Presenilin-dependent Intramembrane Proteolysis of CD44 Leads to the Liberation of Its Intracellular Domain and the Secretion of an Aβ-like Peptide
Open Access
- 1 November 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (47), 44754-44759
- https://doi.org/10.1074/jbc.m206872200
Abstract
No abstract availableKeywords
This publication has 62 references indexed in Scilit:
- A RIP Tide in Neuronal Signal TransductionNeuron, 2002
- Regulated Intracellular Ligand Transport and Proteolysis Control EGF Signal Activation in DrosophilaCell, 2001
- Drosophila Rhomboid-1 Defines a Family of Putative Intramembrane Serine ProteasesCell, 2001
- A Portrait of Alzheimer Secretases--New Features and Familiar FacesScience, 2001
- Intramembrane proteolysis by presenilinsNature Reviews Molecular Cell Biology, 2000
- Aβ-Generating EnzymesNeuron, 2000
- Total inactivation of γ–secretase activity in presenilin-deficient embryonic stem cellsNature Cell Biology, 2000
- Presenilins are required for γ-secretase cleavage of β-APP and transmembrane cleavage of Notch-1Nature Cell Biology, 2000
- Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1Nature, 2000
- Regulated Intramembrane ProteolysisCell, 2000