Results 31 to 40 of about 14,023 (271)
Cell Reports, 2013 Alzheimer’s disease (AD) is characterized by cerebral deposition of β-amyloid (Aβ) peptides, which are generated from amyloid precursor protein (APP) by β- and γ-secretases. APP and the secretases are membrane associated, but whether membrane trafficking
Vinod Udayar +15 more
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Amyloid Precursor Proteins Are Dynamically Trafficked and Processed during Neuronal Development [PDF]
, 2016 Proteolytic processing of the Amyloid Precursor Protein (APP) produces beta-amyloid (Aβ) peptide fragments that accumulate in Alzheimer’s Disease (AD), but APP may also regulate multiple aspects of neuronal development, albeit via mechanisms that are not
Doris Kretzschmar +7 more
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Frontiers in Molecular Neuroscience, 2018 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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Intracellular pH regulates amyloid precursor protein intracellular domain accumulation
Neurobiology of Disease, 2007 The amyloid precursor protein (APP) metabolism is central to pathogenesis of Alzheimer’s disease (AD). Parenchymal amyloid deposits, a neuropathological hallmark of AD, are composed of amyloid-beta peptides (Abeta).
Valérie Vingtdeux +8 more
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Hypoxic regulation of ion channel function and expression [PDF]
, 2002 Acute hypoxia regulates the activity of specific ion channels in a rapid and reversible manner. Such effects underlie appropriate cellular responses to hypoxia which are designed to initiate cardiorespiratory reflexes and contribute importantly to other ...
Peers, C.
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Medical Sciences, 2018 The present review analyzes the results of recent clinical trials of β secretase inhibition in sporadic Alzheimer’s disease (SAD), considers the striking dichotomy between successes in tests of β-site Amyloid Precursor Protein-Cleaving ...
Vladimir Volloch, Sophia Rits
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Upregulation of APP, ADAM10 and ADAM17 in the denervated mouse dentate gyrus. [PDF]
PLoS ONE, 2014 The disintegrin and metalloproteinases ADAM10 and ADAM17 are regarded as the most important α-secretases involved in the physiological processing of amyloid precursor protein (APP) in brain.
Domenico Del Turco +3 more
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Alzheimer’s Disease: A Molecular View of β-Amyloid Induced Morbific Events
Biomedicines, 2021 Amyloid-β (Aβ) is a dynamic peptide of Alzheimer’s disease (AD) which accelerates the disease progression. At the cell membrane and cell compartments, the amyloid precursor protein (APP) undergoes amyloidogenic cleavage by β- and γ-secretases and ...
Rajmohamed Mohamed Asik +8 more
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Why are Functional Amyloids Non-Toxic in Humans? [PDF]
, 2017 Amyloids were first identified in association with amyloidoses, human diseases in which proteins and peptides misfold into amyloid fibrils. Subsequent studies have identified an array of functional amyloid fibrils that perform physiological roles in ...
Hewitt, EW, Jackson, MP
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Apolipoprotein E modulates γ‐secretase cleavage of the amyloid precursor protein [PDF]
Journal of Neurochemistry, 2004 AbstractPolymorphisms in the apolipoprotein E (APOE) gene affect the risk of Alzheimer disease and the amount of amyloid β‐protein (Aβ) deposited in the brain. The apoE protein reduces Aβ levels in conditioned media from cells in culture, possibly through Aβ clearance mechanisms.
Michael C, Irizarry +9 more
openaire +2 more sources