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文献和实验The Phosphorylation of Presenilin Proteins
The phosphorylation of presenilin (PS) proteins was initially analyzed in cultured cells overexpressing the respective proteins. These studies revealed that the homologous PS proteins are differentially phosphorylated in vivo. Fulllength PS2
Quantifying Aβ1–40 and Aβ1–42 Using Sandwich-ELISA
with autosomal penetrance (reviewed in ref . 1 ). Several of these FAD-associated APP mutations, as well as FAD-associated mutations in the presenilin 1 (PS1) and presenilin 2 (PS2) genes, lead to an increase in the production of Aβ1 –42 relative to Aβ1 _40
Interaction of the Presenilins with the Amyloid Precursor Protein (APP)
The genes encoding presenilin-1 (PS1 ) and presenilin-2 (PS2 ) were identified as the genes that harbour mutations that cause more than 60% of early onset familial Alzheimer’s disease cases (FAD) (1 -3 ). So far, more than 40 missense mutations
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