Results 21 to 30 of about 29,069 (201)
Presenilin (PS)/γ-secretase is an aspartyl protease that processes a wide range of transmembrane proteins such as the amyloid precursor protein (APP) and Notch1, playing essential roles in normal biological events and diseases.
Mei C. Q. Houser +5 more
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The competitive ectodomain shedding of amyloid-β precursor protein (APP) by α-secretase and β-secretase, and the subsequent regulated intramembrane proteolysis by γ-secretase are the key processes in amyloid-β peptides (Aβ) generation.
Xin Wang, Gang Pei, Gang Pei
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Targeting Amyloidogenic Processing of APP in Alzheimer’s Disease
Alzheimer’s disease (AD) is the most common type of senile dementia, characterized by neurofibrillary tangle and amyloid plaque in brain pathology. Major efforts in AD drug were devoted to the interference with the production and accumulation of amyloid ...
Jing Zhao +7 more
doaj +1 more source
Notch is important to vessel homeostasis. We investigated the mechanistic role of caveolin‐1 (Cav‐1) in mediating the effects of alcohol (Ethanol/EtOH) on the γ‐secretase proteolytic activity necessary for Notch signaling in vascular cells.
Naresh K. Rajendran +3 more
doaj +1 more source
Molecular mechanism of the intramembrane cleavage of the β-carboxyl terminal fragment of amyloid precursor protein by γ-secretase [PDF]
Amyloid β-protein (Aβ) plays a central role in the pathogenesis of Alzheimer's disease, the most common age-associated neurodegenerative disorder. Aβ is generated through intramembrane proteolysis of the β-carboxyl terminal fragment (βCTF) of β-amyloid precursor protein (APP) by γ-secretase.
openaire +3 more sources
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. APLP2, the amyloid precursor-like protein 2, is a homolog of APP, which shows functional overlap with APP, but lacks an amyloid β domain.
Hogl, Sebastian +3 more
openaire +5 more sources
Background Activating NOTCH1 mutations are common in T-cell acute lymphoblastic leukemia. Inhibition of NOTCH1 signaling with γ-secretase inhibitors causes cell cycle block, but only after treatment for several days.
Kim De Keersmaecker +9 more
doaj +1 more source
Cholesterol-Dependent γ-Secretase Activity in Buoyant Cholesterol-Rich Membrane Microdomains
Buoyant membrane fractions containing presenilin 1 (PS1), an essential component of the γ-secretase complex, and APP CTFβ, a γ-secretase substrate, can be isolated from cultured cells and brain by several different fractionation procedures that are ...
Suzanne Wahrle +8 more
doaj +1 more source
A Novel NIR-FRET Biosensor for Reporting PS/γ-Secretase Activity in Live Cells
Presenilin (PS)/γ-secretase plays a pivotal role in essential cellular events via proteolytic processing of transmembrane proteins that include APP and Notch receptors. However, how PS/γ-secretase activity is spatiotemporally regulated by other molecular
Mei CQ Houser +6 more
doaj +1 more source
γ-Secretase is a proteolytic complex whose substrates include Notch, β-amyloid precursor protein (APP), and several other type I transmembrane proteins. Presenilin (PS) and nicastrin are known components of this high-molecular-weight complex, and recent ...
Stephanie Baulac +6 more
doaj +1 more source

