The Alzheimer's disease (AD)-associated amyloid-β protein precursor (AβPP) is cleaved by
α-, β-, and presenilin (PS)/γ-secretases through sequential regulated proteolysis. These …

Calcium modulates many neural processes, including synaptic plasticity and apoptosis.
Dysregulation of intracellular calcium signalling has been implicated in the pathogenesis of …

Amyloid-β precursor protein (APP), a widely expressed cell-surface protein, is cleaved in the
transmembrane region by γ-secretase. γ-Cleavage of APP produces the extracellular …

Abstract β-Amyloid precursor protein (APP) and its cleaved products are strongly implicated
in Alzheimer's disease (AD). Endosomes are highly active APP processing sites, and …

The β-amyloid precursor protein (APP) is a ubiquitous receptor-like molecule without a
known function. However, the recent recognition that APP and Notch undergo highly similar …

The physiological functions of the beta-amyloid precursor protein (APP) may include nuclear
signaling. To characterize the role of the APP adaptor proteins Fe65, Jip1b, X11α (MINT1) …

Proteolytic processing of the transmembrane domain of the amyloid precursor protein (APP)
is a key component of Alzheimer's disease pathogenesis. Using C-terminally tagged APP …

Since the discovery of the amyloid precursor protein (APP) in 1987, extensive research has
been conducted analyzing the APP-derived β-amyloid (Aβ) which is found in massive …

Amyloid-β precursor protein (APP) forms a transcriptionally active complex with the adaptor
protein Fe65 and the histone acetyltransferase Tip60, but the mechanism of transcriptional …

The amyloid-β precursor protein is proteolytically cleaved by secretases, resulting in a series
of fragments, including the amyloid-β peptide of Alzheimer's disease. The amyloid precursor …