Results 31 to 40 of about 27,905 (224)
Role of X11 and ubiquilin as in vivo regulators of the amyloid precursor protein in Drosophila. [PDF]
PLoS ONE, 2008 The Amyloid Precursor Protein (APP) undergoes sequential proteolytic cleavages through the action of beta- and gamma-secretase, which result in the generation of toxic beta-amyloid (Abeta) peptides and a C-terminal fragment consisting of the ...
Garrett G Gross +5 more
doaj +1 more source
Biomedicines, 2022 Our studies reveal changes in the expression of the main participants in the processing of amyloid precursor protein (APP) in neurons and astrocytes after photothrombotic stroke (PTS). Here we show the increase in the level of N- and C-terminal fragments
Svetlana Sharifulina +10 more
doaj +1 more source
Identification of BACE1 cleavage sites in human voltage-gated sodium channel beta 2 subunit [PDF]
, 2010 Background: The voltage-gated sodium channel β2 subunit (Navβ2) is a physiological substrate of BACE1 (β-site APP cleaving enzyme) and γ-secretase, two proteolytic enzymes central to Alzheimer's disease pathogenesis.
Doo Kim +3 more
core +4 more sources
Lowering beta-amyloid levels rescues learning and memory in a Down syndrome mouse model. [PDF]
PLoS ONE, 2010 beta-amyloid levels are elevated in Down syndrome (DS) patients throughout life and are believed to cause Alzheimer's disease (AD) in adult members of this population.
William J Netzer +7 more
doaj +1 more source
Manipulation of lipid rafts in neuronal cells [PDF]
, 2010 Lipid rafts are specialized plasma membrane micro-domains highly enriched in cholesterol, sphingolipids and glycosylphosphatidylinositol (GPI) anchored proteins.
Eckert, Gunter P.
core +1 more source
Presenilins and γ-Secretase in Membrane Proteostasis
Cells, 2019 The presenilin (PS) proteins exert a crucial role in the pathogenesis of Alzheimer disease (AD) by mediating the intramembranous cleavage of amyloid precursor protein (APP) and the generation of amyloid β-protein (Aβ).
Naoto Oikawa, Jochen Walter
doaj +1 more source
Molecular Brain, 2021 Alterations in the canonical processing of Amyloid Precursor Protein generate proteoforms that contribute to the onset of Alzheimer’s Disease. Modified composition of γ-secretase or mutations in its subunits has been directly linked to altered generation
Shekhar Kedia +5 more
doaj +1 more source
Axonal amyloid precursor protein and its fragments undergo somatodendritic endocytosis and processing. [PDF]
, 2015 Deposition of potentially neurotoxic Aβ fragments derived from amyloid precursor protein (APP) at synapses may be a key contributor to Alzheimer's disease.
Goldstein, Lawrence SB +2 more
core +1 more source
Phosphorylation Regulates Intracellular Trafficking of β-Secretase [PDF]
Journal of Biological Chemistry, 2001 beta-Secretase (BACE) is a transmembrane aspartyl protease, which generates the N terminus of Alzheimer's disease amyloid beta-peptide. Here, we report that BACE can be phosphorylated within its cytoplasmic domain at serine residue 498 by casein kinase 1.
Walter, Jochen +8 more
openaire +2 more sources
Lessons from a BACE1 inhibitor trial: off-site but not off base [PDF]
, 2014 Alzheimer's disease (AD) is characterized by formation of neuritic plaque primarily composed of a small filamentous protein called amyloid-β peptide (Aβ). The rate-limiting step in the production of Aβ is the processing of Aβ precursor protein (APP) by β-
Greig, Nigel H. +3 more
core +1 more source