Presenilin-1, Nicastrin, Amyloid Precursor Protein, and γ-Secretase Activity Are Co-localized in the Lysosomal Membrane
Open Access
- 1 July 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (29) , 26687-26694
- https://doi.org/10.1074/jbc.m304009200
Abstract
No abstract availableKeywords
This publication has 88 references indexed in Scilit:
- Plasma Membrane Repair Is Mediated by Ca2+-Regulated Exocytosis of LysosomesCell, 2001
- Biochemical Characterization of the γ-Secretase Activity That Produces β-Amyloid PeptidesBiochemistry, 2001
- Endogenous Presenilin-1 Targets to Endocytic Rather Than Biosynthetic CompartmentsMolecular and Cellular Neuroscience, 2000
- Subcellular Localization of Presenilins: Association with a Unique Membrane Pool in Cultured CellsNeurobiology of Disease, 2000
- Regulated Intramembrane ProteolysisCell, 2000
- Distinct Secretases, a Cysteine Protease and a Serine Protease, Generate the C Termini of Amyloid β‐Proteins Aβ1‐40 and Aβ1‐42, RespectivelyJournal of Neurochemistry, 1999
- Presenilin 1 Regulates the Processing of β-Amyloid Precursor Protein C-Terminal Fragments and the Generation of Amyloid β-Protein in Endoplasmic Reticulum and GolgiBiochemistry, 1998
- Phagocytosis by Rat Liver: Relationships between Phagosomes and LysosomesBiochemical and Biophysical Research Communications, 1996
- Elevated Levels of the Endosomal‐Lysosomal Proteinase Cathepsin D in Cerebrospinal Fluid in Alzheimer DiseaseJournal of Neurochemistry, 1995
- Proteases and proteolysis in the lysosomeCellular and Molecular Life Sciences, 1992