Broad proteomics analysis of seeding-induced aggregation of a-synuclein in M83 neurons reveals remodeling of proteostasis mechanisms that might contribute to Parkinsons disease pathogenesis
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ABSTRACT: Quantitative total proteomics and phospho-proteomics were used to extensively characterize temporal changes in the total and detergent-insoluble protein fractions isolated from neurons from M83 transgenic mice treated with recombinant a-syn PFF. Protein-protein interaction-based network analysis was utilized to define the biological mechanisms altered due to a-syn aggregation to get a comprehensive understanding of specific mechanisms that can be targeted for rational drug design. Analysis results showed broad changes in several key biological processes such as mechanisms regulating cellular proteostasis including changes in several RNA binding proteins.
INSTRUMENT(S): Orbitrap Fusion Lumos
ORGANISM(S): Mus Musculus (ncbitaxon:10090)
SUBMITTER: Brinda Ravikumar
PROVIDER: MSV000094534 | MassIVE | Sat Apr 13 20:40:00 BST 2024
SECONDARY ACCESSION(S): PXD051424
REPOSITORIES: MassIVE
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