The DOI matches its Crossref record; 94 of the 95 references it cites were found in a registry or an index.
MDMX: from bench to bedside
Open accessAbstract
The tumor suppressor protein p53 is negatively regulated by Mdm2, a ubiquitin ligase protein that targets p53 for degradation. Mdmx (also known as Mdm4) is a relative of Mdm2 that was identified on the basis of its ability to physically interact with p53. An increasing body of evidence, including recent genetic studies, suggests that Mdmx also acts as a key negative regulator of p53. Aberrant expression of MDMX could thus contribute to tumor formation. Indeed, MDMX amplification and/or overexpression occurs in several diverse tumors. Strikingly, recent work identifies MDMX as a specific chemotherapeutic target for treatment of retinoblastoma. Specific MDMX antagonists should therefore be developed as a tool to ensure activation of `dormant' p53 activity in tumors that retain wild-type p53.
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In the citing paper
“The oncogene Mdmx is overexpressed in many human malignancies, and together with Mdm2, negatively regulates the p53 tumor suppressor.”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
In the citing paper
“While Mdmx negatively regulates p53, it does so through inhibiting p53 transcriptional activity rather than promoting p53 degradation through ubiquitination, as is the case for Mdm2.24,25”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
In the citing paper
“While it is clear Mdmx regulates p53,25,43”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
In the citing paper
“it is known that Mdmx can regulate p53 independent of Mdm2.25,43”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [25]
In the citing paper
“Genetic analyses demonstrate that the major cellular target (at least in development) for both Mdm2 and Mdmx is p53 [49].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [49]
In the citing paper
“In vitro and in vivo studies show that damage-induced modifications of Mdm2 and Mdmx lead to their destabilization and degradation, reducing their ability to antagonize p53 [49,50].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [49]
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Citations
Cites
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
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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 · cited 1×
“Mdm2 is a RING-finger-containing protein that acts as an E3 ligase, which is essential for ubiquitylation and subsequent degradation of p53 (Haupt et al., 1997; Kubbutat et al., 1997).”
BackgroundLive or let die: the cell's response to p53
Vousden, K. H., & Lü, X. (2002) · Nature reviews. Cancer · doi:10.1038/nrc864 · Cited by 3,231
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“Mdm2-deficient mice die very early in development prior to implantation, whereas mice lacking both p53 and Mdm2 are viable and indistinguishable from mice lacking only p53 (Montes de Oca Luna et al., 1995; Jones et al., 1995).”
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1 of the 95 references couldn’t be matched to a known paper.
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Items 201–234 of 234
Lien, S. (2024) · American Journal of Cancer Research · doi:10.62347/qifc4021 · Cited by 1
Wang, H., Wang, Q., Chen, Y.-H., Chen, X., Zheng, D., Xie, Z., Feng, D.-M., Liu, L., Li, J., & Liu, Y. (2024) · Phytochemistry · doi:10.1016/j.phytochem.2024.114356 · Cited by 1
In silico design of anti-tumor mini-protein targeting MDM2
Zhang, J., Xu, H., Wang, B., Zhang, X., Fu, L., Li, Y., Wu, G., Zhao, Z., Liu, L., Yang, T., et al. (2022) · Chinese Chemical Letters · doi:10.1016/j.cclet.2022.107871 · Cited by 2
Targeting the Cell Cycle and p53 in Combination with BRAF-Directed Therapy
Han, D., & Smalley, K. S. M. (2014) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-1-4939-2143-0_7
Chong, K. H. (2014) · Lincoln University Research Archive (Lincoln University)
Mechanistic studies of APR-246 in leukemia
Ali, D. (2013) · Figshare
Modulation of p53's transcriptional function by small molecules
Nikulenkov, F. (2011) · Figshare
Mdm2 phosphorylations : Characterization and applications
Malmlöf, M. (2007) · Figshare
Increased Radioresistance and Accelerated B Cell LymphomasinMicewithMdmxMutationsthatPrevent
Wang, Y. V., Leblanc, M., Wade, M. R., Jochemsen, A. G., & Wahl, G. M. (2009)
Self-citationAnálise de polimorfismos da família p53 e sua via regulatória como fatores de risco para aneuploidia
Boquett, J. A. (2013) · Americanae (AECID Library)
Induction of p53 Dependent Cellular Senescence Through HdmX Inhibition or YPEL3 Expression
Miller, K. L. (2010) · Journal of Bioresource Management
IN VIVO SIGNIFICANCE OF THE MDM4 AND P73 INTERACTION DURING DEVELOPMENT AND TUMORIGENESIS
Tashakori, M. (2015) · Digital Commons-TMC (Texas Medical Center)
A mechanistic study of functional polymorphisms in the MDM2 gene
Solbakken, M. H. (2008) · NORA - Norwegian Open Research Archives
In Search For New p53 Regulated Genes
Mpagi, M. D. (2008) · Journal of Bioresource Management
Changing the balance in apoptosis: key to enhance cisplatin sensitivity of testicular cancer
Koster, R. (2010) · University of Groningen research database (University of Groningen / Centre for Information Technology)
Husaini, R. (2014) · Bradford Scholars (University of Bradford)
Characterization of NEK10 Tyrosine Kinase Activity in the Cellular Response to DNA Damage
Haider, N. (2018) · TSpace (University of Toronto)
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Moretti, F. (2011) · Springer eBooks · doi:10.1007/978-3-642-16483-5_3583
Hdm2 disrupts HdmX-mediated nuclear export of p53 by sequestering it in nucleus
Ni, Y., Chen, H., Cheng, X., Sun, B., Wu, Z., Zhan, Q., & Zhuang, Z. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.114185
Functional role of long non-coding RNA MALAT1 and HOTAIR in lung cancer
Wen, H.-W., Afzal, A., Chen, G., Saeed, G., An, Y., Sun, S.-C., Rehman, A., Jamil, M. U., Saddozai, U. A. K., Zhang, L., et al. (2026) · Non-coding RNA Research · doi:10.1016/j.ncrna.2026.01.007
Persano, M., Rimini, M., Rosa, A. D., López-Valbuena, D., Rizzato, M. D., Castet, F., Nichetti, F., Castillo, G., Macarulla, T. M., Camera, S., et al. (2026) · Oncoscience · doi:10.18632/oncoscience.674
BindingDB Entry 3460: N-acylpolyamine inhibitors of HDM2 and HDMX binding to p53.
BindingDB (2009) · UC San Diego · doi:10.7270/q2057d90
BindingDB Entry 50040300: An ultrahigh affinity d-peptide antagonist Of MDM2.
BindingDB (2013) · UC San Diego · doi:10.7270/q20p1143
Metadata
- Authors
- Marine, J.-C. W., Dyer, M. A., & Jochemsen, A. G.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- St. Jude Children's Research Hospital (US)
- Leiden University Medical Center (NL)
- Corresponding author
- Marine, Jean-Christophe W.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2007-02-01
- Volume
- 120
- Issue
- 3
- Pages
- 371-378
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2141224144
- Cited by
- 228
- References
- 95
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 5 · 2023: 3 · 2022: 3 · 2021: 8 · 2020: 10 · 2019: 2 · 2018: 8 · 2017: 6 · 2016: 12 · 2015: 10 · 2014: 18 · 2013: 14 · 2012: 21
- FWCI
- 2.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
- 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
- MDMX, MDM2, p53, tumor suppressor regulation, ubiquitin ligase, retinoblastoma, chemotherapeutic target, wild-type p53
- MeSH terms
- Animals, Humans, Models, Biological, Neoplasms, Nuclear Proteins, Proto-Oncogene Proteins, Gene Expression Regulation, Neoplastic, Tumor Suppressor Protein p53, Cell Cycle Proteins
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