CARP is a novel caspase recruitment domain containing pro-apoptotic protein
- 1 May 2002
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 293 (5) , 1396-1404
- https://doi.org/10.1016/s0006-291x(02)00379-0
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Bcl10 Is a Positive Regulator of Antigen Receptor–Induced Activation of NF-κ B and Neural Tube ClosureCell, 2001
- CARD9 Is a Novel Caspase Recruitment Domain-containing Protein That Interacts With BCL10/CLAP and Activates NF-κBJournal of Biological Chemistry, 2000
- HCaRG, a Novel Calcium-regulated Gene Coding for a Nuclear Protein, Is Potentially Involved in the Regulation of Cell ProliferationJournal of Biological Chemistry, 2000
- An Induced Proximity Model for NF-κB Activation in the Nod1/RICK and RIP Signaling PathwaysJournal of Biological Chemistry, 2000
- Cypher, a Striated Muscle-restricted PDZ and LIM Domain-containing Protein, Binds to α-Actinin-2 and Protein Kinase CJournal of Biological Chemistry, 1999
- c-E10 Is a Caspase-recruiting Domain-containing Protein That Interacts with Components of Death Receptors Signaling Pathway and Activates Nuclear Factor-κBJournal of Biological Chemistry, 1999
- CLAP, a Novel Caspase Recruitment Domain-containing Protein in the Tumor Necrosis Factor Receptor Pathway, Regulates NF-κB Activation and ApoptosisPublished by Elsevier ,1999
- Nod1, an Apaf-1-like Activator of Caspase-9 and Nuclear Factor-κBJournal of Biological Chemistry, 1999
- RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell deathCell, 1995
- FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosisCell, 1995