|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
δ-secretase, also known as asparagine endopeptidase (AEP) or legumain, is a lysosomal cysteine protease that cleaves both amyloid precursor protein (APP) and tau, mediating the amyloid-β and tau pathology in Alzheimer's disease (AD).
|
28345579 |
2017 |
|
Alzheimer's Disease
|
0.900 |
GeneticVariation
|
disease |
BEFREE |
γ-Secretase is a multi-subunit membrane protease complex that catalyses the final intramembrane cleavage of the β-amyloid precursor protein (APP) during the neuronal production of amyloid-β peptides (Aβ), which are implicated as the causative agents of Alzheimer's disease (AD).
|
26811537 |
2016 |
|
Alzheimer's Disease
|
0.900 |
GeneticVariation
|
disease |
BEFREE |
γ-Secretase is a membrane-embedded aspartyl protease complex with presenilin as the catalytic component that cleaves within the transmembrane domain (TMD) of >90 known substrates, including the amyloid precursor protein (APP) of Alzheimer's disease.
|
31625391 |
2019 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
γ-secretase inhibitors (GSIs) have been developed to reduce amyloid-β (Aβ) production for the treatment of Alzheimer's disease by inhibiting the cleavage of amyloid precursor protein (APP).
|
22035227 |
2012 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
γ-Secretase complex, the assembly of nicastrin (NCT), Presenilin (PS), Presenilin Enhancer-2 (PEN-2) and Anterior pharynx defective 1 (Aph-1), catalyzes the cleavage of amyloid precursor protein to generate amyloid-β protein (Aβ), the main culprit of Alzheimer's disease.
|
29787759 |
2018 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
β-site APP-cleaving enzyme 1 (BACE1) initiates amyloid precursor protein (APP) cleavage and β-amyloid (Aβ) production, a critical step in the pathogenesis of Alzheimer's disease (AD).
|
31108937 |
2019 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is a key enzyme to cleave the amyloid precursor protein to develop Alzheimer's disease (AD).
|
29679667 |
2018 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
β-Site APP (amyloid precursor protein) cleaving enzyme 1 (BACE1) is the β-secretase enzyme that initiates production of the toxic amyloid-β peptide that accumulates in the brains of patients with Alzheimer's disease (AD).
|
30232227 |
2018 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
β-secretase/β-site amyloid precursor protein (APP)-cleaving enzyme 1 (BACE1) is a key enzyme involved in Alzheimer's disease that has recently been implicated in insulin-independent glucose uptake in myotubes.
|
29526536 |
2018 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
β-Secretase 1 (BACE1) is a key enzyme in Alzheimer's disease pathogenesis that catalyses the amyloidogenic cleavage of amyloid precursor protein (APP).
|
27138913 |
2016 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
β-Amyloid peptides (Aβ), derived from proteolytic processing of amyloid precursor protein (APP), play a central role in AD pathogenesis.
|
29078331 |
2017 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
β-amyloid (Aβ) peptide, accumulation of which is a culprit for Alzheimer's disease (AD), is derived from the initial cleavage of amyloid precursor protein by the aspartyl protease BACE1.
|
23951005 |
2013 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
α-secretase and β-secretase are known to compete for amyloid precursor protein (APP) processing and thus play a vital role in Alzheimer's disease pathogenesis.
|
29325091 |
2018 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
X11alpha may be involved in APP trafficking and metabolism in neurons and thus may be implicated in amyloidogenesis in normal aging and Alzheimer's disease brain.
|
9614075 |
1998 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
X11alpha is a neuronal adaptor protein that interacts with the amyloid precursor protein (APP) through a centrally located phosphotyrosine binding domain to inhibit the production of Abeta peptide that is deposited in Alzheimer's disease brains.
|
20531236 |
2010 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
Wnt signaling loss accelerates the appearance of neuropathological hallmarks of Alzheimer's disease in J20-APP transgenic and wild-type mice.
|
29240990 |
2018 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
Wnt is here! Could Wnt signalling be promoted to protect against Alzheimer disease?: An Editorial for 'Wnt signaling loss accelerates the appearance of neuropathological hallmarks of Alzheimer's disease in J20- APP transgenic and wild-type mice' on doi:10.1111/jnc.14278.
|
29372570 |
2018 |
|
Alzheimer's Disease
|
0.900 |
AlteredExpression
|
disease |
BEFREE |
With the western blot assay, our results revealed that METH exposure significantly increased the expression of AD-associated pathological proteins, including the amyloid precursor protein (APP) and the phosphorylated tau protein (p-tau).
|
31270305 |
2019 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
While these results suggest a possible mechanism linking midlife obesity with the later development of Alzheimer's disease, further research is necessary to elucidate the regulation and functional significance of APP in adipocytes.
|
19672057 |
2009 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
While these results are discouraging, they underscore the need to understand the physiological roles of Aβ<sub>42</sub> and APP under normal conditions as well as at early pre- symptomatic stages of AD.
|
30367888 |
2019 |
|
Alzheimer's Disease
|
0.900 |
GeneticVariation
|
disease |
BEFREE |
While the exact role of the patient-specific miRNA variants within the 3' UTR region of APP and BACE1 demands further analyses, this study does not support a major contribution of miRNA genetic variability to AD pathogenesis.
|
19462468 |
2009 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
While the amyloid hypothesis remains the leading proposed mechanism to explain AD pathophysiology, anti-amyloid therapeutic strategies have yet to translate into useful therapies, suggesting that amyloid β-protein and its precursor, the amyloid precursor protein (APP) are but a part of the disease cascade.
|
28731260 |
2017 |
|
Alzheimer's Disease
|
0.900 |
Biomarker
|
disease |
BEFREE |
While many studies have been focused on the pathologic role of APP in Alzheimer's disease, the physiological functions of APLP1 have remained largely elusive.
|
28537903 |
2017 |
|
Alzheimer's Disease
|
0.900 |
GeneticVariation
|
disease |
BEFREE |
While for many years, an increased production of Abeta42 was considered to be the prime culprit for the initiation of the disease process, and accordingly Abeta42 is elevated by AD-related presenilin(PS) mutations, recent data strongly suggest that PS mutations also lead to a LOF of PS towards a plethora of its substrates including amyloid precursor protein.
|
17622778 |
2007 |
|
Alzheimer's Disease
|
0.900 |
GeneticVariation
|
disease |
BEFREE |
While familial early onset AD is associated with mutations in the amyloid precursor protein and presenilin genes, only the e4 allele of the apolipoprotein E (APOE) gene has so far been established as a genetic risk factor for late onset familial and sporadic AD.
|
16543533 |
2006 |