Regulation of the transcriptional response to the tumor suppressor p53 occurs at many
levels, including control of its transcriptional activity, and of its stability and concentration …

HDM2 is a ubiquitin E3 ligase that is a key negative regulator of the tumor suppressor p53.
Here, we report the determination of the solution structure of the C4 zinc finger domain of …

HDM2 is a negative regulator of p53 that inhibits its transcriptional activity and subjects it to
degradation by an E3 ligase activity. The primary binding site for HDM2 on p53 is located in …

The stability of the p53 tumor suppressor protein is critically regulated by the Hdm2 and
Hdmx proteins. Hdm2 protein levels are auto-regulated by the self-ubiquitination activity of …

The p53 regulatory network is critically involved in preventing the initiation of cancer. In
unstressed cells, p53 is maintained at low levels and is largely inactive, mainly through the …

The RING finger proteins HdmX and Hdm2 share significant structural and functional
similarity. Hdm2 is a member of the RING finger family of ubiquitin-protein ligases E3 and …

The related RING domain proteins MdmX and Mdm2 are best known for their role as
negative regulators of the tumor suppressor p53. However, although Mdm2 functions as a …

The Hdmx gene product is related to the Hdm2 oncoprotein, both of which interact with and
regulate p53 stability and function. Like Hdm2, Hdmx is able to inhibit p53 transactivation; …

The oncoprotein hdm2 ubiquitinates p53, resulting in the rapid degradation of p53 through
the ubiquitin (Ub)–proteasome pathway. Hdm2-mediated destabilization and inactivation of …

Mdm2, a key negative regulator of the p53 tumor suppressor, is a RING‐type E3 ubiquitin
ligase. The Mdm2 RING domain can be biochemically fractionated into two discrete species …