The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
MDMX: a novel p53‐binding protein with some functional properties of MDM2.
Open accessAbstract
Here we report the isolation of a cDNA encoding a new p53-associating protein. This new protein has been called MDMX on the basis of its structural similarity to MDM2, which is especially notable in the p53-binding domain. In addition, the putative metal binding domains in the C-terminal part of MDM2 are completely conserved in MDMX. The middle part of the MDMX and MDM2 proteins shows a low degree of conservation. We can show by co-immunoprecipitation that the MDMX protein interacts specifically with p53 in vivo. This interaction probably occurs with the N-terminal part of p53, because the activity of the transcription activation domain of p53 was inhibited by co-transfection of MDMX. Northern blotting showed that MDMX, like MDM2, is expressed in all tissues tested, and that several mRNAs for MDMX can be detected. Interestingly, the level of MDMX mRNA is unchanged after UV irradiation, in contrast to MDM2 transcription. This observation suggests that MDMX may be a differently regulated modifier of p53 activity in comparison with MDM2. Our study indicates that at least one additional member of the MDM protein family exists which can modulate p53 function.
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Metadata
- Authors
- Shvarts, A., Steegenga, W. T., Riteco, N., van Laar, T., Dekker, P., Bazuine, M., van Ham, R. C., van der Houven van Oordt, W., Hateboer, G., van der Eb, A. J., & Jochemsen, A. G.
- Affiliations
- Leiden University (NL)
- Venue
- The EMBO Journal
- Published
- 1996-10-01
- Volume
- 15
- Issue
- 19
- Pages
- 5349-5357
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC452278
- OpenAlex
- W1592021885
- Cited by
- 648
- References
- 59
- Citations by year
- 2026: 14 · 2025: 13 · 2024: 14 · 2023: 23 · 2022: 26 · 2021: 20 · 2020: 26 · 2019: 21 · 2018: 19 · 2017: 24 · 2016: 39 · 2015: 16 · 2014: 40 · 2013: 25 · 2012: 36
- FWCI
- 4.05
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- MDMX, MDM2, p53, p53-binding protein, protein-protein interaction, metal-binding domain, p53 regulation, cDNA cloning
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cell Line, Cloning, Molecular, Humans, Molecular Sequence Data, Nuclear Proteins, Organ Specificity, Protein Binding, Proto-Oncogene Proteins, Recombinant Fusion Proteins, RNA, Messenger, Transcription, Genetic, Transfection, Ultraviolet Rays, Transcriptional Activation, Tumor Suppressor Protein p53, Sequence Homology, Amino Acid, Sequence Analysis, DNA, DNA, Complementary, Mice, Proto-Oncogene Proteins c-mdm2
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