MDM2 function.
MDM2, an introduction.
MDM2 and prognosis.
Mdm2 in evolution.
The 3 best characterized are Mdm2-A, Mdm2-B, and Mdm2-C.
The contribution of the acidic domain of MDM2 to p53 and MDM2 stability.
Binding of an inhibitor of the p53/MDM2 interaction to MDM2.
ARF participates in the regulation of mdm2-p53 pathway by mdm2.
The -309 SNP in MDM2 is associated with increased MDM2 transcription.
Expression of MDM2 was significantly reduced by AS-MDM2 in the setting of RT.
The polyubiquitination activity of Mdm2/MdmX is Mdm2-dependent.
The MDM2 gene amplification database.
In no case was MDM2 amplification present.
The mdm2 proto-oncogene.
Hdmx stabilizes Mdm2 and p53.
MDM2: life without p53.
Analysis of the degradation function of Mdm2.
Functions of the MDM2 oncoprotein.
Mdm2: the ups and downs.
The organization and expression of the mdm2 gene.
MDM2 and p53: a question of balance.
Regulation of p53 stability by Mdm2.
[Tumorogenesis and mdm2 protein].
Mdm2-SUMO1: is bigger better?
Mdm2 in the response to radiation.
Mdmx and Mdm2: brothers in arms?
The MDM2-p53 interaction.
Accumulation of MDM2 in pleomorphic xanthoastrocytomas.
p53 ubiquitination: Mdm2 and beyond.
p53-independent functions of MDM2.
The p53 and Mdm2 families in cancer.
Mdm2 in growth signaling and cancer.
Posttranslational modification of MDM2.
Intrasteric regulation of MDM2.
Mdm2: p53's lifesaver?
MDM2 inhibitors for cancer therapy.
No MDM2 gene amplification was detected.
ERK and MDM2 prey on FOXO3a.
The p53 mRNA-Mdm2 interaction.
p53 and Mdm2: an auld alliance.
Targeting MDM2 and MDMX in retinoblastoma.
Mdm2 widens its repertoire.
To confirm it, HEK293 cells were transfected with human HA-MDM2 (+MDM2) or siRNA to MDM2 (-MDM2).
The MDM2-p53 pathway revisited.
Detection of P53 and Mdm2 in vitiligo.
P53 mdm2 inhibitors.
MDM2 as a modifier gene in retinoblastoma.
The molecular dynamics of MDM2.
MDM2 and MDMX in cancer and development.
The evolution of MDM2 family genes.
Resistance acquisition to MDM2 inhibitors.
Cardiac sarcoma with MDM2 amplification.
Splice variants of MDM2 in oncogenesis.
MDM2's social network.
Staining for MDM2 and CDK4 was negative.
p53-independent effects of Mdm2.
The MDM2 gene family.
p300/MDM2 complexes participate in MDM2-mediated p53 degradation.
There is a positive correlation between MDM2 binding to TAFII250 and MDM2 activation of the cyclin A promoter.
No evidence of MDM2 gene amplification or rearrangement accounting for such an increase in MDM2 expression was found.
Mdm2 levels must be regulated tightly because overexpression of mdm2 contributes to tumorigenesis.
p53 mediated death of cells overexpressing MDM2 by an inhibitor of MDM2 interaction with p53.
p76(MDM2) inhibits the ability of p90(MDM2) to destabilize p53.
Cocompartmentalization of p53 and Mdm2 is a major determinant for Mdm2-mediated degradation of p53.
Because of the biological implication of Mdm2 sumoylation, we mapped Ubc9 binding on Mdm2.
Correlation between levels of MDM2 mRNA and MDM2 protein could not be detected in the specimens.
The point mutants, which cannot bind to Mdm2, are not ubiquitinated by Mdm2.
mdm2 gene alterations and mdm2 protein expression in breast carcinomas.
p53 expression was associated neither with mdm2 gene amplification nor with mdm2 immunoreactivity.
MDM2-TBP interaction suggests a p53-independent, transcription regulatory role of MDM2.
Overexpression of Mdm2 in mice reveals a p53-independent role for Mdm2 in tumorigenesis.
Mdm2 induced by activated Raf degrades p53 in the absence of the Mdm2 inhibitor p19ARF.
The mdm2 oncogene was amplified by nonradioactive hybridization of tumor DNA with an mdm2 cDNA probe.
MDM2 is under the transcriptional control of p53, and MDM2 acts as a negative regulator of p53.
MDM2 p90 (usually considered to be the major MDM2 protein) binds to and inactivates P53.
MDM2 facilitates p21 degradation independent of ubiquitination and the E3 ligase function of MDM2.
Several spliced forms of MDM2 have been detected in cells that overexpress MDM2.
E2 significantly decreased the stability of p90(MDM2) and p60(MDM2) in MCF-7.
Mdm2 is itself modified with NEDD8 with very similar characteristics to the autoubiquitination activity of Mdm2.