The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Accelerated MDM2 auto‐degradation induced by DNA‐damage kinases is required for p53 activation
Open accessAbstract
p53 activation prevents the proliferation of genetically unstable cells. Conversely, p53 antagonism by its transcriptional target, the E3 ubiquitin ligase MDM2, is critical for the viability of unstressed, cycling cells. We demonstrate that MDM2 induces the degradation of p53 in both the nucleus and the cytoplasm. As p53 and MDM2 accumulate in the nuclei of stressed cells, we investigated mechanisms enabling p53 activation despite the high MDM2 levels generated during a DNA-damage response. We show that DNA damage destabilized MDM2 by a mechanism involving damage-activated kinases and MDM2 auto-ubiquitination. p53 was stable and transcriptionally active when MDM2 was unstable, but became unstable and inactive as the damage response waned and MDM2 stabilized. Importantly, blocking MDM2 destabilization in DNA-damaged cells prevented p53 target gene activation. Our data reveal that controlled MDM2 degradation is an important new step in p53 regulation.
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.
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
“However, in addition to degrading p53, Mdm2 also undergoes auto-degradation [12,13] and targets Mdmx for degradation [14–16], which is critical for optimal p53 activation after stress.”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [12]
In the citing paper
“The disruption of Mdm2 oligomers might also contribute to their destabilization following DNA damage [12].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [12]
In the citing paper
“A recent study showed that DNA damage also accelerates MDM2 degradation through a mechanism that requires its own RING domain (Stommel and Wahl, 2004).”
From ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage (2005) · cites this paper as Stommel and Wahl, 2004
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
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
DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
Bakkenist, C. J., & Kastan, M. B. (2003) · Nature · doi:10.1038/nature01368 · Cited by 3,466
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
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
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 · cited 2×
“The importance of MDM2 in p53 regulation is evidenced by the embryonic lethality of MDM2 knockout mice, presumably due to unrestrained p53 activity (Jones et al, 1995; Montes de Oca Luna et al, 1995).”
BackgroundRescue 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 4×
“The importance of MDM2 in p53 regulation is evidenced by the embryonic lethality of MDM2 knockout mice, presumably due to unrestrained p53 activity (Jones et al, 1995; Montes de Oca Luna et al, 1995).”
BackgroundInfluentialPost‐translational modifications and activation of p53 by genotoxic stresses
Appella, E., & Anderson, C. W. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02225.x · Cited by 1,095
Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53
Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044
The INK4a/ARF network in tumour suppression
Sherr, C. J. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096061 · Cited by 1,001
The MDM2 gene amplification database
Momand, J. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.15.3453 · Cited by 982
Cited by
Sorted by citations
Items 301–383 of 383
Multiple Time Delays Induced Dynamics of p53 Gene Regulatory Network
Bi, Y., Li, Y., Hou, J., & Liu, Q. (2021) · International Journal of Bifurcation and Chaos · doi:10.1142/s0218127421502345 · Cited by 4
Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53
Xirodimas, D. P., & Scheffner, M. (2010) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4419-6676-6_10 · Cited by 5
A switch‐like dynamic mechanism for the initiation of replicative senescence
Zhang, Q.-H., Tian, X., Liu, F., & Wang, W. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.09.043 · Cited by 4
Okoshi, R., Kubo, N., Nakashima, K., Shimozato, O., Nakagawara, A., & Ozaki, T. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.01.114 · Cited by 4
Oscillation and bistable switching dynamical behavior of p53 regulated by PTEN upon DNA damage
Liu, N., Yang, H., Li, S., Wang, D., & Yang, L. (2021) · Acta Mechanica Sinica · doi:10.1007/s10409-020-01041-3 · Cited by 4
“In the case of cells DNA being damaged by stimuli, the degradation of Mdm2n can be facilitated [27].”
BackgroundZhao, B., Huang, Y., Shi, J., Zhou, X., Fagman, J. B., Wang, L., Liu, S., Wang, W., Liu, Y., Chen, Z., et al. (2025) · Advanced Science · doi:10.1002/advs.202517563 · Cited by 3
Cellular Senescence and Tumor Promotion
Demaria, M. (2020) · Springer eBooks · doi:10.1007/978-3-319-57415-8_79 · Cited by 3
Characterization of NimA-related Kinase 10 (NEK10): A Role in Checkpoint Control
Moniz, L. S. (2010) · TSpace (University of Toronto) · Cited by 3
Flt3 receptor tyrosine kinase in AML and its modulation of the p53/Hdm2/Bcl-2 pathway
Wergeland, L. (2007) · NORA - Norwegian Open Research Archives · Cited by 3
Krejčíř, R., Arcimowicz, Ł., Hároníková, L., Hrabal, V., Kokas, F. Z., Henek, T., Kucerikova, M., Bonczek, O., Zatloukalová, P., Hernychová, L., et al. (2025) · Molecular Oncology · doi:10.1002/1878-0261.70143 · Cited by 2
“MDM2 has a half-life as short as 5 min in stress conditions due to rapid ubiquitination and proteasomal degradation [46].”
Kwon, Y., Yoon, H., Han, J., Park, J. W., & Jang, K. L. (2026) · FEBS Letters · doi:10.1002/1873-3468.70275 · Cited by 2
“1), presumably by destabilizing and degrading MDM2 [40].”
Goffinet, S., Mauro, I. D., Doyen, J., Boyer, J., Birtwisle‐Peyrottes, I., Keslair, F., Pédeutour, F., & Dadone‐Montaudié, B. (2023) · Genes Chromosomes and Cancer · doi:10.1002/gcc.23137 · Cited by 2
“Another explanation regarding the loss of amplified MDM2 cells could be related to induction of MDM2 destabilization by a mechanism involving damage-activated kinases and MDM2 auto-ubiquitination.(33,34) It may have resulted in transcription activation and stability of TP53 leading to the activation of cell death path…”
BackgroundCytomorphic Electrical Circuit Modeling of Tumor Suppressor p53 Protein Pathway
Patra, T., Chatterjee, S., & Barman, S. (2023) · Transactions of Indian National Academy of Engineering · doi:10.1007/s41403-023-00403-0 · Cited by 2
“Mdm2 is degraded by various mechanisms, including ARF, ATM, proteasomes etc. (Stommel and Wahl 2004; Sparks et al.”
BackgroundEl‐Hawary, S. S., Hassan, M. H. A., Hudhud, A. O., Al-Karmalawy, A. A., Mustafa, M., Hamed, E. S. A. E., Abdelmohsen, U. R., & Mohammed, R. A. (2024) · Chemistry & Biodiversity · doi:10.1002/cbdv.202301617 · Cited by 2
Cooperation between MDM2 and MDMX in the Regulation of p53
Blaydes, J. P. (2010) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-8231-5_6 · Cited by 2
Modeling the heterogeneity of p53 dynamics in DNA damage response
Wu, W., Sun, W., & Sun, T. (2015) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720016500013 · Cited by 2
Modeling the roles of 14-3-3 σ and Wip1 in p53 dynamics and programmed cell death*
Liu, N., Yang, H., & Yang, L. (2021) · Communications in Theoretical Physics · doi:10.1088/1572-9494/abfd2a · Cited by 2
The p53-Mdm2 Loop: A Critical Juncture of Stress Response
Levav-Cohen, Y., Goldberg, Z., Alsheich-Bartok, O., Zuckerman, V., Haupt, S., & Haupt, Y. (2010) · Molecular biology intelligence unit · doi:10.1007/978-1-4419-8231-5_5 · Cited by 2
Tanouri, Z., Motlagh, O. R., & Mohammadinezhad, H. (2015) · British Journal of Mathematics & Computer Science · doi:10.9734/bjmcs/2015/14435 · Cited by 2
Influence of Mdm2-mediated positive feedback loop on the oscillation behavior of p53 gene network
Yang, H., Liu, N., & Yang, L. (2021) · Acta Physica Sinica · doi:10.7498/aps.70.20210015 · Cited by 2
Novel p53-Based Therapies: Strategies and Future Prospects
Laı́n, S., & Lane, D. P. (2005) · Springer eBooks · doi:10.1007/978-1-4020-2922-6_16 · Cited by 2
(2018) · Yale University Press eBooks · doi:10.2307/j.ctvqc6gvg.12 · Cited by 2
Suzuki, M., Isobe, R., Sato, T., Ishikawa, R., Suzuki, K., Kino, Y., Miura, T., Inaba, Y., Chida, K., & Fukumoto, M. (2024) · Radiation Protection Dosimetry · doi:10.1093/rpd/ncae118 · Cited by 1
Bonsignore, F., Pozzi, S., Aloi, E., Mazza, D., & Zambrano, S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1656051 · Cited by 2
“Active p53 tetramerizes and binds to promoters and enhancers of its target genes to activate their transcription (Stommel and Wahl, 2004) (Figure 3A).”
Horochowska, M., Przystupski, D., Kamińska, M., Bil‐Lula, I., Kazanowska, B. J., & Ussowicz, M. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48010074 · Cited by 1
“What’s more, NCL is able to bind to MDM2, an E3 ubiquitin ligase of TP53, reduce its level and hereby leads to an increase of p53 in cells which are not under stress conditions [43,44].”
Dynamical biocontrol systems: insights through mechanistic modelling
Javier, R. M., & DiStefano, J. J. (2008) · Mathematical and Computer Modelling of Dynamical Systems · doi:10.1080/13873950802379340 · Cited by 1
“In yet another series of independent experimental studies, Stommel and Wahl showed that the rate at which Mdm2 degrades itself (autodegradation) increases significantly following DNA damage [18].”
BackgroundThe ATM-mediated DNA-damage response
Shiloh, Y. (2013) · Cambridge University Press eBooks · doi:10.1017/cbo9781139046947.035 · Cited by 1
p53 as a unique target of action of cisplatin in acute leukaemia cells
Kumar, S., & Tchounwou, P. B. (2022) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17502 · Cited by 1
Konrath, F., Loewer, A., & Wolf, J. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3008-2_12 · Cited by 1
Lam, M. H. Y. (2011) · TSpace (University of Toronto) · Cited by 1
Kinase Liabilities in Early Drug Discovery
Kirchner, S. (2024) · Wiley eBooks · doi:10.1002/9781394182862.ch6 · Cited by 1
Upstream Targets in the p53 Pathway
McCarthy, A. R., & Laı́n, S. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3676-8_12
Targeting HAUSP: Killing Two Birds with One Stone
Brooks, C. L., & Gu, W. J. (2009) · Springer eBooks · doi:10.1007/978-0-387-69147-3_3
Chong, K. H. (2014) · Lincoln University Research Archive (Lincoln University)
Regulation of the p53 Tumor‐Suppressor Protein by Ubiquitin and Ubiquitin‐Like Molecules
Xirodimas, D. P. (2007) · Wiley eBooks · doi:10.1002/9783527619320.ch2c
FUNCTION OF ZNF668 IN CANCER DEVELOPMENT
Hu, R. (2011) · Digital Commons-TMC (Texas Medical Center)
Modulation of p53 activities by the prolyl-isomerase PIN1 and the bromodomain protein BRD7
Tocco, F. (2008) · OpenstarTs (Univeristy of Trieste https://www.units.it/)
A computational approach to discovering p53 binding sites in the human genome
Lim, J. (2013) · St Andrews Research Repository (St Andrews Research Repository)
Molecular mechanisms of growth suppression by pharmacologically activated p53
Hedström, E. (2009) · Figshare
p53 activity during adenovirus infection
Savelyeva, I. V. (2010) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-366
Hdm2 Small-Molecule Inhibitors For Therapeutic Intervention In B-Cell Lymphoma
Sosin, A. M. (2012) · Human Biology
Studies of mutant p53-targeting small molecules
Zache, N. (2007) · Figshare
Hybrid modeling of p53 and Akt associated gene regulatory network
Bibi, F., & Ahmad, J. (2014) · International Conference on Emerging Technologies · doi:10.1109/icet.2014.7021015
“This takes place both by accelerating p53 degradation through ubiquitination [6] and by blockage of the transcriptional activity of p53 [7].”
BackgroundThe role of microRNAs in the p53 tumor suppressor pathway
Zhang, X. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3171
p53 and DNA damage checkpoint responses in the human prostate
af Hällström, T. (2007)
Small molecule inhibitors of Mdm2 E3 ubiquitin ligase activity
Dickens, M. P. (2011) · UPT. Syiah Kuala University Library (Syiah Kuala University)
Mathematical Models of Some Signaling Pathways Regulating Cell Survival and Death
Zhang, T., Tyson, J. J., Brazhnik, P., Li, L., Mendes, P., Finkielstein, C. V., & Burns, J. A. (2008) · VTechWorks (Virginia Tech)
Increased Radioresistance and Accelerated B Cell LymphomasinMicewithMdmxMutationsthatPrevent
Wang, Y. V., Leblanc, M., Wade, M. R., Jochemsen, A. G., & Wahl, G. M. (2009)
Self-citationMolecular Mechanisms Underlying the Oncogenic Function of SS18 and SSX
D’Arcy, P. (2008) · Figshare
Park, H. (2008) · Rutgers University Community Repository (Rutgers University) · doi:10.7282/t3hq403v
“Stress-induced PI3K family members, such as ATM, ATR, and DNA-PK, may regulate Mdm2 by enhancing autoubiquitination and proteasome-mediated degradation in response to DNA damage (Stommel and Wahl, 2004).”
Stochastic Oscillations in Living Cells
Fakultät, L. (2015)
THE P53-NMNAT2 FEEDBACK REGULATORY LOOP: MECHANISMS UNDERLYING P53 ACTIVATION
Pan, L.-Z. (2012) · Library and Archives Canada (Government of Canada)
PDCD5 interacts with p53 and functions as a regulator of p53 dynamics in the DNA damage responsePreprint
Zhuge, C., Sun, X., Chen, Y., & Lei, J. (2015) · arXiv (Cornell University) · doi:10.48550/arxiv.1503.08274
“First, ATM∗promotes the phosphorylation of p53 on Ser-15 (37) and accelerates the degradation of Mdm2 through phosphorylation (46).”
Backgroundthe ATR-Chk1 Pathway Independently of the Mismatch Repair Pathway
Cui, B., Johnson, S. P., Bullock, N., Ali‐Osman, F., & Friedman, H. S. (2009)
The evolution of p53 network behaviorPreprint
Sivakumar, H., Hespanha, J. P., Roh, K., & Proulx, S. R. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/098376
“…DNA repair, or apoptosis, as soon as DNA damage is detected network includes a core regulation network [23] consisting the proteins MDM 2 [30–32], PTEN , [33, 34], and ARF [35–37] among a host of other upstream, downstream and intermediate species involved in sensing, transduction and…”
BackgroundRegulation of MDM2 and the p53 Family by the NEDD8 Pathway
Watson, I. R. (2011) · TSpace (University of Toronto)
Kim, Y. J., Sung, M., Yu, D. B., Kim, M., Song, J., Song, K., Jung, K., & Choi, Y. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/293068
“MDM2 functions as aubiquitin ligase that targets p53 through the proteasomal degradation pathway, as well as participates in its own auto-degradation to prohibit MDM2 activity, inhibiting p53 during periods of cellular stress (Choi et al., 2018; Stommel and Wahl, 2004).”
BackgroundCellular Senescence and Tumor Promotion
Demaria, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-44870-1_79-1
Oliveira, D. V. C. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.42.2019.tde-18022019-101454
In Vivo Discoveries in MDM2-Mediated p53 Regulation
Tackmann, N. R. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/z7ta-7m83
Characterization of NEK10 Tyrosine Kinase Activity in the Cellular Response to DNA Damage
Haider, N. (2018) · TSpace (University of Toronto)
Oncogenic alterations in the p53 pathway abolish oscillatory competencePreprint
Xiong, L., & Garfinkel, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.09.430245
Friedberg, E. C., Walker, G. C., Siede, W., Wood, R. D., Schultz, R. A., & Ellenberger, T. E. (2014) · ASM Press eBooks · doi:10.1128/9781555816704.ch21
Regulation of the p53 Tumor‐Suppressor Protein by Ubiquitin and Ubiquitin‐Like Molecules
Xirodimas, D. P. (2007) · Wiley eBooks · doi:10.1002/9783527620234.ch2
Gerber, S. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8184
Oscillatory dynamics of p53 pathway in etoposide sensitive and resistant cell lines
Yan, F., Dai, C., & Liu, H. (2022) · Electronic Research Archive · doi:10.3934/era.2022105
Riedel, R. F. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.735180166.793580994
Bang, S., Bhatt, H. C., Chen, Y. Y., & Kurokawa, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101574
Bang, S., Bhatt, H. C., Chen, Y. Y., & Kurokawa, M. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101574-1
Ubiquitin receptors play redundant roles in the proteasomal degradation of the p53 repressor MDM2
Sparks, A., Kelly, C. J., & Saville, M. K. (2022) · FEBS Letters · doi:10.1002/1873-3468.14436
Hu, R., Peng, G., Dai, H., Breuer, E.-K. Y., Stemke‐Hale, K., Li, K., Gonzalez-Angulo, A. M., Mills, G. B., & Lin, S. (2023) · doi:10.1158/0008-5472.c.6502727.v1
Roberts, A. M., Watson, I. R., Evans, A. J., Foster, D. A., Irwin, M. S., & Ohh, M. (2023) · doi:10.1158/0008-5472.c.6500499
Higgins, B. G., Glenn, K., Walz, A., Tovar, C., Filipovic, Z., Hussain, S., Lee, E., Kolinsky, K. D., Tannu, S. A., Adames, V., et al. (2023) · doi:10.1158/1078-0432.c.6523232
Germ cell tumor treatment resistance and liquid biopsy-based microRNA biomarkers
Timmerman, D. M. (2024) · Utrecht University Repository (Utrecht University) · doi:10.33540/2055
Shah, H., Manzoor, A., Ashraf, T., & Dar, A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.09.663887
“…in promoting DNA replication via degradation of PARP1 (Giansanti et al. 2022) , supporting cancer cell growth and survival through targeting of p73 (Stommel and Wahl 2004)(Klein et al. 2021a), and paradoxically inhibiting cell cycle progression via degradation of Cdc25C (Stark and Taylor…”
Parkinson, C., March-Steinman, W., Jose, E., Shanks, L., & Paek, A. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.28.701883
Epigenetic characterization of cellular pliancy in breast cancer
Benhassoun, R. (2024) · theses.fr (ABES) · doi:10.70675/0b1d39b2za3d7z4b26zb4b0zaafa77d5068a
The ubiquitin ligase G2E3 modulates cell proliferation, survival and the DNA damage response
Schmidt, F. (2014) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-4625
Mdm2-p53 Signaling in Tissue Homeostasis and the DNA Damage Response: A Dissertation
Gannon, H. (2012) · eScholarship@UMassChan · doi:10.13028/sfjc-xh51
“Mdm2 destabilization in response to DNA damage has been shown previously (Stommel and Wahl, 2004), and we observed an initial decrease in Mdm2 protein in both Mdm2+/+ and Mdm2A/A tissues.”
BackgroundStructure, Dynamics, and Evolution of the Intrinsically Disordered p53 Transactivation Domain
Borcherds, W. M. (2013) · Digital Commons - University of South Florida (University of South Florida)
Metadata
- Authors
- Stommel, J. M., & Wahl, G. M.
- Affiliations
- Salk Institute for Biological Studies (US)
- Corresponding author
- Wahl, Geoffrey M
- Venue
- The EMBO Journal
- Published
- 2004-03-18
- Volume
- 23
- Issue
- 7
- Pages
- 1547-1556
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC391059
- OpenAlex
- W2091818021
- Cited by
- 386
- References
- 54
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 9 · 2023: 13 · 2022: 10 · 2021: 16 · 2020: 13 · 2019: 19 · 2018: 10 · 2017: 9 · 2016: 8 · 2015: 15 · 2014: 21 · 2013: 13 · 2012: 24
- FWCI
- 11.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Institutes of Health
- National Cancer Institute (CA61449, R01CA061449)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- MDM2, p53 activation, DNA damage response, E3 ubiquitin ligase, p53 stabilization, cell cycle arrest
- MeSH terms
- Animals, Cell Line, Cell Nucleus, Cytoplasm, DNA Damage, Gene Expression Regulation, Humans, Nuclear Proteins, Proto-Oncogene Proteins, Transcription, Genetic, Transcriptional Activation, Tumor Suppressor Protein p53, Phosphatidylinositol 3-Kinases, Active Transport, Cell Nucleus, Proteasome Endopeptidase Complex, Mice, Proto-Oncogene Proteins c-mdm2, Proteasome Inhibitors
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
