ArticleMolecular biology reports2011
Interplay between MDM2, MDMX, Pirh2 and COP1: the negative regulators of p53.
Article in Molecular biology reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 3 of them syntheses that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 3 syntheses or guidelines pooled it, 59 citations in OpenAlex.
- Association of p73 G4C14-to-A4T14 polymorphism with lung cancer risk.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Pooled it
- Combined analysis of the association between p73 G4C14-to-A4T14 polymorphisms and cancer risk.Molecular biology reports · 2012Pooled it
- TP53 codon 72 polymorphism and colorectal cancer susceptibility: a meta-analysis.Molecular biology reports · 2011Pooled it
- Review
- The Role of P53 in Myocardial Ischemia-Reperfusion Injury.Cardiovascular drugs and therapy · 2025Review
- The Impact of Genetic Mutations on the Efficacy of Immunotherapies in Lung Cancer.International journal of molecular sciences · 2024Review
- Targeting the p53 signaling pathway in cancers: Molecular mechanisms and clinical studies.MedComm · 2023Review
- Independent role of caspases and Bik in augmenting influenza A virus replication in airway epithelial cells and mice.Virology journal · 2023Article
- Association between p73 RS2273953 to RS1801173 polymorphism and risk of lung cancer: a meta-analysis of 2,897 cases and 3,317 controls.International journal of clinical and experimental pathology · 2023Article
- Mechanism and Disease Association With a Ubiquitin Conjugating E2 Enzyme: UBE2L3.Frontiers in immunology · 2022Review
- Targeting RFWD2 as an Effective Strategy to Inhibit Cellular Proliferation and Overcome Drug Resistance to Proteasome Inhibitor in Multiple Myeloma.Frontiers in cell and developmental biology · 2021Article
- Amniotic Fluid Cells, Stem Cells, and p53: Can We Stereotype p53 Functions?International journal of molecular sciences · 2019Review
- Tan IIA inhibits H1299 cell viability through the MDM4‑IAP3 signaling pathway.Molecular medicine reports · 2018Article
- Delineating Crosstalk Mechanisms of the Ubiquitin Proteasome System That Regulate Apoptosis.Frontiers in cell and developmental biology · 2018Review
- The Ubiquitin Ligase COP1 Promotes Glioma Cell Proliferation by Preferentially Downregulating Tumor Suppressor p53.Molecular neurobiology · 2017Article
- Essential Roles of E3 Ubiquitin Ligases in p53 Regulation.International journal of molecular sciences · 2017Review
- Targetable genetic features of primary testicular and primary central nervous system lymphomas.Blood · 2016Article
- Role of E3 ubiquitin ligases in gastric cancer.World journal of gastroenterology · 2015Review
- A nanotechnological, molecular-modeling, and immunological approach to study the interaction of the anti-tumorigenic peptide p28 with the p53 family of proteins.International journal of nanomedicine · 2014Article
- The MDM2-p53 pathway revisited.Journal of biomedical research · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MDM2, Pirh2 and COP1 are important E3 ubiquitin ligases, which directly interact with p53 and target p53 for proteasome-mediated degradation. MDMX, the MDM2 homologous protein, inhibits p53-mediated transcription activity. The interplay between MDM2, MDMX, Pirh2 and COP1 has not been reported, except the interaction between MDM2 and MDMX. Here, we reported that there were interactions between these four proteins independently of p53. The protein levels of MDM2, MDMX, Pirh2 and COP1 changed when any two of them were co-transfected. Our data also showed that the integrity of MDM2 RING finger domain was crucial for its ability to elevate the protein levels of COP1 and Pirh2. Any two of these four proteins could inhibit p53-mediated transcriptional activity synergistically. Furthermore, COP1 inhibited MDM2 self-ubiquitination and interfered with MDMX ubiquitination by MDM2. Our results suggest that MDM2, MDMX, Pirh2 and COP1 might inhibit p53 activity synergistically in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.