β‐secretase‐cleaved amyloid precursor protein in Alzheimer brain: a morphologic study [PDF]
Abstractβ‐amyloid (Aβ) is the main constituent of senile plaques seen in Alzheimer's disease. Aβ is derived from the amyloid precursor protein (APP) via proteolytic cleavage by proteases β‐ and β‐secretase. In this study, we examined content and localization of β‐secretase‐cleaved APP (β‐sAPP) in brain tissue sections from the frontal, temporal and ...
Sennvik, Kristina +4 more
openaire +3 more sources
Genome-wide, high-content siRNA screening identifies the Alzheimer’s genetic risk factor FERMT2 as a major modulator of APP metabolism [PDF]
Genome-wide association studies (GWASs) have identified 19 susceptibility loci for Alzheimer’s disease (AD). However, understanding how these genes are involved in the pathophysiology of AD is one of the main challenges of the “post-GWAS” era.
Cruchaga, Carlos +2 more
core +4 more sources
Localization and regional distribution of p23/TMP21 in the brain
Sequential processing of amyloid precursor protein by β- and γ-secretases generates Alzheimer's disease (AD)-associated β-amyloid peptides. Recently it was reported that the transmembrane protein p23/TMP21 associates with γ-secretase, and negatively ...
Kulandaivelu S. Vetrivel +6 more
doaj +1 more source
Determination of the proteolytic cleavage sites of the amyloid precursor-like protein 2 by the proteases ADAM10, BACE1 and γ-secretase. [PDF]
Regulated intramembrane proteolysis of the amyloid precursor protein (APP) by the protease activities α-, β- and γ-secretase controls the generation of the neurotoxic amyloid β peptide.
Sebastian Hogl +3 more
doaj +1 more source
-Secretase-Regulated Signaling Mechanisms: Notch and Amyloid Precursor Protein [PDF]
In Drosophila, Notch mutations lost a lateral signaling ability and produced a neurogenic phenotype, where cells destined to become epidermis switch fate and give rise to neural tissue (Artavanis-Tsakonas et al. 1995; Lewis 1998). Therefore, when Notch signaling was disrupted, too many neurons were generated.
Nakayama, Kohzo +3 more
openaire +2 more sources
Cellular prion protein regulates β-secretase cleavage of the Alzheimer's amyloid precursor protein [PDF]
Proteolytic processing of the amyloid precursor protein (APP) by β-secretase, β-site APP cleaving enzyme (BACE1), is the initial step in the production of the amyloid β (Aβ) peptide, which is involved in the pathogenesis of Alzheimer's disease.
Parkin, Ed +8 more
openaire +3 more sources
Role of membrane biophysics in Alzheimer\u27s–related cell pathways [PDF]
Cellular membrane alterations are commonly observed in many diseases, including Alzheimer's disease (AD). Membrane biophysical properties, such as membrane molecular order, membrane fluidity, organization of lipid rafts, and adhesion between membrane and
Bungart, Brittani L +4 more
core +8 more sources
SENP1 and SENP2 regulate SUMOylation of amyloid precursor protein
Amyloid β, a key molecule in the pathogenesis of Alzheimer's disease (AD), is produced from amyloid precursor protein (APP) by the cleavage of secretases. APP is SUMOylated near the cleavage site of β-secretase.
Takuma Maruyama +2 more
doaj +1 more source
Anti-Aβ drug screening platform using human iPS cell-derived neurons for the treatment of Alzheimer's disease. [PDF]
BackgroundAlzheimer's disease (AD) is a neurodegenerative disorder that causes progressive memory and cognitive decline during middle to late adult life.
Naoki Yahata +13 more
doaj +1 more source
Navigating the cholesterol maze: Key insights on use of statins in neurodegenerative disorders
The graphical abstract encapsulates the dual neuroprotective mechanisms of statins in neurodegenerative diseases, highlighting both cholesterol‐dependent and cholesterol‐independent pathways. By inhibiting 3‐hydroxy‐3‐methylglutaryl coenzyme A (HMG‐CoA) reductase, statins reduce cholesterol synthesis, leading to altered lipid raft structures that ...
Jun Han Kuan +5 more
wiley +1 more source

