Amyloidogenic Processing but Not Amyloid Precursor Protein (APP) Intracellular C-terminal Domain Production Requires a Precisely Oriented APP Dimer Assembled by Transmembrane GXXXG Motifs
Open Access
- 1 March 2008
- journal article
- Published by Elsevier BV
- Vol. 283 (12), 7733-7744
- https://doi.org/10.1074/jbc.m707142200
Abstract
No abstract availableThis publication has 60 references indexed in Scilit:
- GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42The EMBO Journal, 2007
- Loss‐of‐function presenilin mutations in Alzheimer diseaseEMBO Reports, 2007
- Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genesEMBO Reports, 2006
- Inhibitors of Amyloid Toxicity Based on β-sheet Packing of Aβ40 and Aβ42Biochemistry, 2006
- TMP21 is a presenilin complex component that modulates γ-secretase but not ɛ-secretase activityNature, 2006
- Homo- and heterodimerization of APP family members promotes intercellular adhesionThe EMBO Journal, 2005
- Presenilin-Dependent Transcriptional Control of the Aβ-Degrading Enzyme Neprilysin by Intracellular Domains of βAPP and APLPNeuron, 2005
- Structural Role of Glycine in Amyloid Fibrils Formed from Transmembrane α-HelicesBiochemistry, 2005
- The GxxxG motif: A framework for transmembrane helix-helix associationJournal of Molecular Biology, 2000
- The Role of Presenilin-1 in the γ-Secretase Cleavage of the Amyloid Precursor Protein of Alzheimer's DiseasePublished by Elsevier BV ,2000