The DOI matches its Crossref record; 30 of the 31 references it cites were found in a registry or an index.
HDM2 antagonist Nutlin-3 disrupts p73-HDM2 binding and enhances p73 function
Abstract
Nutlin-3, a small molecule inhibitor, activates p53 by disrupting p53-HDM2 association. In this study, we found that Nutlin-3 suppressed cell growth and induced apoptosis in the absence of wild-type p53, suggesting a p53-independent mechanism for Nutlin-3-induced cell death. Like p53, its homolog p73 transactivates proapoptotic genes and induces cell death. Since HDM2, a key negative regulator of p53, also binds to and inhibits p73, we asked whether p73 could mediate Nutlin-3-induced apoptosis. We demonstrate that Nutlin-3 inhibits endogenous binding between the proapoptotic p73 isoform TAp73alpha and HDM2 in p53-null cells. Dissociation of p73 and HDM2 leads to increased p73 transcriptional activity with upregulation of p73 target genes noxa, puma and p21, as well as enhanced apoptosis. p73 knockdown by siRNA results in rescue of Nutlin-3-treated cells, indicating that Nutlin-3-induced apoptosis is, at least in part, p73 dependent. In addition, Nutlin-3 treatment increases TAp73alpha protein levels with prolongation of p73 half-life. These results provide the first evidence that Nutlin-3 disrupts endogenous p73-HDM2 interaction and enhances the stability and proapoptotic activities of p73 and thus, provides a rationale for the use of Nutlin-3 in the large number of human tumors in which p53 is inactivated.
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
“The MDM2 protein–protein interaction (PPI) inhibitor nutlin3a binds to the N-terminal hydrophobic pocket of MDM2 and blocks interaction of MDM2 with not only p53 but also a number of other key signal transducers, including p73α, E2F1, Rb, and HIF-1α”
From Combination therapy in a xenograft model of glioblastoma: Enhancement of the antitumor activity of temozolomide by an MDM2 antagonist (2017) · cites this paper as [22]
In the citing paper
“information on dosing regimens that build upon front-line chemotherapy for GBM is lacking.19,21,22,34,43,45”
From Combination therapy in a xenograft model of glioblastoma: Enhancement of the antitumor activity of temozolomide by an MDM2 antagonist (2017) · cites this paper as [22]
In the citing paper
“Nutlin-3a also inhibits the binding of the p73 isoform p73α, as well as E2F1 and hypoxia inducible factor 1α (Hif-1α), to the N-terminal hydrophobic pocket of Mdm2 (11–13).”
From Potentiation of carboplatin-mediated DNA damage by the Mdm2 modulator Nutlin-3a in a humanized orthotopic breast-to-lung metastatic model (2015) · cites this paper as [12]
In the citing paper
“Lau and colleagues showed that when cells were treated with Nutlin-3a, the binding of p73α to Mdm2 was inhibited, leading to p73α-mediated induction of pro-apoptotic downstream targets and increased apoptosis in cells lacking wild-type p53 (12).”
From Potentiation of carboplatin-mediated DNA damage by the Mdm2 modulator Nutlin-3a in a humanized orthotopic breast-to-lung metastatic model (2015) · cites this paper as [12]
In the citing paper
“While p53 and p73α can both interact with Mdm2 in the same N-terminal hydrophobic pocket (12), Mdm2 does not ubiquitinate p73α (44–46).”
From Potentiation of carboplatin-mediated DNA damage by the Mdm2 modulator Nutlin-3a in a humanized orthotopic breast-to-lung metastatic model (2015) · cites this paper as [12]
In the citing paper
“These data are consistent with previous reports indicating that p73α can directly bind to the Mdm2 promoter and increase Mdm2 gene expression (12, 47).”
From Potentiation of carboplatin-mediated DNA damage by the Mdm2 modulator Nutlin-3a in a humanized orthotopic breast-to-lung metastatic model (2015) · cites this paper as [12]
In the citing paper
“Blockade of the binding of Mdm2 to p73α by Nutlin-3a increases the pool of p73α available to transcriptionally activate pro-apoptotic gene expression and promote apoptosis in mutant p53 and p53 null cells (12).”
From Potentiation of carboplatin-mediated DNA damage by the Mdm2 modulator Nutlin-3a in a humanized orthotopic breast-to-lung metastatic model (2015) · cites this paper as [12]
Citations
Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Structure 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
Role for the p53 homologue p73 in E2F-1-induced apoptosis
Irwin, M. S., Marín, M. C., Phillips, A. C., Seelan, R. S., Smith, D. I., Liu, W., Flores, E. R., Tsai, K. Y., Jacks, T., Vousden, K. H., et al. (2000) · Nature · doi:10.1038/35036614 · Cited by 710
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
Inactivation of the p53 pathway in retinoblastoma
Laurie, N. A., Donovan, S. L., Shih, C.-S., Zhang, J., Mills, N., Fuller, C., Teunisse, A., Lam, S., Ramos, Y., Mohan, A., et al. (2006) · Nature · doi:10.1038/nature05194 · Cited by 595
AIS is an oncogene amplified in squamous cell carcinoma
Hibi, K., Trink, B., Patturajan, M., Westra, W. H., Caballero, O. L., Hill, D. E., Ratovitski, E. A., Jen, J., & Sidransky, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5462 · Cited by 464
p63 mediates survival in squamous cell carcinoma by suppression of p73-dependent apoptosis
Rocco, J. W., Leong, C., Kuperwasser, N., DeYoung, M. P., & Ellisen, L. W. (2006) · Cancer Cell · doi:10.1016/j.ccr.2005.12.013 · Cited by 435
Chemosensitivity linked to p73 function
Irwin, M. S., Kondo, K., Marín, M. C., Cheng, L. S., Hahn, W. C., & Kaelin, W. G. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00078-3 · Cited by 406
Iwakuma, T., & Lozano, G. (2003) · PubMed · Cited by 390
MDM2 suppresses p73 function without promoting p73 degradation
Zeng, X., Chen, L., Jost, C. A., Maya, R., Keller, D., Wang, X., Kaelin, W. G., Oren, M., Chen, J., & Lu, H. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3257 · Cited by 334
Flagged first, then by citations
1 of the 31 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–182 of 182
P63 and P73 Activation in Cancers with p53 Mutation
Cai, B., Hsu, Y.-C., Yeh, F.-Y., Lin, Y.-R., Lu, R.-Y., Yu, S.-J., Shaw, J., Wu, M.-H., Tsai, Y.-Z., Lin, Y.-C., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10071490 · Cited by 24
Small molecule inhibitors in acute myeloid leukemia: from the bench to the clinic
Al-Hussaini, M., & DiPersio, J. F. (2014) · Expert Review of Hematology · doi:10.1586/17474086.2014.932687 · Cited by 26
MDM2-Mediated p21 Proteasomal Degradation Promotes Fluoride Toxicity in Ameloblasts
Deng, H., Ikeda, A., Cui, H., Bartlett, J. D., & Suzuki, M. (2019) · Cells · doi:10.3390/cells8050436 · Cited by 24
Zhang, M., Zhang, J., Yan, W., & Chen, X. (2016) · Oncotarget · doi:10.18632/oncotarget.13126 · Cited by 23
Structural Basis for ASPP2 Recognition by the Tumor Suppressor p73
Canning, P., von Delft, F., & Bullock, A. N. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.08.005 · Cited by 22
p73 Plays a Role in Erythroid Differentiation through GATA1 Induction
Marqués-García, F., Ferrándiz, N., Fernández-Alonso, R., González-Cano, L., Herreros‐Villanueva, M., Rosa‐Garrido, M., Fernández‐García, B., Vaque, J. P., Marqués, M. M., Alonso-Ferrero, M. E., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.026849 · Cited by 22
p53/p73 Protein Network in Colorectal Cancer and Other Human Malignancies
Horvat, A., Tadijan, A., Vlašić, I., & Slade, N. (2021) · Cancers · doi:10.3390/cancers13122885 · Cited by 22
Reactivation of p53 via MDM2 inhibition
Kim, E. S., & Shohet, J. M. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.302 · Cited by 21
Targeting p63 Upregulation Abrogates Resistance to MAPK Inhibitors in Melanoma
Patel, A. A., García, L. F., Mannella, V., Gammon, L., Borg, T., Maffucci, T., Scatolini, M., Chiorino, G., Vergani, E., Rodolfo, M., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3230 · Cited by 22
TP53 in AML and MDS: The new (old) kid on the block
Marks, J. A., Wang, X., Fenu, E. M., Bagg, A., & Lai, C. (2023) · Blood Reviews · doi:10.1016/j.blre.2023.101055 · Cited by 20
p53 Family: Therapeutic Targets in Neuroblastoma
Wolter, J. K., Angelini, P., & Irwin, M. S. (2010) · Future Oncology · doi:10.2217/fon.09.176 · Cited by 22
Sulg, M., Kirjavainen, A., Pajusola, K., Büeler, H., Ylikoski, J. S., Laiho, M., & Pirvola, U. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06563.x · Cited by 19
Lee, S., Choi, H. C., Choe, Y.-J., Shin, S. J., Lee, S. H., & Kim, H. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2463 · Cited by 18
Recent advances in the pharmacological targeting of ubiquitin-regulating enzymes in cancer
Montagut, A. M., Armengol, M., Gorjón-de-Pablo, G., Estrada‐Tejedor, R., Borrell, J. I., & Roué, G. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.007 · Cited by 17
Zawacka‐Pankau, J. (2020) · Cancers · doi:10.3390/cancers12092717 · Cited by 16
Ohgami, T., Kato, K., Kobayashi, H., Sonoda, K., Inoue, T., Yamaguchi, S., Yoneda, T., & Wake, N. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2010.01543.x · Cited by 17
Targeting of p53 and its homolog p73 by protoporphyrin IX
Sznarkowska, A., Maleńczyk, K., Kadziński, L., Bielawski, K. P., Banecki, B., & Zawacka‐Pankau, J. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.12.004 · Cited by 17
Fregni, M., Ciribilli, Y., & Zawacka‐Pankau, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137213 · Cited by 16
Marcus, J. M., Burke, R. T., Doak, A. E., Park, S., & Orth, J. D. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1480224 · Cited by 17
Nutlin-3 induces HO-1 expression by activating JNK in a transcription-independent manner of p53
Choe, Y.-J., Lee, S.-Y., Ko, K. W., Shin, S. J., & Kim, H.-S. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.2227 · Cited by 16
p53 family interactions and yeast: together in anticancer therapy
Gomes, S., Leão, M., Raimundo, L., Ramos, H., Soares, J., & Saraiva, L. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.02.007 · Cited by 18
Enhanced response of melanoma cells to MEK inhibitors following unbiased IGF-1R down-regulation
Suleymanova, N., Crudden, C., Worrall, C., Dricu, A., Girnita, A., & Girnita, L. (2017) · Oncotarget · doi:10.18632/oncotarget.19286 · Cited by 15
Leão, M., Gomes, S., Bessa, C., Soares, J., Raimundo, L., Monti, P., Fronza, G., Pereira, C., & Saraiva, L. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.09.028 · Cited by 15
Marimuthu, P., Kaur, K., Kandalam, U., Jasani, V., Bukhari, N., Nguyen, M., Abdul, A., Pervez, F. F., & Rathinavelu, A. (2010) · Journal of Medicinal Food · doi:10.1089/jmf.2009.0270 · Cited by 14
Emerging therapeutic targets for retinoblastoma
Manukonda, R., Narayana, R. V. L., Kaliki, S., Mishra, D. K., & Vemuganti, G. K. (2022) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2022.2158812 · Cited by 13
Kinase activity-independent suppression of p73α by AMP-activated kinase α (AMPKα)
Lee, Y.-G., Lee, S.-W., Sin, H.-S., Kim, E., & Um, S.-J. (2008) · Oncogene · doi:10.1038/onc.2008.452 · Cited by 13
Sznarkowska, A., Kostecka, A., Kawiak, A., Acedo, P., Lion, M., Inga, A., & Zawacka‐Pankau, J. (2018) · Cell Division · doi:10.1186/s13008-018-0043-3 · Cited by 13
Ye, D.-J., Kwon, Y., Baek, H., Cho, E.-A., Kwon, T.-U., & Chun, Y. (2019) · Journal of Toxicology and Environmental Health · doi:10.1080/15287394.2019.1635934 · Cited by 13
An Effective Virtual Screening Protocol To Identify Promising p53–MDM2 Inhibitors
Tortorella, P., Laghezza, A., Durante, M., Gomez-Monterrey, I. M., Bertamino, A., Campiglia, P., Loiodice, F., Daniele, S., Martini, C., & Agamennone, M. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00747 · Cited by 12
Zheng, T., Wang, J., Chen, X., Meng, X., Song, X., Lu, Z., Jiang, H., & Liu, L. (2010) · Tumor Biology · doi:10.1007/s13277-010-0035-7 · Cited by 11
Hainaut, P. L., Wiman, K. G., & Olivier, M. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3676-8 · Cited by 10
Abrams, S. L., Akula, S. M., Steelman, L. S., Follo, M. L., Cocco, L., Ratti, S., Martelli, A. M., Libra, M., Falzone, L., Candido, S., et al. (2021) · Advances in Biological Regulation · doi:10.1016/j.jbior.2021.100840 · Cited by 10
Li, Y., Shao, J., Shen, K., Xu, Y. F., Liu, J., & Qian, X. H. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24194 · Cited by 9
Wu, L., Hu, Y., He, Y., Xia, Y., Lu, H., Cao, Z. Y., Yi, X., & Wang, J. (2019) · The Analyst · doi:10.1039/c9an00301k · Cited by 9
Shi, Y., Takenobu, H., Kurata, K., Yamaguchi, Y., Yanagisawa, R., Ohira, M., Koike, K., Nakagawara, A., Jiang, L., & Kamijo, T. (2010) · European Journal of Cancer · doi:10.1016/j.ejca.2010.05.026 · Cited by 9
Zhang, L., Yan, Y., Zhu, D., Yang, W., Wang, W., Hu, Y., Yang, B., & He, Q. (2010) · Investigational New Drugs · doi:10.1007/s10637-010-9512-5 · Cited by 8
Li, F., Du, Z., Huang, X., Dong, C., & Ren, J. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03521 · Cited by 9
Ribeiro, H. D. O., Cortez, A. P., de Ávila, R. I., da Silva, A. C. G., de Carvalho, F. S., Menegatti, R., Lião, L. M., & Valadares, M. C. (2020) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12540 · Cited by 8
Pharmacological Inhibition of MDM2 Induces Apoptosis in p53-Mutated Triple-Negative Breast Cancer
On, J. L., Ghaderi, S., Rittmann, C., Hoffmann, G., Gier, F., Woloschin, V., Tu, J., Bhatia, S., Kulik, A., Niederacher, D., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031078 · Cited by 7
Wang, X., Chen, Y., Liu, H., Guo, S., Hu, Y., Zhan, Y., & An, H. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.07.106 · Cited by 7
Mochizuki, H., Goto‐Koshino, Y., Sato, M., Fujino, Y., Ohno, K., & Tsujimoto, H. (2012) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2012.04.017 · Cited by 6
P53 gene: major mutations in neoplasias and anticancer gene therapy
Lima, C. R. D. O., Rabelo, R. E., Vulcani, V. A. S., Cardoso, L. D., Sousa, N. L. D. M., & de Moura, V. M. B. D. (2012) · Ciência Rural · doi:10.1590/s0103-84782012000500014 · Cited by 6
Programmed Cell Death in the Gastrointestinal Tract
Johnson, L. R., & Ray, R. M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00013-0 · Cited by 7
Therapeutic considerations for Mdm2: not just a one trick pony
Lehman, J. A., Eitel, J. A., Batuello, C. N., & Mayo, L. D. (2008) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.3.11.1309 · Cited by 6
Recruiting TP53 to target chronic myeloid leukemia stem cells
Grant, S. (2020) · Haematologica · doi:10.3324/haematol.2019.246306 · Cited by 5
Lai, X., Yoda, H., Qiao, Y., Kida, Y., Takenaga, K., Shinozaki, Y., Koshikawa, N., & Takatori, A. (2025) · Cancer Science · doi:10.1111/cas.70043 · Cited by 4
Targeting MDM2 affects spastin protein levels and functions: implications for HSP treatment
Sardina, F., Polverino, F., Valentini, S., Carsetti, C., Falvo, E., Tisci, G., Soddu, S., Moretti, F., Paiardini, A., & Rinaldo, C. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02333-y · Cited by 3
Bajelan, B., Zaki‐Dizaji, M., Darabi, S., & Rajaei, F. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27798 · Cited by 3
Chakraborty, R., Dutta, A., & Mukhopadhyay, R. (2025) · Clinical & Translational Oncology · doi:10.1007/s12094-024-03841-6 · Cited by 3
Targeting the MDM2–p53 interaction as a therapeutic strategy for the treatment of cancer
Peirce, S. K. (2010) · Cell Health and Cytoskeleton · doi:10.2147/chc.s4952 · Cited by 3
Lu, M., Ren, Y., Feng, S., Wang, S., Xia, W., Gu, B., Shen, Y., Yue, A., Li, N., Zhang, Y., et al. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1508421 · Cited by 2
p53-Reactivating Molecules as Research Tools and Anticancer Drugs
Grinkevich, V. V., Warnecke, A., & Selivanova, G. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3676-8_13 · Cited by 2
Regunath, K., Fomin, V., Liu, Z., Wang, P., Hoque, M., Tian, B., Rabadán, R., & Prives, C. L. (2024) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-23-0295 · Cited by 2
Mechanisms and Ways to Overcome Acquired Resistance of Cancer Cells to Mcl-1 Antagonists
Pervushin, N. V., Fernandez, B. Y. V., Senichkin, V. V., Yapryntseva, M. A., Pavlov, V., Zhivotovsky, B., & Kopeina, G. S. (2025) · Biochemistry (Moscow) · doi:10.1134/s0006297925602710 · Cited by 1
BMAL1 silencing as a promising chemosensitizing strategy for triple-negative breast cancer
Wang, L.-Y., Xu, X., Xuan, W.-J., Bi, X.-Y., & Zhou, Q. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-026-01788-8 · Cited by 1
MOLECULAR GENETICS OF SOFT TISSUE TUMORS
Lasota, J. P. (2010) · Cambridge University Press eBooks · doi:10.1017/cbo9780511781049.006 · Cited by 1
Resistance of human primary mesenchymal stem cells to cytotoxic effects of nutlin‐3 in vitro
Bajelan, B., Zaki‐Dizaji, M., Rahmani, B., Darzi, S., Darabi, S., & Rajaei, F. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29324 · Cited by 1
Schwaller, J. (2020) · Haematologica · doi:10.3324/haematol.2019.246348 · Cited by 1
Targeting the Transcription Factors of ROS Tumorigenic Pathways as a Therapeutic Strategy in Cancer
Sriramajayam, K., Gokulan, R. C., & Tharmalingam, J. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-5422-0_275 · Cited by 1
Sznarkowska, A., Kostecka, A., Kawiak, A., Acedo, P., Lion, M., Inga, A., & Zawacka‐Pankau, J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/357293 · Cited by 1
IKKalpha mediated NOTCH1 Activation Promotes Tumorigenesis via FOXA2 Suppression
Liu, M. (2012) · Digital Commons-TMC (Texas Medical Center)
Pharmacological targeting of mutant p53 family members
Rökaeus, N. (2011) · Figshare
Phospho-regulation and metastatic potential of Murine Double Minute 2
Batuello, C. N. (2012) · doi:10.7912/c2/1866
Modulation of the Mdm2 signaling axis sensitizes triple-negative breast cancer cells to carboplatin
Tonsing-Carter, E. Y. (2014) · ProQuest Demo Repository · doi:10.7912/c2/308
p73 gene and its role in gynecological tumors: an advance
Peng, P., Huang, L., & Wang, Y. (2011) · Academic Journal of Second Military Medical University · doi:10.3724/sp.j.1008.2011.00334
Role of p53 in Apoptosis and Cancer Therapy
Daloii, M. R. N., & Abdollahzade, R. (2014) · مجله علمی پژوهشی افق دانش
Regulation of MDM2 and the p53 Family by the NEDD8 Pathway
Watson, I. R. (2011) · TSpace (University of Toronto)
Investigation of the intrinsic mechanism of drug resistance in multiple myeloma
Ooi, M. G. M. (2011) · Dublin City University Open Access Institutional Repository (Dublin City University)
Targeting the Transcription Factors of ROS Tumorigenic Pathways as a Therapeutic Strategy in Cancer
Sriramajayam, K., Gokulan, R. C., & Tharmalingam, J. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-1247-3_275-1
Latest advances in cell-death pathway approaches in treating high-risk neuroblastoma
Temirbek, A., & Then, S. (2022) · Neuroscience Research Notes · doi:10.31117/neuroscirn.v5i3.147
Molecular genetics of soft tissue tumors
Lasota, J. P. (2016) · Cambridge University Press eBooks · doi:10.1017/9781107707504.006
Synthesis and Mechanism of p53‐MDM2 Inhibitors with Heterocyclic Structures: A Focused Review
Ji, L., Zhang, W., Zhang, Y., Zhao, S., Long, H., Qin, L., Tian, J., Li, H., Zhu, D., Zhou, Y., et al. (2023) · ChemistrySelect · doi:10.1002/slct.202302240
On, J. L., Woloschin, V., Gier, F., Tu, J., Bhatia, S., Lenz, T., Kulik, A., Stühler, K., Niederacher, D., Neubauer, H. J., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.02.582899
Nobumoto, T., Yamasaki, S., Hamada, A., Higaki, M., Ito, N., Obayashi, F., Ishida, Y., Hamana, T., Shintani, T., Tani, R., et al. (2024) · Journal of Oral and Maxillofacial Surgery Medicine and Pathology · doi:10.1016/j.ajoms.2024.12.017
Biomass-based enantioselective approach to 1,2-di(furan-2-yl)ethane-1,2-diamine and its derivatives
Vasechkin, K. V., Kovalevsky, R. A., Kucherenko, A. S., Romanenko, A. R., Korlyukov, A. A., & Zlotin, S. G. (2025) · Mendeleev Communications · doi:10.71267/mencom.7871
PROTAC-Driven Protective Therapy increases the therapeutic window of anticancer drugsPreprint
Simón-Carrasco, L., Raya, S., Pietrini, E., Luque-Perez, M., Oliva, M. D. R., Rosado, I., & Lopez-Contreras, A. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.12.698947
Expression et fonctions biologiques de l’isoforme ΔNp63
de Gasperis, A. (2011) · theses.fr (ABES) · doi:10.70675/3b754ccbz3f14z4949z9f45z1bdd5995d3d3
The role of p53 modulation in correcting aberrant placental apoptosis in pre-eclampsia and IUGR
Sharp, A. (2011) · Research Explorer (The University of Manchester)
Metadata
- Authors
- Lau, L. M. S., Nugent, J. K., Zhao, X., & Irwin, M. S.
- Affiliations
- University of Toronto (CA)
- Corresponding author
- Irwin, M S
- Venue
- Oncogene
- Published
- 2007-08-13
- Volume
- 27
- Issue
- 7
- Pages
- 997-1003
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2029865335
- Cited by
- 182
- References
- 31
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 5 · 2023: 2 · 2022: 10 · 2021: 7 · 2020: 10 · 2019: 8 · 2018: 5 · 2017: 6 · 2016: 9 · 2015: 11 · 2014: 15 · 2013: 6 · 2012: 18
- FWCI
- 6.99
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canada Research Chairs
- Terry Fox Foundation
- Hospital for Sick Children
- National Cancer Institute
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- Nutlin-3, p73, MDM2, p53-independent apoptosis, Noxa, PUMA, p21, transcriptional activation, p53-null cells, p53 inactivation, cancer therapy
- MeSH terms
- Bone Neoplasms, DNA-Binding Proteins, Humans, Imidazoles, Nuclear Proteins, Piperazines, Protein Binding, Proto-Oncogene Proteins, Osteosarcoma, Transcription, Genetic, Protein Biosynthesis, Immunoblotting, Tumor Suppressor Protein p53, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Tumor Suppressor Proteins, RNA, Small Interfering, HCT116 Cells, Immunoprecipitation, Cyclin-Dependent Kinase Inhibitor p21, Apoptosis Regulatory Proteins, Proto-Oncogene Proteins c-mdm2
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