Alzheimer's disease (AD) is the most common form of dementia and is characterized
pathologically by the accumulation of β‐amyloid (Aβ) plaques and neurofibrillary tangles in …

Processing of amyloid beta precursor protein (APP) into amyloid-beta peptide (Aβ) by β-
secretase and γ-secretase complex is at the heart of the pathogenesis of Alzheimer's …

The age-dependent deposition of amyloid-β peptides, derived from amyloid precursor
protein (APP), is a neuropathological hallmark of Alzheimer's disease (AD). Despite age …

A complex composed of presenilin (PS), nicastrin, PEN-2, and APH-1 is absolutely required
for γ-secretase activity in vivo. Evidence has emerged to suggest a role for PS as the …

Presenilin (PSEN)/γ-secretase is a protease complex responsible for the proteolytic
processing of numerous substrates. These substrates include the amyloid precursor protein …

Megalin, a member of the low density lipoprotein receptor gene family, is required for
efficient protein absorption in the proximal tubule. Recent studies have shown that the low …

Abstract γ‐Secretase cleavage, mediated by a complex of presenilin, presenilin enhancer
(Pen‐2), nicastrin, and Aph‐1, is the final proteolytic step in generating amyloid β protein …

Presenilins (PSs) are the catalytic core of γ-secretase complex. However, the mechanism of
FAD-associated PS mutations in AD pathogenesis still remains elusive. Here we review the …

Presenilin (PS1 or PS2) is the catalytic component of the γ-secretase complex, which
mediates the final proteolytic processing step leading to the Alzheimer's disease (AD) …

Abstract β‐Amyloid cleaving enzyme‐1 (BACE1) has become a significant target for the
therapy of Alzheimer's disease. After the discovery of the first non‐peptidomimetic β …