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We report that MDM2, a negative regulator of p53, can bind to EBNA‐5. Using GST pull‐down assay, immunoprecipitation, surface plasmon resonance and immunostaining of lymphoblastoid cells, we found that trimolecular complexes are formed between EBNA‐5, MDM2 and p53, where MDM2 serves as a bridge. The EBNA‐5 binding to MDM2 counteracted destabilizing effect of the latter on the p53. In ubiquitination...
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