Results 41 to 50 of about 14,107 (263)

Multi-compartmental modeling of SORLA’s influence on amyloidogenic processing in Alzheimer’s disease [PDF]

open access: yes, 2012
BACKGROUND: Proteolytic breakdown of the amyloid precursor protein (APP) by secretases is a complex cellular process that results in formation of neurotoxic Aβ peptides, causative of neurodegeneration in Alzheimer’s disease (AD).
Angelyn Lao   +4 more
core   +2 more sources

A Paired RNAi and RabGAP Overexpression Screen Identifies Rab11 as a Regulator of β-Amyloid Production

open access: yesCell 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
doaj   +1 more source

Tau is central in the genetic Alzheimer-frontotemporal dementia spectrum [PDF]

open access: yes, 2005
In contrast to the common and genetically complex senile form of Alzheimer's disease (AD), the molecular genetic dissection of inherited presenile dementias has given important mechanistic insights into the pathogenesis of degenerative brain disease ...
Cruts, Marc   +5 more
core   +1 more source

Results of Beta Secretase-Inhibitor Clinical Trials Support Amyloid Precursor Protein-Independent Generation of Beta Amyloid in Sporadic Alzheimer’s Disease

open access: yesMedical 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
doaj   +1 more source

Striking reduction of amyloid plaque burden in an Alzheimer's mouse model after chronic administration of carmustine [PDF]

open access: yes, 2013
BACKGROUND: Currently available therapies for Alzheimer's disease (AD) do not treat the underlying cause of AD. Anecdotal observations in nursing homes from multiple studies strongly suggest an inverse relationship between cancer and AD.
Adel Nefzi   +7 more
core   +1 more source

Visualization of Alzheimer’s Disease Related α-/β-/γ-Secretase Ternary Complex by Bimolecular Fluorescence Complementation Based Fluorescence Resonance Energy Transfer

open access: yesFrontiers 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
doaj   +1 more source

Amyloid Precursor Proteins Are Dynamically Trafficked and Processed during Neuronal Development [PDF]

open access: yes, 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
core   +2 more sources

Intracellular pH regulates amyloid precursor protein intracellular domain accumulation

open access: yesNeurobiology 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
doaj   +1 more source

Upregulation of APP, ADAM10 and ADAM17 in the denervated mouse dentate gyrus. [PDF]

open access: yesPLoS 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
doaj   +1 more source

Increased amyloidogenic processing of transgenic human APP in X11-like deficient mouse brain [PDF]

open access: yes, 2010
Background: X11-family proteins, including X11, X11-like (X11L) and X11-like 2 (X11L2), bind to the cytoplasmic domain of amyloid beta-protein precursor (APP) and regulate APP metabolism. Both X11 and X11L are expressed specifically in brain, while X11L2
Maho Kondo   +10 more
core   +3 more sources

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