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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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Cites
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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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