The ubiquitin–proteasome pathway in thymocyte apoptosis: caspase-dependent processing of the deubiquitinating enzyme USP7 (HAUSP)
- 1 November 2002
- journal article
- Published by Elsevier in Molecular Immunology
- Vol. 39 (7-8) , 431-441
- https://doi.org/10.1016/s0161-5890(02)00123-2
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilizationNature, 2002
- A Diverse Family of Proteins Containing Tumor Necrosis Factor Receptor-associated Factor DomainsJournal of Biological Chemistry, 2001
- Ubiquitin Protein Ligase Activity of IAPs and Their Degradation in Proteasomes in Response to Apoptotic StimuliScience, 2000
- Proteasome activation as a critical event of thymocyte apoptosisCell Death & Differentiation, 2000
- Deubiquitinating Enzymes: Their Diversity and Emerging RolesBiochemical and Biophysical Research Communications, 1999
- SELECTION OF THE T CELL REPERTOIREAnnual Review of Immunology, 1999
- Emerging roles of caspase-3 in apoptosisCell Death & Differentiation, 1999
- Cellular interactions in the thymus regulate the protein kinase C signaling pathwayEuropean Journal of Immunology, 1998
- A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory proteinThe EMBO Journal, 1997
- Flow‐cytometric analysis of apoptotic and nonapoptotic T‐cell receptor‐transgenic thymocytes following in vitro presentation of antigenCytometry, 1994