Presenilins were first discovered as sites of missense mutations responsible for early-onset
Alzheimer disease (AD). The encoded multipass membrane proteins were subsequently …

Presenilin-1 (PSEN1) has been verified as an important causative factor for early onset
Alzheimer's disease (EOAD). PSEN1 is a part of γ-secretase, and in addition to amyloid …

The γ-secretase complex, comprising presenilin 1 (PS1), PEN-2, APH-1 and nicastrin, is a
membrane-embedded protease that controls a number of important cellular functions …

One of the most critical pathological features of Alzheimer's disease (AD) is the
accumulation of β-amyloid (Aβ) peptides that form extracellular senile plaques in the brain …

J. Neurochem.(2011) 117, 779–796. Abstract Regulated intramembrane proteolysis (RIP)
controls the communication between cells and the extracellular environment. RIP is …

γ-Secretase is a promiscuous protease that cleaves bitopic membrane proteins within the
lipid bilayer. Elucidating both the mechanistic basis of γ-secretase proteolysis and the …

γ-Secretase is a membrane-embedded protease complex, with presenilin as the catalytic
component containing two transmembrane aspartates in the active site. With more than 90 …

Membrane proteins are constantly being trafficked in cells and the relevant proteins in
Alzheimer's disease (AD), such as the amyloid precursor protein (APP) and its processing …

Presenilin and signal peptide peptidase (SPP) are intramembrane aspartyl proteases that
regulate important biological functions in eukaryotes. Mechanistic understanding of …

Abstract γ-Secretase catalyzes the final cleavage of the β-amyloid precursor protein to
generate amyloid-β peptide, the principal component of amyloid plaques in the brains of …