Functional Implications of the Presenilin Dimerization
Open Access
- 1 August 2004
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 279 (35), 36519-36529
- https://doi.org/10.1074/jbc.m404832200
Abstract
No abstract availableKeywords
This publication has 71 references indexed in Scilit:
- Signal Peptide Peptidase Forms a Homodimer That Is Labeled by an Active Site-directed γ-Secretase InhibitorPublished by Elsevier BV ,2004
- Conserved “PAL” sequence in presenilins is essential for γ-secretase activity, but not required for formation or stabilization of γ-secretase complexesNeurobiology of Disease, 2004
- Activated Notch1 associates with a presenilin‐1/γ‐secretase docking siteJournal of Neurochemistry, 2003
- Catalytic Site-Directed γ-Secretase Complex Inhibitors Do Not Discriminate Pharmacologically between Notch S3 and β-APP CleavagesBiochemistry, 2003
- The Mechanism of γ-Secretase Activities through High Molecular Weight Complex Formation of Presenilins Is Conserved inDrosophila melanogaster and MammalsJournal of Biological Chemistry, 2002
- APP Processing and Synaptic Plasticity in Presenilin-1 Conditional Knockout MiceNeuron, 2001
- Distinct Intramembrane Cleavage of the β-Amyloid Precursor Protein Family Resembling γ-Secretase-like Cleavage of NotchJournal of Biological Chemistry, 2001
- The First Proline of PALP Motif at the C Terminus of Presenilins Is Obligatory for Stabilization, Complex Formation, and γ-Secretase Activities of PresenilinsPublished by Elsevier BV ,2001
- Regulated Intramembrane ProteolysisCell, 2000
- Effect of site‐directed mutagenesis on conserved positions of Drosophila alcohol dehydrogenaseFEBS Letters, 1993