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Updated: Jun 15, 2026

Monitoring Cell-to-cell Transmission of Prion-like Protein Aggregates in Drosophila Melanogaster
Published on: March 12, 2018
The relationship between the 20S proteasomes and prion-mediated neurodegenerations: potential therapeutic
Valentina Cecarini1, Laura Bonfili, Massimiliano Cuccioloni
1School of Biosciences and Biotechnology, University of Camerino, Via Gentile III da Varano, 62032 Camerino, MC, Italy.
Abstract:
The dysfunction of cellular degradation pathways of aberrant and misfolded proteins is a critical event in the onset of neurodegenerative disorders. Among these pathologies, prion diseases are a unique class of transmissible fatal disorders affecting mammals, characterized by the presence of an abnormal isoform of a membrane-bound protein, namely the prion protein. The proteasome is the main proteolytic machinery in charge of removing damaged, oxidized and misfolded proteins and numerous authors have approached the involvement of this complex in the prion protein cellular processing. Herein, we described the general features of prion disorders focusing our attention on the available data on the interplay between the infectious agent and the proteasome system, exploring its implications in prion-mediated toxicity. Finally, considering the proteasome as a potential drug target, we reviewed possible therapeutic opportunities in the treatment of such pathologies.
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