Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
The β-site amyloid cleavage enzyme 1 (BACE1) is the major constituent of amyloid plaques and plays a central role in this brain pathogenesis, thus it constitutes an auspicious pharmacological target for its treatment.
|
31235739 |
2019 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
BACE1 was inhibited, thereby reducing amyloid plaques (Aβ) deposition and eventually reducing inflammation and apoptosis of neurons as revealed by immunohistopathological examination.
|
31276550 |
2019 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
Transcript levels of the genes associated with loss of synaptic plasticity (Bdnf, Syn, GluN1, α7-nAChR, and M<sub>1</sub>-mAChR), formation of neurofibrillary tangles (Tau4 and Tau3), and amyloid plaques (App, Adam10, and Bace1), in the hippocampus of rats at 0, 1, 3, 6, and 9 days after ODX (D<sub>0</sub>, D<sub>1</sub>, D<sub>3</sub>, D<sub>6</sub> and D<sub>9</sub>, respectively) were determined.
|
31114953 |
2019 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
Excess Aβ production by the key protease BACE1, results in Aβ aggregation, forming amyloid plaques, all of which contribute to the pathogenesis of Alzheimer's disease.
|
30842555 |
2019 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
The senile plaques (SPs) in the brain are one of the most pathophysiological characteristics of cognitive dysfunction and its major constituent amyloid β (Aβ) released from amyloid precursor protein (APP) by β (BACE1) and γ (presenilin 1) secretases .
|
29775888 |
2018 |
Senile Plaques
|
0.100 |
AlteredExpression
|
disease |
BEFREE |
In APP/PS1 transgenic mice, the nanocomplexes significantly decrease BACE1 mRNA and the amyloid plaques, suppress phosphorylated tau protein levels, as well as promote hippocampal neurogenesis.
|
29679667 |
2018 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
We found that oral treatment with FLDK reversed learning and memory impairment, reduced Aβ burden and expression of β-site amyloid precursor protein cleavage enzyme 1 (BACE1), and decreased microglial activation in senile plaques.
|
29038004 |
2018 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
BACE1, a key protein involved in Alzheimer's progression, initiates Aβ42 generation that induce senile plaques in brain.
|
29266373 |
2018 |
Senile Plaques
|
0.100 |
AlteredExpression
|
disease |
BEFREE |
Effects of altered RTN3 expression on BACE1 activity and Alzheimer's neuritic plaques.
|
27883331 |
2017 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
Coimmunostaining results showed BACE-1 surrounded amyloid plaques in brain sections.
|
27294139 |
2016 |
Senile Plaques
|
0.100 |
AlteredExpression
|
disease |
BEFREE |
Our work provides a new insight that BACE1 overexpression not only promotes neuritic plaque formation but may also potentiate neurodegeneration mediated by SET elevation in Alzheimer-associated dementia in DS.
|
24935721 |
2015 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
BACE1 cleaves β-amyloid precursor protein (APP) to generate amyloid β protein (Aβ), a central component of neuritic plaques in AD brains.
|
21329555 |
2012 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
Targeting BACE1 (β-site APP cleaving enzyme 1 or β-secretase) is the focus of Alzheimer's disease (AD) research because this aspartyl protease is involved in the abnormal production of β amyloid plaques (Aβ), the hallmark of its pathophysiology.
|
22926063 |
2012 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
β-Site APP cleaving enzyme 1 (β-secretase 1, BACE1) is an enzyme involved in the abnormal production of Aβ42, the major component of senile plaques in Alzheimer's disease (AD).
|
22178732 |
2012 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
Proteolytic processing of amyloid-β precursor protein at the β site by beta-site amyloid-β precursor protein-cleaving enzyme 1 (BACE1) is essential to generate Aβ, a central component of the neuritic plaques.
|
22122349 |
2012 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
Cleavage of APP by BACE1 is the first proteolytic step in the production of amyloid-beta (Abeta), which accumulates in senile plaques in Alzheimer's disease.
|
20685197 |
2010 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
The sortilin-related receptor SorLA/LR11 (LR11) is a transmembrane neuronal sorting protein that reduces beta-amyloid precursor protein trafficking to secretases, notably BACE1 that generates beta-amyloid, the principal component of senile plaques in Alzheimer disease (AD).
|
19364929 |
2009 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
These results demonstrate that amyloid plaques induce BACE1 in surrounding neurons at early stages of pathology before neuron death occurs.
|
17409228 |
2007 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
The beta-site amyloid precursor protein-cleaving enzyme 1 (BACE1) is a prerequisite for the generation of beta-amyloid peptides, the principle constituents of senile plaques in the brains of patients with Alzheimer's disease (AD).
|
16539685 |
2006 |
Senile Plaques
|
0.100 |
Biomarker
|
disease |
BEFREE |
Amyloid precursor protein (APP) is endoproteolytically processed by BACE1 and gamma-secretase to release amyloid peptides (Abeta40 and 42) that aggregate to form senile plaques in the brains of patients with Alzheimer's disease (AD).
|
14645205 |
2004 |