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- W3039418677 startingPage "101" @default.
- W3039418677 abstract "Aggregation of the misfolded proteins β-amyloid, tau, huntingtin, and α-synuclein is one of the most important steps in the pathology underlying a wide spectrum of neurodegenerative disorders, including the two most common ones—Alzheimer’s and Parkinson’s disease. Activity and toxicity of these proteins depends on the stage and form of aggregates. Excessive production of free radicals, including reactive oxygen species which lead to oxidative stress, is proven to be involved in the mechanism of pathology in most of neurodegenerative disorders. Both reactive oxygen species and misfolded proteins play a physiological role in the brain, and only deregulation in redox state and aggregation of the proteins leads to pathology. Here, we review the role of misfolded proteins in the activation of ROS production from various sources in neurons and glia. We discuss if free radicals can influence structural changes of the key toxic intermediates and describe the putative mechanisms by which oxidative stress and oligomers may cause neuronal death." @default.
- W3039418677 created "2020-07-10" @default.
- W3039418677 creator A5001456577 @default.
- W3039418677 creator A5013722989 @default.
- W3039418677 creator A5055353781 @default.
- W3039418677 creator A5062095201 @default.
- W3039418677 date "2020-06-30" @default.
- W3039418677 modified "2023-09-30" @default.
- W3039418677 title "Interaction of Oxidative Stress and Misfolded Proteins in the Mechanism of Neurodegeneration" @default.
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