ArticleOncogene2002
Phosphorylation of HDM2 by Akt.
Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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
80 citing papers in PubMed, 194 citations in OpenAlex.
- Murine double minute 2 (MDM2) as an appealing target for natural products in cancer treatment.Molecular biology reports · 2026Review
- Maintaining Genome Integrity: Protein Kinases and Phosphatases Orchestrate the Balancing Act of DNA Double-Strand Breaks Repair in Cancer.International journal of molecular sciences · 2023Review
- Understanding the interaction of 14-3-3 proteins with hDMX and hDM2: a structural and biophysical study.The FEBS journal · 2022Article
- Mathematical Modelling of p53 Signalling during DNA Damage Response: A Survey.International journal of molecular sciences · 2021Review
- Preconditioning-Activated AKT Controls Neuronal Tolerance to Ischemia through the MDM2-p53 Pathway.International journal of molecular sciences · 2021Article
- Identification of Hub Genes and Key Pathways Associated with Anti-Biomolecules · 2021Article
- Mdm2 phosphorylation by Akt regulates the p53 response to oxidative stress to promote cell proliferation and tumorigenesis.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Regulation of p53 by the 14-3-3 protein interaction network: new opportunities for drug discovery in cancer.Cell death discovery · 2020Review
- RBM10, a New Regulator of p53.Cells · 2020Review
- MDM2's dual mRNA binding domains co-ordinate its oncogenic and tumour suppressor activities.Nucleic acids research · 2020Article
- Metabolic functions of the tumor suppressor p53: Implications in normal physiology, metabolic disorders, and cancer.Molecular metabolism · 2020Review
- Identification of hub genes and pathways in glioblastoma by bioinformatics analysis.Oncology letters · 2019Article
- Article
- The co-treatment of metformin with flavone synergistically induces apoptosis through inhibition of PI3K/AKT pathway in breast cancer cells.Oncology letters · 2018Article
- PTEN: Tumor Suppressor and Metabolic Regulator.Frontiers in endocrinology · 2018Review
- Modeling the response of a tumor-suppressive network to mitogenic and oncogenic signals.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- FMRP-dependent Mdm2 dephosphorylation is required for MEF2-induced synapse elimination.Human molecular genetics · 2017Article
- PIM1 destabilization activates a p53-dependent response to ribosomal stress in cancer cells.Oncotarget · 2016Article
- Hypoxia-Inducible Factors (HIFs) and Phosphorylation: Impact on Stability, Localization, and Transactivity.Frontiers in cell and developmental biology · 2016Review
- Low expression of phosphatase and tensin homolog in clear‑cell renal cell carcinoma contributes to chemoresistance through activating the Akt/HDM2 signaling pathway.Molecular medicine reports · 2015Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The HDM2 protein is a key regulator of the tumour suppressor, p53. Control of HDM2 function is critical for normal cell proliferation and stress responses, and it is becoming evident that multiple modifications of HDM2 can regulate its function within cells. In this study we show that HDM2 associated with the serine-threonine kinase, Akt, in response to growth factor stimulation of human primary cells. This association was concurrent with phosphorylation of Akt (at Ser 473), and resulted in elevated expression of HDM2 and enhanced nuclear localization. However, analysis of HDM2 proteins mutated at the consensus Akt recognition sites at serines 166 and 186 indicated that modification at these residues was not sufficient for the increased expression of the protein, which was blocked by the PI3 kinase inhibitor LY294002. Tryptic peptide and mutational analyses revealed evidence for an Akt phosphorylation site in HDM2 additional to the two consensus sites.
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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.