Alzheimer's disease (AD) is caused by synaptic and neuronal loss in the brain. One of the
characteristic hallmarks of AD is senile plaques containing amyloid β-peptide (Aβ). Aβ is …

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 …

γ-Secretase is a membrane-embedded proteolytic complex composed of presenilin and
three other subunits. The γ-secretase complex generates the amyloid β-peptide of …

Abstract Twenty years ago, Wolfe, Xia, and Selkoe identified two aspartate residues in
Alzheimer's presenilin protein that constitute the active site of the γ-secretase complex …

J. Neurochem.(2012) 120 (Suppl. 1), 89–98. Abstract γ‐Secretase is a membrane
embedded aspartyl protease complex with presenilin as the catalytic component. Along with …

γ-Secretase mediates the final proteolytic cleavage, which liberates amyloid β-peptide (Aβ),
the major component of senile plaques in the brains of Alzheimer disease patients …

The 4-kDa amyloid β-peptide (Aβ) is strongly implicated the pathogenesis of Alzheimer's
disease (AD), and this peptide is cut out of the amyloid β-protein precursor (APP) by the …

Aims: Drugs currently used for the treatment of Alzheimer's disease (AD) partially stabilize
patients' symptoms without modifying disease progression. Brain accumulation of oligomeric …

Genetic and experimental evidence points to amyloid-β (Aβ) peptide as the culprit in
Alzheimer's disease pathogenesis. This protein fragment abnormally accumulates in the …

γ-Secretase is an aspartyl intramembranal protease composed of presenilin, Nicastrin,
Aph1, and Pen2 with 19 transmembrane domains. γ-Secretase cleaves the amyloid …