vCLAP, a Caspase-recruitment Domain-containing Protein of Equine Herpesvirus-2, Persistently Activates the IκB Kinases through Oligomerization of IKKγ

This publication has 34 references indexed in Scilit:

• c-E10 Is a Caspase-recruiting Domain-containing Protein That Interacts with Components of Death Receptors Signaling Pathway and Activates Nuclear Factor-κB
  Journal of Biological Chemistry, 1999
• CLAP, a Novel Caspase Recruitment Domain-containing Protein in the Tumor Necrosis Factor Receptor Pathway, Regulates NF-κB Activation and Apoptosis
  Published by Elsevier ,1999
• CIPER, a Novel NF κB-activating Protein Containing a Caspase Recruitment Domain with Homology to Herpesvirus-2 Protein E10
  Published by Elsevier ,1999
• Equine Herpesvirus-2 E10 Gene Product, but Not Its Cellular Homologue, Activates NF-κB Transcription Factor and c-Jun N-terminal Kinase
  Published by Elsevier ,1999
• Anti-apoptotic strategies of lymphotropic viruses
  Published by Elsevier ,1998
• The Multisubunit IκB Kinase Complex Shows Random Sequential Kinetics and Is Activated by the C-terminal Domain of IκBα
  Journal of Biological Chemistry, 1998
• Identification and Characterization of an IκB Kinase
  Cell, 1997
• Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination.
  Proceedings of the National Academy of Sciences, 1995
• Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway.
  Genes & Development, 1995
• Control of IκB-α Proteolysis by Site-Specific, Signal-Induced Phosphorylation
  Science, 1995