BACE1, beta-secretase 1, 23621

N. diseases: 120; N. variants: 8
Source: ALL
Disease Score gda Association Type Type Original DB Sentence supporting the association PMID PMID Year
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
Senile Plaques
0.100 Biomarker disease BEFREE BACE1 was inhibited, thereby reducing amyloid plaques () deposition and eventually reducing inflammation and apoptosis of neurons as revealed by immunohistopathological examination. 31276550 2019
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
Senile Plaques
0.100 AlteredExpression disease BEFREE Effects of altered RTN3 expression on BACE1 activity and Alzheimer's neuritic plaques. 27883331 2017
CUI: C0333463
Disease: Senile Plaques
Senile Plaques
0.100 Biomarker disease BEFREE Coimmunostaining results showed BACE-1 surrounded amyloid plaques in brain sections. 27294139 2016
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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 (), the hallmark of its pathophysiology. 22926063 2012
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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
CUI: C0333463
Disease: Senile Plaques
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