The Presenilin Proteins Are Components of Multiple Membrane-bound Complexes That Have Different Biological Activities
Open Access
- 1 July 2004
- journal article
- Published by Elsevier
- Vol. 279 (30), 31329-31336
- https://doi.org/10.1074/jbc.m401548200
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Detergent-Dependent Dissociation of Active γ-Secretase Reveals an Interaction between Pen-2 and PS1-NTF and Offers a Model for Subunit Organization within the ComplexBiochemistry, 2003
- Assembly of the γ-Secretase Complex Involves Early Formation of an Intermediate Subcomplex of Aph-1 and NicastrinJournal of Biological Chemistry, 2003
- The Mechanism of γ-SecretasePublished by Elsevier ,2003
- APH-1 Interacts with Mature and Immature Forms of Presenilins and Nicastrin and May Play a Role in Maturation of Presenilin·Nicastrin ComplexesJournal of Biological Chemistry, 2003
- Presenilin 1 Mutations Activate γ42-Secretase but Reciprocally Inhibit ε-Secretase Cleavage of Amyloid Precursor Protein (APP) and S3-Cleavage of NotchJournal of Biological Chemistry, 2002
- A Novel γ-Secretase Assay Based on Detection of the Putative C-terminal Fragment-γ of Amyloid β Protein PrecursorPublished by Elsevier ,2001
- Carboxyl-terminal Fragments of Alzheimer β-Amyloid Precursor Protein Accumulate in Restricted and Unpredicted Intracellular Compartments in Presenilin 1-deficient CellsJournal of Biological Chemistry, 2000
- The Presenilin 1 Protein Is a Component of a High Molecular Weight Intracellular Complex That Contains β-CateninJournal of Biological Chemistry, 1998
- Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's diseaseNature, 1995
- Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragmentsNature, 1992