Results 41 to 50 of about 175,143 (304)

A Novel Protocol to Quantitatively Measure the Endocytic Trafficking of Amyloid Precursor Protein (APP) in Polarized Primary Neurons with Sub-cellular Resolution

open access: yesBio-Protocol, 2017
Alzheimer’s disease’s established primary trigger is β-amyloid (Aβ) (Mucke and Selkoe, 2012). The amyloid precursor protein (APP) endocytosis is required for Aβ generation at early endosomes (Rajendran and Annaert, 2012).
Florent Ubelmann   +2 more
doaj   +1 more source

Amyloid precursor protein in peripheral granulocytes as a potential biomarker for Alzheimer’s disease

open access: yesBangladesh Journal of Pharmacology, 2016
The aim of this study was to assess the potential of amyloid precursor protein in peripheral granulocytes as a diagnostic biomarker for early detection of Alzheimer’s disease.
Xiaonan Wang   +4 more
doaj   +2 more sources

Neuregulin-1 Exerts Protective Effects Against Neurotoxicities Induced by C-Terminal Fragments of APP via ErbB4 Receptor

open access: yesJournal of Pharmacological Sciences, 2012
Neuregulin-1 (NRG1) plays important roles in the development and plasticity of the brain, and it is also reported to have potent neuroprotective properties.
Junghwa Ryu   +6 more
doaj   +1 more source

Manipulation of lipid rafts in neuronal cells [PDF]

open access: yes, 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

Amyloid Precursor-like Protein 1 Influences Endocytosis and Proteolytic Processing of the Amyloid Precursor Protein [PDF]

open access: yesJournal of Biological Chemistry, 2006
Ectodomain shedding of the amyloid precursor protein (APP) is a key regulatory step in the generation of the Alzheimer disease amyloid beta peptide (Abeta). The molecular mechanisms underlying the control of APP shedding remain little understood but are in part dependent on the low density lipoprotein receptor-related protein (LRP), which is involved ...
Neumann, Stephanie   +6 more
openaire   +3 more sources

Rosiglitazone ameliorates diffuse axonal injury by reducing loss of tau and up-regulating caveolin-1 expression

open access: yesNeural Regeneration Research, 2016
Rosiglitazone up-regulates caveolin-1 levels and has neuroprotective effects in both chronic and acute brain injury. Therefore, we postulated that rosiglitazone may ameliorate diffuse axonal injury via its ability to up-regulate caveolin-1, inhibit ...
Yong-lin Zhao   +5 more
doaj   +1 more source

Genetic dissection of down syndrome-associated alterations in APP/amyloid-β biology using mouse models

open access: yesScientific Reports, 2021
Individuals who have Down syndrome (caused by trisomy of chromosome 21), have a greatly elevated risk of early-onset Alzheimer’s disease, in which amyloid-β accumulates in the brain. Amyloid-β is a product of the chromosome 21 gene APP (amyloid precursor
Justin L. Tosh   +12 more
doaj   +1 more source

Controlled cortical impact traumatic brain injury in 3xTg-AD mice causes acute intra-axonal amyloid-β accumulation and independently accelerates the development of tau abnormalities [PDF]

open access: yes, 2011
Alzheimer\u27s disease (AD) is a neurodegenerative disorder characterized pathologically by progressive neuronal loss, extracellular plaques containing the amyloid-β (Aβ) peptides, and neurofibrillary tangles composed of hyperphosphorylated tau proteins.
Brody, David L   +3 more
core   +2 more sources

The role of lipid metabolism in neuronal senescence

open access: yesFEBS Open Bio, EarlyView.
Disrupted lipid metabolism, through alterations in lipid species or lipid droplet accumulation, can drive neuronal senescence. However, lipid dyshomeostasis can also occur alongside neuronal senescence, further amplifying tissue damage. Delineating how lipid‐induced senescence emerges in neurons and glial cells, and how it contributes to ageing and ...
Dikaia Tsagkari   +2 more
wiley   +1 more source

Binding of F-spondin to amyloid-β precursor protein: A candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage [PDF]

open access: yesProceedings of the National Academy of Sciences, 2004
Amyloid-β precursor protein (APP), a type I membrane protein, is physiologically processed by α- or β-secretases that cleave APP N-terminal to the transmembrane region. Extracellular α-/β-cleavage of APP generates a large secreted N-terminal fragment, and a smaller cellular C-terminal fragment.
Angela, Ho, Thomas C, Südhof
openaire   +2 more sources

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