Human mdm2 Mediates Multiple Mono-ubiquitination of p53 by a Mechanism Requiring Enzyme Isomerization
Open Access
- 1 August 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (33) , 31357-31367
- https://doi.org/10.1074/jbc.m011517200
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- Ubiquitin in chainsPublished by Elsevier ,2000
- Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligaseOncogene, 2000
- The SCFHOS/β-TRCP-ROC1 E3 Ubiquitin Ligase Utilizes Two Distinct Domains within CUL1 for Substrate Targeting and Ubiquitin LigationMolecular and Cellular Biology, 2000
- Recognition of the polyubiquitin proteolytic signalThe EMBO Journal, 2000
- Regulation of p53 in response to DNA damageOncogene, 1999
- Ubiquitin pathway: Another link in the polyubiquitin chain?Current Biology, 1999
- Regulation of p53 stability by Mdm2Nature, 1997
- Mdm2 promotes the rapid degradation of p53Nature, 1997
- Does this have a familiar RING?Trends in Biochemical Sciences, 1996
- A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase.Proceedings of the National Academy of Sciences, 1995