Controlled cortical impact traumatic brain injury in 3xTg-AD mice causes acute intra-axonal amyloid-β accumulation and independently accelerates the development of tau abnormalities [PDF]
Alzheimer\u27s disease (AD) is a neurodegenerative disorder characterized pathologically by progressive neuronal loss, extracellular plaques containing the amyloid-β (Aβ) peptides, and neurofibrillary tangles composed of hyperphosphorylated tau proteins.
Brody, David L +3 more
core +2 more sources
Why are Functional Amyloids Non-Toxic in Humans? [PDF]
Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in ...
Hewitt, EW, Jackson, MP
core +2 more sources
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
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
Background Synaptic degeneration and accumulation of amyloid β-peptides (Aβ) are hallmarks of the Alzheimer diseased brain. Aβ is synaptotoxic and produced by sequential cleavage of the amyloid precursor protein (APP) by the β-secretase BACE1 and by γ ...
Jolanta L. Lundgren +8 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
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
The Uppsala APP Mutation Promotes Wild‐Type Amyloid‐β Aggregation and Deposition In Vivo
We investigated in vivo cross‐seeding of amyloid‐β (Aβ) isoforms in transgenic mice co‐expressing wild‐typeAβ and the Uppsala‐mutant Aβ variant (AβUpp), lacking six central residues. Weleveraged MALDI‐MS imaging and hyperspectral microscopy to follow spatio‐temporalAβ deposition.
Junyue Ge +14 more
wiley +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

