AI Article Synopsis
- * Recent theories suggest that Parkinson's disease shares a similar mechanism with other neurological disorders, where α-synuclein spreads in a way that resembles prion diseases.
- * The review compares the characteristics of α-synuclein with prion proteins and examines the factors that affect how these proteins change shape and contribute to neurodegeneration.
Article Abstract
The principal pathogenic event in Parkinson's disease is characterized by the conformational change of α-synuclein, which form pathological aggregates of misfolded proteins, and then accumulate in intraneuronal inclusions causing dopaminergic neuronal loss in specific brain regions. Over the last few years, a revolutionary theory has correlated Parkinson's disease and other neurological disorders with a shared mechanism, which determines α-synuclein aggregates and progresses in the host in a prion-like manner. In this review, the main characteristics shared between α-synuclein and prion protein are compared and the cofactors that influence the remodeling of native protein structures and pathogenetic mechanisms underlying neurodegeneration are discussed.
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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8347681 | PMC |
| http://dx.doi.org/10.3390/ijms22158022 | DOI Listing |
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