Multiple interacting domains contribute to p14ARF mediated inhibition of MDM2
- 27 June 2002
- journal article
- Published by Springer Nature in Oncogene
- Vol. 21 (29) , 4498-4507
Abstract
Oncogene is one of the world’s leading cancer journals. It is published weekly and covers all aspects of the structure and function of Oncogenes. Oncogene also publishes 8 Reviews issues a year, on a broad range of topics.Keywords
This publication has 34 references indexed in Scilit:
- Defining the molecular basis of Arf and Hdm2 interactionsJournal of Molecular Biology, 2001
- A melanoma-associated germline mutation in exon 1β inactivates p14ARFOncogene, 2001
- Human ARF binds E2F1 and inhibits its transcriptional activityOncogene, 2001
- Solution Structure of the p53 Regulatory Domain of the p19Arf Tumor Suppressor ProteinBiochemistry, 2001
- Two arginine rich domains in the p14ARF tumour suppressor mediate nucleolar localizationOncogene, 2000
- An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivoOncogene, 2000
- Immunolocalization of Human p14ARF to the Granular Component of the Interphase NucleolusExperimental Cell Research, 2000
- Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53The EMBO Journal, 1999
- Regulation of p53 stability by Mdm2Nature, 1997
- Mdm2 promotes the rapid degradation of p53Nature, 1997