Interaction of oxidative stress and misfolded proteins in the mechanism of neurodegeneration

Andrey Y. Abramov*, Elena V. Potapova, Viktor V. Dremin, Andrey V. Dunaev

*Corresponding author for this work

    Research output: Contribution to journalReview articlepeer-review


    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.

    Original languageEnglish
    Article number101
    Number of pages14
    Issue number7
    Publication statusPublished - 30 Jun 2020

    Bibliographical note

    This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited


    • Mutant huntingtin protein
    • Neurodegeneration
    • Oxidative stress
    • Reactive oxygen species
    • Tau protein
    • α-synuclein
    • β-amyloid


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