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Broad proteomics analysis of seeding‑induced aggregation of α‑synuclein in M83 neurons reveals remodeling of proteostasis mechanisms that might contribute to Parkinson’s disease pathogenesis

This groundbreaking publication, featured in Molecular Brain, was co-authored by researchers, including Shilpi Chaurasia from Excelra Knowledge Solutions Pvt. Ltd., and sheds light on a critical aspect of Parkinson’s disease (PD) progression: α-synuclein aggregation and its impact on cellular health.

Here’s what you’ll discover:

  • The Link Between α-synuclein and Cellular Dysfunction: The study explores how the aggregation of a protein called α-synuclein, a hallmark of PD, disrupts vital processes within neurons (brain cells).
  • A Deep Dive into Cellular Proteomics: Researchers employed advanced mass spectrometry techniques for total and phospho-proteomics to analyze protein changes in a well-established mouse model of PD. This analysis reveals “gross changes” in the cellular protein makeup linked to α-synuclein aggregation.
  • Unveiling Proteostasis Mechanisms: The publication delves into the body’s protein management system (proteostasis) and how it responds to α-synuclein misfolding. This includes identifying potential mechanisms that could be dysregulated in PD.
  • Hope for New Treatments: By understanding how α-synuclein disrupts proteostasis, researchers open doors for the development of novel therapeutic strategies for PD and related synucleinopathies.

Download the full publication to gain a comprehensive understanding of this exciting research and its potential implications for future PD treatments!


Note: No part of this report may be reproduced or distributed without prior written permission.

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