Proteins Interplay in Neurodegeneration
A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biomacromolecules: Proteins".
Deadline for manuscript submissions: 30 April 2024 | Viewed by 9786
Special Issue Editor
Special Issue Information
Dear Colleagues,
Several neurodegenerative diseases are associated with the extracellular or intracellular accumulation of protein inclusions regulated by a vast network of protein and metal interactions. Specific key proteins linked to neurodegeneration, such as amyloid-β, α-synuclein, islet amyloid polypeptide, and prion protein, share the ability to form toxic oligomeric and aggregate species. The precise mechanisms responsible for protein aggregation are still not clear; however, there is plenty of evidence indicating that metal ions, pH, membrane environments, ligand binding, and ionic strength might impact the aggregation rate. In addition to this, familial mutations and post-translational modifications might strongly affect the misfolding of aggregation-prone proteins. All these processes can induce novel or altered protein interactions, which in turn can impact numerous essential cellular processes, such as vesicle trafficking, altered metal homeostasis, cellular oxidative stress, and mitochondria dysfunction.
Dr. Daniela Valensin
Guest Editor
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Keywords
- amyloidogenic proteins
- metal ions
- ROS
- protein misfolding
- neurons