The DOI matches its Crossref record; 269 of the 275 references it cites were found in a registry or an index.
The role of ubiquitin modification in the regulation of p53
Open accessAbstract
The p53 tumor suppressor protein is involved in regulating a wide variety of stress responses, from senescence and apoptosis to more recently discovered roles in allowing adaptation to metabolic and oxidative stress. After 34years of research, significant progress has been made in unraveling the complexity of the p53 network, and it is clear that the regulation of p53 protein stability is critical in the control of p53 activity. This article focuses on our current understanding of how the level and activity of p53 is controlled by this seemingly simple mechanism. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.
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
“MDM2 can cooperate with MDMX (mouse double minute X) to kinetically enhance p53 polyubiquitination, resulting in p53 stability and the occurrence of tumors [11–13].”
From Targeting p53–MDM2 interaction by small-molecule inhibitors: learning from MDM2 inhibitors in clinical trials (2022) · cites this paper as [11]
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
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
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
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
Self-citationMechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
Self-citationSenescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
Restoration of p53 function leads to tumour regression in vivo
Ventura, A., Kirsch, D. G., McLaughlin, M. E., Tuveson, D. A., Grimm, J., Lintault, L., Newman, J., Reczek, E. E., Weissleder, R., & Jacks, T. (2007) · Nature · doi:10.1038/nature05541 · Cited by 1,820
Flagged first, then by citations
6 of the 275 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–171 of 171
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02057-8 · Cited by 17
APR-246 Enhances Colorectal Cancer Sensitivity to Radiotherapy
Xie, X., Fan, C., Luo, B., Zhang, J., Jensen, L. D., Burman, J., Jönsson, C., Ljusberg, A., Larsson, P., Zhao, Z., et al. (2023) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-22-0275 · Cited by 16
Butein activates p53 in hepatocellular carcinoma cells via blocking MDM2-mediated ubiquitination
Zhou, Y., Wang, K., Zhou, N., Huang, T., Zhu, J., & Li, J. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s160119 · Cited by 15
Hu, Y., Jiang, Y., Zhang, Z., Wang, J., Zhang, B., Gong, L., Li, J., Pu, Z., Yang, X., Zou, J., et al. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-1068 · Cited by 14
Zhou, S., Lu, J., Li, Y., Chen, C., Cai, Y., Tan, G., Peng, Z., Zhang, Z., Dong, Z., Kang, T., et al. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0956-3 · Cited by 14
RetractedMechanisms of p53 Functional De-Regulation: Role of the IκB-α/p53 Complex
Carrà, G., Crivellaro, S., Taulli, R., Guerrasio, A., Saglio, G. N., & Morotti, A. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17121997 · Cited by 14
STIP is a critical nuclear scaffolding protein linking USP7 to p53-Mdm2 pathway regulation
Ye, M., Tang, Y.-N., Tang, S.-J., Liu, J., Wu, K., Yao, S., Sun, Y., Zhou, L. J., Deng, T., Chen, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5303 · Cited by 12
Reconstitution of human rRNA gene transcription in mouse cells by complete SL1 complex
Murano, K., Okuwaki, M., Momose, F., Kumakura, M., Ueshima, S., Newbold, R. F., & Nagata, K. (2014) · Journal of Cell Science · doi:10.1242/jcs.146787 · Cited by 14
Mechanisms involved in p53 downregulation by leptin in trophoblastic cells
Toro, A. R., Pérez‐Pérez, A., Corrales-Gutiérrez, I., Sánchez‐Margalet, V., & Varone, C. L. (2015) · Placenta · doi:10.1016/j.placenta.2015.08.017 · Cited by 11
Atherosclerosis and tumor suppressor molecules (Review)
Suzuki, M., Minami, A., NAKANISHI, A., Kobayashi, K., Matsuda, S., Ogura, Y., & Kitagishi, Y. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1866 · Cited by 11
Microchip-Based Structure Determination of Disease-Relevant p53
Solares, M. J., Jonaid, G. M., Luqiu, W. Y., Liang, Y., Evans, M. C., Dearnaley, W. J., Sheng, Z., & Kelly, D. F. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03599 · Cited by 11
Role of BRCA1-associated protein (BRAP) variant in childhood pulmonary arterial hypertension
Nagai, A., Shintani, M., Sato, H., Nakayama, T., Nii, M., Akagawa, H., Furukawa, T., Rana, A. A., Furutani, Y., Inai, K., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0211450 · Cited by 10
High expression of TRIM36 is associated with radiosensitivity in gastric cancer
Man, Z., Chen, T., Zhu, Z., Zhang, H., Ao, L., Xi, L., Zhou, J., & Tang, Z. (2019) · Oncology Letters · doi:10.3892/ol.2019.10122 · Cited by 10
Jung, K. T., & Oh, S. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00782-4 · Cited by 9
HOPS and p53: thick as thieves in life and death
Fazia, M. A. D., Castelli, M., Piobbico, D., Pieroni, S., & Servillo, G. (2020) · Cell Cycle · doi:10.1080/15384101.2020.1838772 · Cited by 9
TRIM21: a multifaceted regulator in cancer
Li, A., Wang, J., & Qu, Y. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1637451 · Cited by 8
Targeting the Ubiquitin–Proteasome System for Cancer
Liu, Z., Lai, J., Ma, Z., Pan, J., Yang, C., & Fu, R. (2025) · MedComm · doi:10.1002/mco2.70391 · Cited by 9
Complementary omics strategies to dissect p53 signaling networks under nutrient stress
Galhuber, M., Michenthaler, H., Heininger, C., Reinisch, I., Nössing, C., Krstić, J., Kupper, N., Moyschewitz, E., Auer, M., Heitzer, E., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04345-8 · Cited by 8
Liang, L., Huang, Y., Chen, L., Shi, Z., Wang, H., Zhang, T., Li, Z., Mi, J., Fan, T., Lu, Y., et al. (2023) · Environmental Toxicology · doi:10.1002/tox.23931 · Cited by 10
Cullin7 in tumor development: a novel potential anti-cancer target
Li, Y., Zang, A., Fu, J., & Jia, Y. (2021) · Neoplasma · doi:10.4149/neo_2021_201207n1324 · Cited by 8
Phenotypical mapping of TP53 unique missense mutations spectrum in human cancers
Malhotra, L., Singh, A., Kaur, P., & Ethayathulla, A. S. (2024) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2024.2435060 · Cited by 7
Ubiquitin, Ubiquitin-Like Proteins, and Proteasome-Mediated Degradation
Dohmen, R. J., Huibregtse, J. M., & Scheffner, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10069-0 · Cited by 8
ARTS and small-molecule ARTS mimetics upregulate p53 levels by promoting the degradation of XIAP
Abbas, R., Hartmann, O., Asiss, D. T., Abbas, R., Kagan, J., Kim, H.-T., Oren, M., Diefenbacher, M. E., Orian, A., & Larisch, S. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01957-2 · Cited by 6
Interferon‐stimulated gene 15 enters posttranslational modifications of p53
Wang, Y., Ding, Q., Lu, Y., Cao, S., Liu, Q., & Zhang, L. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27347 · Cited by 6
Andrews, J. L., Newell, K. A., Matosin, N., Huang, X., & Fernandez, F. (2015) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2015.06.003 · Cited by 6
p53 vs. ISG15: Stop, you’re killing me
Anderson, C. W. (2014) · Cell Cycle · doi:10.4161/cc.29466 · Cited by 6
Studies of ATM Kinase Activity Using Engineered ATM Sensitive to ATP Analogues (ATM-AS)
Enari, M., Matsushima‐Hibiya, Y., Miyazaki, M., & Otomo, R. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6955-5_11 · Cited by 6
Targeting mutant p53 in cancer: from mechanistic insights to therapeutic strategies
Wu, H. H., Leng, S., Eisenstat, D. D., Sergi, C. M., & Leng, R. P. (2026) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-026-00907-x · Cited by 6
Side-stepping the guardian of the genome: current cancer therapeutics targeting mutant p53
Taritsa, I. C., & Fossel, E. T. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1529483 · Cited by 5
Fukui, Y., Hayano, S., Kawanabe, N., Wang, Z., Shimada, A., Saito, M. K., Asaka, I., & Kamioka, H. (2021) · Pathology International · doi:10.1111/pin.13168 · Cited by 5
Calò, M., Bitto, A., Cascio, P. L., Giarratana, F., Altavilla, D., Gervasi, T., Campone, L., Cicero, N., & Licata, P. (2017) · Natural Product Research · doi:10.1080/14786419.2017.1320794 · Cited by 5
Cancer Genetics and Epigenetics in Cancer Risk Assesment
Meiliana, A., Dewi, N. M., & Wijaya, A. (2021) · Molecular and Cellular Biomedical Sciences · doi:10.21705/mcbs.v5i2.198 · Cited by 5
Zhang, Y., Li, X., Gong, Y., Du, D., Chen, H., Liu, L., & Cheng, Z. (2023) · Medicine · doi:10.1097/md.0000000000033834 · Cited by 4
Sahay, O., Barik, G. K., Sharma, T., Pillai, A. D., Rapole, S., & Santra, M. K. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103261 · Cited by 4
The Role of p53 Protein in the Regulation of Neuronal Differentiation
Glazova, M. V. (2016) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-016-0342-6 · Cited by 4
Millado, J. B. H., Hamajima, R., Sugiura, W., Makino, S., Kobayashi, M., & Ikeda, M. (2021) · Journal of insect biotechnology and sericology · doi:10.11416/jibs.90.2_021 · Cited by 3
Hao, Y., Guy, M. M., Liu, Q., Li, R., Mao, Z., Jiang, N., Wang, B., Cui, B., & Zhang, W. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1142938 · Cited by 3
Alshammari, Q. A., Alshammari, S. O., Alshammari, A., Alfarhan, M., & Baali, F. H. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03564-z · Cited by 3
Calò, M., Licata, P., Bitto, A., Cascio, P. L., Giarratana, F., & Altavilla, D. (2017) · Experimental and Toxicologic Pathology · doi:10.1016/j.etp.2017.04.005 · Cited by 2
A Systematic Review on Leukemogenesis: Is there any Pitfall in Human Health
Gupta, S., Nigam, N., Sinha, S., Upadhyay, K., Rawat, N., Kumar, P. M., Verma, S., & Kushwaha, R. (2023) · Family Medicine and Primary Care Open Access · doi:10.29011/2688-7460.100229 · Cited by 2
Taillandier, D. (2021) · Biologie Aujourd hui · doi:10.1051/jbio/2021006 · Cited by 2
Xiao, G., Huang, X., Huang, T., Chen, Z., Huang, Y., Huang, R., & Wang, X. (2024) · Annals of Hepatology · doi:10.1016/j.aohep.2024.101543 · Cited by 1
Ferroptosis as a therapeutic vulnerability in MDM2 inhibition in dedifferentiated liposarcoma
Yen, C., Chen, P., Chen, S., Wu, W., Yen, C., Lin, Y., Wu, P., Chen, C.-M., Wang, J., Chao, T., et al. (2025) · Oncology Letters · doi:10.3892/ol.2025.15015 · Cited by 1
Kotadiya, D. D., Thakur, P. S., Nair, R., Prajapati, A., Patel, D. A., Patel, S. S., Kumari, S., Priya, K., & Patel, H. D. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.109948 · Cited by 1
Autophagy in cancer: friend or foe?
Vega-Rubín-de-Celis, S. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822003-0.00009-7 · Cited by 1
Molecular Mechanisms of Gap Junction Regulation by the E3 Ubiquitin Ligase WWP1
Abreha, M. H. (2014) · Scholar Commons (University of South Carolina)
Deubiquitinating Enzymes as Novel Targets for Cancer Therapies
Baek, K., Lim, K., & Park, J.-J. (2014) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-319-06752-0_15
Small molecules that affect the p53 pathway and their potential use in the treatment of cancer
Sachweh, M. C. C. (2014) · Figshare
Panorama dos nutlins como protótipo para terapia do câncer
Rodrigues, C. R., da Cunha, L. C., & Guillo, L. A. (2014) · Americanae (AECID Library)
Huang, S., Cao, B., Wang, J., Zhang, Y.-W., Ledet, E. M., Sartor, O. A., Xiong, Y., Zeng, S. X., & Lu, H. (2021) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjab078
Complementary Omics Strategies to Dissect p53 Signaling Networks Under Nutrient StressPreprint
Galhuber, M., Michenthaler, H., Heininger, C., Reinisch, I., Nössing, C., Krstić, J., Kupper, N., Moyschewitz, E., Auer, M., Heitzer, E., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1224764/v1
The Role of miRNAs and Alternative Polyadenylation in Modulating the P53 Response
Browning, J. W. L. (2018) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2018-13260
Hariharan, H. P., Mitra, A., Panicker, S., & Ramalingam, S. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815136500123020010
Hassan, F. M., Alsultan, A. A., Albuali, W. H., Bubshait, D., Abass, E. M., Elbasheer, M., Shaikh, S. S., Alkhanbashi, A., & Alzahrani, F. (2025) · Electronic Journal of General Medicine · doi:10.29333/ejgm/17525
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128586
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128571
Ding, L., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128565
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128583
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128574
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128580
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128577
Ding, L. J., Zhang, Z., Zhao, C., Chen, L., Chen, Z., Zhang, J., Liu, Y., Nie, Y., He, Y., Liao, K., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15128568
Protein Neddylation Beyond Tumor Cells is a Vital Modulator of Anticancer Immunity
Xu, M., Liu, W., Liu, F., & Xie, P. (2026) · Phenomics · doi:10.1007/s43657-025-00233-w
Host-pathogens interactions during RSV / S. pneumoniae infection immune response and p53 pathway
Machado, D. B. B. (2017) · theses.fr (ABES) · doi:10.70675/3b4a9038z62abz41fcz8fa8zd0dbd4dcbfe4
Assemblage et dysfonctionnement de ribosomes mammifères : une étude structure-fonction par cryo-MET
Plassart, L. (2022) · theses.fr (ABES) · doi:10.70675/9d3faeb7z7e31z499fza127z80b1e9d7503c
Determinants of C16-Ceramide Binding to p53
Childress, M. S., Jeffries, K. A., Krupenko, S. A., & Krupenko, N. I. (2026) · Biomolecules · doi:10.3390/biom16091343
BindingDB (2025) · UC San Diego · doi:10.7270/q2571hks
BindingDB Entry 50002425: Identification of small-molecule inhibitors of USP2a.
BindingDB (2020) · UC San Diego · doi:10.7270/q28g8p98
Metadata
- Authors
- Hock, A. K., & Vousden, K. H.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- Corresponding author
- Vousden, Karen H.
- ORCID
- Vousden, Karen H.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 1843
- Issue
- 1
- Pages
- 137-149
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2062976534
- Cited by
- 168
- References
- 275
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 12 · 2021: 27 · 2020: 9 · 2019: 9 · 2018: 15 · 2017: 17 · 2016: 18 · 2015: 19 · 2014: 15
- FWCI
- 1.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- CR-UK
- 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
- p53, ubiquitin modification, protein stability, ubiquitin-proteasome system, tumor suppressor regulation, apoptosis, senescence, oxidative stress, metabolic stress, stress response
- MeSH terms
- Animals, Humans, Protein Processing, Post-Translational, Transcriptional Activation, Tumor Suppressor Protein p53, Ubiquitin, Proto-Oncogene Proteins c-mdm2, Ubiquitination, Protein Stability
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