MassIVE MSV000094534

Partial Public PXD051424

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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Description

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. [doi:10.25345/C5DJ58T54] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Parkinsons Disease, M83 mouse model, total and phosphoproteomics

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Principal Investigators:
(in alphabetical order) 		Brinda Ravikumar, AbbVie, United States of America
Submitting User: pottsgr
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