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Published in 2019 at "International Journal of Nanomedicine"
DOI: 10.2147/ijn.s190354
Abstract: Background Most of nanoparticles are nontoxic and have high absorption capability. Therefore, nanoparticles binding can effectively restrain fibrillation of β-amyloid and α-synuclein proteins and eventually prevent the toxicity of pathogenesis peptide of Alzheimer. Super paramagnetic…
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Keywords:
amyloid synuclein;
nanoparticles coated;
fibrillation;
superparamagnetic nanoparticles ... See more keywords
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Published in 2023 at "Frontiers in Molecular Biosciences"
DOI: 10.3389/fmolb.2023.1153839
Abstract: Aberrant self-assembly of an intrinsically disordered protein is a pathological hallmark of protein misfolding diseases, such as Alzheimer’s and Parkinson’s diseases (AD and PD, respectively). In AD, the 40–42 amino acid-long extracellular peptide, β-amyloid (Aβ),…
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Keywords:
amyloid synuclein;
oligomerization assembly;
synuclein;
assembly amyloid ... See more keywords
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Published in 2022 at "Frontiers in Neuroscience"
DOI: 10.3389/fnins.2022.822420
Abstract: The central role of oligomers, small soluble aggregates of misfolded proteins, in the pathogenesis of neurodegenerative disorders is recognized in numerous experimental conditions and is compatible with clinical evidence. To underline this concept, some years…
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Keywords:
prion;
inflammation;
prion protein;
amyloid synuclein ... See more keywords
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Published in 2021 at "Molecules"
DOI: 10.3390/molecules26206120
Abstract: 14-3-3 proteins are abundant, intramolecular proteins that play a pivotal role in cellular signal transduction by interacting with phosphorylated ligands. In addition, they are molecular chaperones that prevent protein unfolding and aggregation under cellular stress…
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Keywords:
fibril forming;
amyloid synuclein;
spectroscopy;
amyloid fibril ... See more keywords