, Y. (2000) · Nature · doi:10.1038/35003506 · Cited by 904
ASPP Proteins Specifically Stimulate the Apoptotic Function of p53
Samuels-Lev, Y., O'Connor, D. J., Bergamaschi, D., Trigiante, G., Hsieh, J.-K., Zhong, S., Campargue, I., Naumovski, L., Crook, T., & Lu, X. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00367-7 · Cited by 664
Mechanisms of p53-dependent apoptosis
Schuler, M., & Green, D. R. (2001) · Biochemical Society Transactions · doi:10.1042/bst0290684 · Cited by 641
Cited by
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Integrating cell-signalling pathways with NF-κB and IKK function
Perkins, N. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2083 · Cited by 2,350
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
TIGAR, a p53-Inducible Regulator of Glycolysis and Apoptosis
Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C., Nakano, K., Bartrons, R., Gottlieb, E., & Vousden, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.05.036 · Cited by 2,019
Self-citationFridman, J. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1207116 · Cited by 1,401
p53- and Drug-Induced Apoptotic Responses Mediated by BH3-Only Proteins Puma and Noxa
Villunger, A., Michalak, E. M., Coultas, L., Müllauer, F., Böck, G., Ausserlechner, M. J., Adams, J. M., & Strasser, A. (2003) · Science · doi:10.1126/science.1090072 · Cited by 1,327
Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286
mCSM: Predicting the effects of mutations in proteins using graph-based signatures
Pires, D. E. V., Ascher, D. B., & Blundell, T. L. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btt691 · Cited by 1,066
Serine and one-carbon metabolism in cancer
Yang, M., & Vousden, K. H. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.81 · Cited by 992
Self-citationLu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891
De Bosscher, K., Vanden Berghe, W., & Haegeman, G. (2003) · Endocrine Reviews · doi:10.1210/er.2002-0006 · Cited by 898
Molecular mechanisms of fluoride toxicity
Barbier, O., Arreola-Mendoza, L., & Del Razo, L. M. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.07.011 · Cited by 878
Takaoka, A., Hayakawa, S., Yanai, H., Stoiber, D., Negishi, H., Kikuchi, H., Sasaki, S., Imai, K., Shibue, T., Honda, K., et al. (2003) · Nature · doi:10.1038/nature01850 · Cited by 847
Inhibiting the p53–MDM2 interaction: an important target for cancer therapy
Chène, P. (2003) · Nature Reviews Cancer · doi:10.1038/nrc991 · Cited by 765
Acetylation of the p53 DNA-binding domain regulates apoptosis induction.
Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.026 · Cited by 752
Life in the balance: how BH3-only proteins induce apoptosis
Willis, S. N., & Adams, J. M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.10.001 · Cited by 743
Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy
Tovar, C., Rosinski, J., Filipovic, Z., Higgins, B., Kolinsky, K., Hilton, H., Zhao, X., Vu, B. T., Qing, W., Packman, K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507493103 · Cited by 708
Ding, K., Lu, Y., Nikolovska-Coleska, Z., Wang, G., Qiu, S., Shangary, S., Gao, W., Qin, D., Stuckey, J., Krajewski, K., et al. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm051122a · Cited by 702
Shangary, S., Qin, D., McEachern, D., Liu, M., Miller, R. S., Qiu, S., Nikolovska-Coleska, Z., Ding, K., Wang, G., Chen, J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708917105 · Cited by 660
Role of p53 in Cell Death and Human Cancers
Ozaki, T., & Nakagawara, A. (2011) · Cancers · doi:10.3390/cancers3010994 · Cited by 650
Shangary, S., & Wang, S. (2009) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.48.113006.094723 · Cited by 623
Modeling the Therapeutic Efficacy of p53 Restoration in Tumors
Martins, C. P., Brown-Swigart, L., & Evan, G. I. (2006) · Cell · doi:10.1016/j.cell.2006.12.007 · Cited by 600
The casein kinase 1 family: participation in multiple cellular processes in eukaryotes
Knippschild, U., Gocht, A., Wolff, S., Huber, N., Löhler, J., & Stöter, M. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2004.12.011 · Cited by 601
PRIMA-1 reactivates mutant p53 by covalent binding to the core domain
Lambert, J. M. R., Gorzov, P., Veprintsev, D. B., Söderqvist, M., Segerbäck, D., Bergman, J., Fersht, A. R., Hainaut, P., Wiman, K. G., & Bykov, V. J. N. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.03.003 · Cited by 592
Signaling to p53: ribosomal proteins find their way
Zhang, Y., & Lu, H. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.024 · Cited by 591
The expanding universe of p53 targets
Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568
eRNAs Are Required for p53-Dependent Enhancer Activity and Gene Transcription
Melo, C. A., Drost, J., Wijchers, P. J., van de Werken, H., de Wit, E., Vrielink, J. A. F. O., Elkon, R., Melo, S. A., Léveillé, N., Kalluri, R., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.021 · Cited by 544
MDM2 inhibitors for cancer therapy
Vassilev, L. T. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.11.002 · Cited by 532
Proliferation of aneuploid human cells is limited by a p53-dependent mechanism
Thompson, S. L., & Compton, D. A. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200905057 · Cited by 494
p53 and E2f: partners in life and death
Polager, S., & Ginsberg, D. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2718 · Cited by 498
Sirtuins: critical regulators at the crossroads between cancer and aging
Saunders, L. R., & Verdin, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210616 · Cited by 489
Transcription-independent pro-apoptotic functions of p53
Moll, U. M., Wolff, S., Speidel, D., & Deppert, W. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.09.007 · Cited by 468
Zhao, Y., Aguilar, A., Bernard, D., & Wang, S. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501092z · Cited by 462
Kenzelmann Broz, D., Spano Mello, S., Bieging, K. T., Jiang, D., Dusek, R. L., Brady, C. A., Sidow, A., & Attardi, L. D. (2013) · Genes & Development · doi:10.1101/gad.212282.112 · Cited by 443
Structural Basis of DNA Recognition by p53 Tetramers
Kitayner, M., Rozenberg, H., Kessler, N., Rabinovich, D., Shaulov, L., Haran, T. E., & Shakked, Z. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.015 · Cited by 408
BID regulation by p53 contributes to chemosensitivity
Sax, J. K., Fei, P., Murphy, M. E., Bernhard, E., Korsmeyer, S. J., & El-Deiry, W. S. (2002) · Nature Cell Biology · doi:10.1038/ncb866 · Cited by 420
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
Pazgier, M., Liu, M., Zou, G., Yuan, W., Li, C., Li, C., Li, J., Monbo, J., Zella, D., Tarasov, S. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900947106 · Cited by 391
PPM1D dephosphorylates Chk1 and p53 and abrogates cell cycle checkpoints
Lu, X., Nannenga, B., & Donehower, L. A. (2005) · Genes & Development · doi:10.1101/gad.1291305 · Cited by 389
HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53
Linares, L. K., Hengstermann, A., Ciechanover, A., Müller, S., & Scheffner, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2030930100 · Cited by 361
The p53 response to DNA damage
Meek, D. W. (2004) · DNA Repair · doi:10.1016/j.dnarep.2004.03.027 · Cited by 329
Selective Evolution of Stromal Mesenchyme with p53 Loss in Response to Epithelial Tumorigenesis
Hill, R., Song, Y., Cardiff, R. D., & Van Dyke, T. (2005) · Cell · doi:10.1016/j.cell.2005.09.030 · Cited by 324
Danovi, D., Meulmeester, E., Pasini, D., Migliorini, D., Capra, M., Frenk, R., de Graaf, P., Francoz, S., Gasparini, P., Gobbi, A., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5835-5843.2004 · Cited by 310
Targeting the MDM2–p53 Protein–Protein Interaction for New Cancer Therapy: Progress and Challenges
Wang, S., Zhao, Y., Aguilar, A., Bernard, D., & Yang, C.-Y. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026245 · Cited by 300
Tovar, C., Graves, B., Packman, K., Filipovic, Z., Xia, B. H. M., Tardell, C., Garrido, R., Lee, E., Kolinsky, K., To, K.-H., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2807 · Cited by 283
Espinosa, J. M., Verdun, R. E., & Emerson, B. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00359-9 · Cited by 256
A threshold mechanism mediates p53 cell fate decision between growth arrest and apoptosis.
Kracikova, M., Akiri, G., George, A., Sachidanandam, R., & Aaronson, S. A. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.155 · Cited by 261
Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells in vivo
Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260
PRIMA-1MET synergizes with cisplatin to induce tumor cell apoptosis
Bykov, V. J. N., Zache, N., Stridh, H., Westman, J., Bergman, J., Selivanova, G., & Wiman, K. G. (2005) · Oncogene · doi:10.1038/sj.onc.1208419 · Cited by 252
Cell fate decision mediated by p53 pulses
Zhang, X.-P., Liu, F., Cheng, Z., & Wang, W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813088106 · Cited by 253
A nuclear poly(ADP-Ribose)-dependent signalosome confers DNA damage-induced IκB kinase activation.
Stilmann, M., Hinz, M., Arslan, S. Ç., Zimmer, A., Schreiber, V., & Scheidereit, C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.032 · Cited by 232
Feng, L., Lin, T., Uranishi, H., Gu, W., & Xu, Y. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5389-5395.2005 · Cited by 236
Marine, J.-C. W., Dyer, M. A., & Jochemsen, A. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.03362 · Cited by 228
p21/CDKN1A Mediates Negative Regulation of Transcription by p53
Löhr, K., Möritz, C., Contente, A., & Dobbelstein, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212517200 · Cited by 227
Textor, S., Fiegler, N., Arnold, A., Porgador, A., Hofmann, T. G., & Cerwenka, A. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3211 · Cited by 221
Changes in Regenerative Capacity through Lifespan
Yun, M. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161025392 · Cited by 216
The c‐myc Promoter: Still MysterY and Challenge
(2008) · Advances in Cancer Research · doi:10.1016/s0065-230x(07)99004-1 · Cited by 211
The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression
Minsky, N., & Oren, M. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.016 · Cited by 204
Targeting the p53–MDM2 interaction to treat cancer
Klein, C., & Vassilev, L. T. (2004) · British Journal of Cancer · doi:10.1038/sj.bjc.6602164 · Cited by 204
Toledo, F., Krummel, K. A., Lee, C. J., Liu, C.-W., Rodewald, L.-W., Tang, M., & Wahl, G. M. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.03.014 · Cited by 199
Wang, W., Cortes, J. E., Tang, G., Khoury, J. D., Wang, S., Bueso-Ramos, C. E., DiGiuseppe, J. A., Chen, Z., Kantarjian, H. M., Medeiros, L. J., et al. (2016) · Blood · doi:10.1182/blood-2016-01-690230 · Cited by 198
Identification and Characterization of the First Small Molecule Inhibitor of MDMX
Reed, D., Shen, Y., Shelat, A. A., Arnold, L. A., Ferreira, A. M., Zhu, F., Mills, N., Smithson, D. C., Regni, C. A., Bashford, D., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.056747 · Cited by 198
p53 Upregulates Death Receptor 4 Expression through an Intronic p53 Binding Site
Liu, X., Yue, P., Khuri, F. R., & Sun, S.-Y. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1195 · Cited by 184
Reactivation of mutant p53: molecular mechanisms and therapeutic potential
Selivanova, G., & Wiman, K. G. (2007) · Oncogene · doi:10.1038/sj.onc.1210295 · Cited by 186
p53 and regulation of DNA damage recognition during nucleotide excision repair
Adimoolam, S., & Ford, J. M. (2003) · DNA Repair · doi:10.1016/s1568-7864(03)00087-9 · Cited by 181
Potent and orally active small-molecule inhibitors of the MDM2-p53 interaction
Yu, S., Qin, D., Shangary, S., Chen, J., Wang, G., Ding, K., McEachern, D., Qiu, S., Nikolovska-Coleska, Z., Miller, R., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901400z · Cited by 180
Solution structure of p53 core domain: Structural basis for its instability
Cañadillas, J. M. P., Tidow, H., Freund, S. M. V., Rutherford, T. J., Ang, H. C., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510941103 · Cited by 174
Li, X., Lee, Y.-K., Jeng, J.-C., Yen, Y., Schultz, D. C., Shih, H.-M., & Ann, D. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706912200 · Cited by 168
Divide and conquer: nucleotide excision repair battles cancer and ageing
Mitchell, J. R., Hoeijmakers, J. H., & Niedernhofer, L. J. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00018-8 · Cited by 160
Apoptotic Cell Death Under Hypoxia
Sendoel, A., & Hengartner, M. O. (2014) · Physiology · doi:10.1152/physiol.00016.2013 · Cited by 157
Niedbala, W., Cai, B., Liu, H., Pitman, N., Chang, L., & Liew, F. Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703725104 · Cited by 156
Xie, H., Ma, K., Zhang, K., Zhou, J., Li, L., Yang, W., Gong, Y., Cai, L., & Gong, K. (2021) · Cell Death & Disease · doi:10.1038/s41419-020-03229-8 · Cited by 155
Chang, C.-J., Mulholland, D. J., Valamehr, B., Mosessian, S., Sellers, W. R., & Wu, H. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00310-08 · 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
Vikhanskaya, F., Lee, M. K., Mazzoletti, M., Broggini, M., & Sabapathy, K. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm099 · Cited by 145
hTERT: a novel endogenous inhibitor of the mitochondrial cell death pathway
Massard, C., Zermati, Y., Pauleau, A.-L., Larochette, N., Métivier, D., Sabatier, L., Kroemer, G., & Soria, J.-C. (2006) · Oncogene · doi:10.1038/sj.onc.1209487 · Cited by 144
Hdmx protein stability is regulated by the ubiquitin ligase activity of Mdm2
de Graaf, P., Little, N. A., Ramos, Y. F. M., Meulmeester, E., Letteboer, S. J. F., & Jochemsen, A. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213034200 · Cited by 143
Cell Type- and Promoter-specific Roles of Ser18 Phosphorylation in Regulating p53 Responses
Chao, C., Hergenhahn, M., Kaeser, M. D., Wu, Z., Saito, S., Iggo, R., Hollstein, M., Appella, E., & Xu, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306938200 · Cited by 141
The UMD TP53 database and website: update and revisions
Hamroun, D., Kato, S., Ishioka, C., Claustres, M., Béroud, C., & Soussi, T. (2006) · Human Mutation · doi:10.1002/humu.20269 · Cited by 140
Glycogen synthase kinase 3-dependent phosphorylation of Mdm2 regulates p53 abundance
Kulikov, R., Boehme, K. A., & Blattner, C. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.16.7170-7180.2005 · Cited by 132
Okamoto, K., Kashima, K., Pereg, Y., Ishida, M., Yamazaki, S., Nota, A., Teunisse, A., Migliorini, D., Kitabayashi, I., Marine, J.-C., et al. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.21.9608-9620.2005 · Cited by 129
The p53 pathway in hematopoiesis: lessons from mouse models, implications for humans
Pant, V., Quintás-Cardama, A., & Lozano, G. (2012) · Blood · doi:10.1182/blood-2012-05-356014 · Cited by 129
The beneficial effects of spirulina focusing on its immunomodulatory and antioxidant properties
Maddaly, R. (2010) · Nutrition and Dietary Supplements · doi:10.2147/nds.s9838 · Cited by 127
Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3
LeBron, C., Chen, L., Gilkes, D. M., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601032 · Cited by 122
DNA repair and aging: The impact of the p53 family
Nicolai, S., Rossi, A., Di Daniele, N., Melino, G., Annicchiarico-Petruzzelli, M., & Raschellà, G. (2015) · Aging · doi:10.18632/aging.100858 · Cited by 118
Perp Is a Mediator of p53-Dependent Apoptosis in Diverse Cell Types
Ihrie, R. A., Reczek, E., Horner, J. S., Khachatrian, L., Sage, J., Jacks, T., & Attardi, L. D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.055 · Cited by 118
Regulation of DNA damage recognition and nucleotide excision repair: another role for p53
Ford, J. M. (2005) · Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis · doi:10.1016/j.mrfmmm.2005.04.005 · Cited by 117
Vilgelm, A. E., Pawlikowski, J. S., Liu, Y., Hawkins, O. E., Davis, T. A., Smith, J., Weller, K. P., Horton, L. W., McClain, C. M., Ayers, G. D., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2405 · Cited by 115
Spurgers, K. B., Gold, D. L., Coombes, K. R., Bohnenstiehl, N. L., Mullins, B., Meyn, R. E., Logothetis, C. J., & McDonnell, T. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513901200 · Cited by 114
DNA Binding Cooperativity of p53 Modulates the Decision between Cell-Cycle Arrest and Apoptosis
Schlereth, K., Beinoraviciute-Kellner, R., Zeitlinger, M. K., Bretz, A. C., Sauer, M., Charles, J. P., Vogiatzi, F., Leich, E., Samans, B., Eilers, M., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.037 · Cited by 113
Involvement of the INK4a/Arf gene locus in senescence
Collins, C. J., & Sedivy, J. M. (2003) · Aging Cell · doi:10.1046/j.1474-9728.2003.00048.x · Cited by 113
Mitotic catastrophe and cancer drug resistance: A link that must to be broken
Denisenko, T. V., Sorokina, I. V., Gogvadze, V., & Zhivotovsky, B. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2015.11.002 · Cited by 108
Disruption of protein–protein interactions: Towards new targets for chemotherapy
Loregian, A., & Palù, G. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20356 · Cited by 108
Current status and new treatment approaches in TP53 mutated AML
Hunter, A. M., & Sallman, D. A. (2019) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2019.05.004 · Cited by 102
Baltzis, D., Pluquet, O., Papadakis, A. I., Kazemi, S., Qu, L.-K., & Koromilas, A. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704491200 · Cited by 107
Gannon, H. S., Woda, B. A., & Jones, S. N. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.04.011 · Cited by 105
Apoptosis: molecular mechanisms and pathogenicity
Rastogi, R. P., R., & Sinha, R. P. (2010) · Technische Universität Dortmund · doi:10.17877/de290r-8930 · Cited by 106
p53 target gene AEN is a nuclear exonuclease required for p53-dependent apoptosis
Kawase, T., Ichikawa, H., Ohta, T., Nozaki, N., Tashiro, F., Ohki, R., & Taya, Y. (2008) · Oncogene · doi:10.1038/onc.2008.32 · Cited by 105
MdmX is a substrate for the deubiquitinating enzyme USP2a
Allende-Vega, N., Sparks, A., Lane, D. P., & Saville, M. K. (2010) · Oncogene · doi:10.1038/onc.2009.330 · Cited by 100
Transcriptional regulation of cellular senescence
Lanigan, F., Geraghty, J. G., & Bracken, A. P. (2011) · Oncogene · doi:10.1038/onc.2011.34 · Cited by 95
Iijima, K., Gatt, A., & Iijima-Ando, K. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq200 · Cited by 96
Metadata
- Authors
- Vousden, K. H., & Lu, X.
- Venue
- Nature Reviews Cancer
- Published
- 2002-08-01
- Volume
- 2
- Issue
- 8
- Pages
- 594-604
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- OpenAlex
- W2063669247
- Cited by
- 3,192
- References
- 16
- FWCI
- 7.49
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.