c-MIR, a Human E3 Ubiquitin Ligase, Is a Functional Homolog of Herpesvirus Proteins MIR1 and MIR2 and Has Similar Activity
Open Access
- 1 April 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (17) , 14657-14668
- https://doi.org/10.1074/jbc.m211285200
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradationThe EMBO Journal, 2002
- The PHD Domain of MEKK1 Acts as an E3 Ubiquitin Ligase and Mediates Ubiquitination and Degradation of ERK1/2Molecular Cell, 2002
- Perinatal Blockade of B7-1 and B7-2 Inhibits Clonal Deletion of Highly Pathogenic Autoreactive T CellsThe Journal of Experimental Medicine, 2002
- Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complexNature Cell Biology, 2002
- Costimulation and endogenous MHC ligands contribute to T cell recognitionNature Immunology, 2001
- Molecular piracy of Kaposi's sarcoma associated herpesvirusCytokine & Growth Factor Reviews, 2001
- A viral protein that selectively downregulates ICAM-1 and B7-2 and modulates T cell costimulationJournal of Clinical Investigation, 2001
- Complexities of CD28/B7: CTLA-4 Costimulatory Pathways in Autoimmunity and TransplantationAnnual Review of Immunology, 2001
- Solution structure of the PHD domain from the KAP-1 corepressor: structural determinants for PHD, RING and LIM zinc-binding domainsThe EMBO Journal, 2001
- RING Finger ProteinsCell, 2000