Generation of the β-Amyloid Peptide and the Amyloid Precursor Protein C-terminal Fragment γ Are Potentiated by FE65L1
Open Access
- 1 December 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (51), 51100-51107
- https://doi.org/10.1074/jbc.m309561200
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Characterization of an amyloid precursor protein-binding protein Fe65L2 and its novel isoforms lacking phosphotyrosine-interaction domainsBiochemical Journal, 2002
- Calpain Activity Regulates the Cell Surface Distribution of Amyloid Precursor ProteinPublished by Elsevier ,2002
- A Transcriptively Active Complex of APP with Fe65 and Histone Acetyltransferase Tip60Science, 2001
- Cell‐free assays for γ‐secretase activityThe FASEB Journal, 2000
- Modulation of β-Amyloid Precursor Protein Processing by the Low Density Lipoprotein Receptor-related Protein (LRP)Journal of Biological Chemistry, 2000
- Expression of β-Amyloid Precursor Protein-CD3γ Chimeras to Demonstrate the Selective Generation of Amyloid β1–40and Amyloid β1–42 Peptides within Secretory and Endocytic CompartmentsPublished by Elsevier ,1999
- Cleavage of Alzheimer's Amyloid Precursor Protein by α-Secretase Occurs at the Surface of Neuronal CellsBiochemistry, 1999
- Interaction of Cytosolic Adaptor Proteins with Neuronal Apolipoprotein E Receptors and the Amyloid Precursor ProteinJournal of Biological Chemistry, 1998
- γ-Secretase Cleavage Is Distinct from Endoplasmic Reticulum Degradation of the Transmembrane Domain of the Amyloid Precursor ProteinPublished by Elsevier ,1998
- 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