AMYPdb: A database dedicated to amyloid precursor proteins [PDF]
Abstract Background Misfolding and aggregation of proteins into ordered fibrillar structures is associated with a number of severe pathologies, including Alzheimer's disease, prion diseases, and type II diabetes. The rapid accumulation of knowledge about the sequences and structures of these proteins allows using of ...
Sandrine Pawlicki +2 more
openaire +5 more sources
[18F]Fluorodeprenyl‐D2 PET as a Tool to Monitor Disease Activity in GAD65‐Ab Autoimmune Encephalitis
ABSTRACT Objective To evaluate [18F]fluorodeprenyl‐D2 ([18F]F‐DED) positron‐emission tomography (PET) imaging as a biomarker of disease activity in autoimmune encephalitis (AIE) associated with glutamic acid decarboxylase 65 (GAD65) antibodies. Methods [18F]F‐DED PET was performed in 25 GAD65‐AIE patients and 8 controls using dynamic (0–60 min) and ...
Julia S. Dorneich +19 more
wiley +1 more source
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
Cleavage of Amyloid-β Precursor Protein and Amyloid-β Precursor-like Protein by BACE 1 [PDF]
Site-specific proteolysis of the amyloid-beta precursor protein (APP) by BACE 1 and gamma-secretase, a central event in Alzheimer disease, releases a large secreted extracellular fragment (called APP(S)), peptides of 40-43 residues derived from extracellular and transmembrane sequences (Abeta), and a short intracellular fragment (APP intracellular ...
Qiming, Li, Thomas C, Südhof
openaire +2 more sources
All‐Amyloid Functional Coacervates
This study introduces an all‐amyloid interfacial complex coacervate technique that employs charge‐mediated or functionalization‐assisted complexation of oppositely charged food protein‐derived amyloid nanofibrils to engineer functional soft constructs across multiple length scales.
Seyyed Alireza Hashemi +4 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]
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
Cytoprotective functions of amyloid precursor protein family members in stress signaling and aging [PDF]
Poster presentation: Molecular Neurodegeneration: Basic biology and disease pathways Cannes, France. 10-12 September 2013. Background: The amyloid precursor protein (APP) is processed via two different metabolic pathways: the amyloidogenic and the non ...
Kundu, Arpita +9 more
core +1 more source
. ABSTRACT Neuroinflammation driven by microglial activation is a defining feature of Alzheimer's disease (AD), yet the molecular mechanisms sustaining this proinflammatory state remain unclear. Here, we identify the deubiquitinase OTUD7B as a critical regulator of microglial activation and AD pathology.
Luyao Li +15 more
wiley +1 more source
Smart Nanotechnologies for Multimodal Neuromodulation and Brain Interfacing
Recent advances in smart nanotechnologies are expanding the toolbox for brain interfacing, from wireless neuromodulation and high‐resolution sensing to targeted delivery within the central nervous system. By combining responsive nanomaterials with bioinspired design, these platforms enable multimodal interactions with neurons and glia, while also ...
Tommaso Curiale +6 more
wiley +1 more source
Pro-inflammatory interleukin-18 increases Alzheimer’s disease-associated amyloid-β production in human neuron-like cells [PDF]
Background: Alzheimer’s disease (AD) involves increased accumulation of amyloid-β (Aβ) plaques and neurofibrillary tangles as well as neuronal loss in various regions of the neocortex.
Anderson, G. +14 more
core +2 more sources

