The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation
Open Access
- 1 July 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (29) , 27443-27448
- https://doi.org/10.1074/jbc.m501574200
Abstract
No abstract availableKeywords
This publication has 68 references indexed in Scilit:
- The ubiquitin ligase COP1 is a critical negative regulator of p53Nature, 2004
- Expansion of Protein Interaction Maps by Phage Peptide Display Using MDM2 as a Prototypical Conformationally Flexible Target ProteinJournal of Molecular Biology, 2004
- Pirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 DegradationCell, 2003
- Ubiquitylation of BAG-1 Suggests a Novel Regulatory Mechanism during the Sorting of Chaperone Substrates to the ProteasomeJournal of Biological Chemistry, 2002
- Live or let die: the cell's response to p53Nature Reviews Cancer, 2002
- Regulation of p53 stability by Mdm2Nature, 1997
- Mdm2 promotes the rapid degradation of p53Nature, 1997
- Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic MutationsScience, 1994
- Mutant conformation of p53: Precise epitope mapping using a filamentous phage epitope libraryJournal of Molecular Biology, 1992
- Hsp70 binds specifically to a peptide derived from the highly conserved domain (I) region of P53Biochemical and Biophysical Research Communications, 1992