Autors:

CiteWeb id: 19920000120

CiteWeb score: 3868

DOI: 10.1016/0092-8674(92)90644-R

A cellular phosphoprotein with an apparent molecular mass of 90 kd (p90) that forms a complex with both mutant and wild-type p53 protein has been characterized, purified, and identified. The protein was identified as a product of the murine double minute 2 gene (mdm-2). The mdm-2 gene enhances the tumorigenic potential of cells when it is overexpressed and encodes a putative transcription factor. To determine if mdm-2 could modulate p53 transactivation, a p53-responsive element from the muscle creatine kinase gene was employed. A wild-type p53-expressing plasmid enhanced the expression of the p53-responsive element when cotransfected into cells that contain no endogenous p53. When a cosmid expressing mdm-2 was transfected with this p53-expressing plasmid, the transactivation of the p53-responsive element was inhibited. Thus, a product of the mdm-2 oncogene forms a tight complex with the p53 protein, and the mdm-2 oncogene can inhibit p53-mediated transactivation.

The publication "The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation" is placed in the Top 10000 of the best publications in CiteWeb. Also in the category Biology it is included to the Top 1000. Additionally, the publicaiton "The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation" is placed in the Top 1000 among other scientific works published in 1992.
Links to full text of the publication: