The C-terminal Tail of Presenilin Regulates Omi/HtrA2 Protease Activity
Open Access
- 1 October 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (44) , 45844-45854
- https://doi.org/10.1074/jbc.m404940200
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Dual Role of BRUCE as an Antiapoptotic IAP and a Chimeric E2/E3 Ubiquitin LigaseMolecular Cell, 2004
- RIPped out by presenilin-dependent γ-secretaseCellular Signalling, 2003
- Inhibitor of Apoptosis Proteins Are Substrates for the Mitochondrial Serine Protease Omi/HtrA2Journal of Biological Chemistry, 2003
- Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosisGenes & Development, 2003
- Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/OmiNature Structural & Molecular Biology, 2002
- HtrA2 Promotes Cell Death through Its Serine Protease Activity and Its Ability to Antagonize Inhibitor of Apoptosis ProteinsJournal of Biological Chemistry, 2002
- Identification of Omi/HtrA2 as a Mitochondrial Apoptotic Serine Protease That Disrupts Inhibitor of Apoptosis Protein-Caspase InteractionJournal of Biological Chemistry, 2002
- X11α and X11β Interact with Presenilin-1 via Their PDZ DomainsMolecular and Cellular Neuroscience, 2000
- Tissue-Specific Splicing of Omi Stress-Regulated Endoprotease Leads to an Inactive Protease with a Modified PDZ MotifGenomics, 2000
- Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ DomainsScience, 1997