Introduction
Parkinson’s disease (PD) – the second most prevalent neurodegenerative disorder worldwide [1] – is characterized by the progressive accumulation of misfolded and aggregated alpha-synuclein (aSyn), whose toxic oligomeric and fibrillar species are closely associated with disease onset and progression [1]. While in vitro studies have clarified aSyn aggregation kinetics under controlled conditions, the cellular environment remains more complex and less understood. In cells, aSyn synthesis, proteasomal and lysosomal degradation, lipid interactions, and other cellular components can strongly modify aggregation dynamics compared to test-tube conditions [2]. Therefore, translating aSyn aggregation into a physiologically relevant cellular context requires the explicit representation of intracellular protein turnover.
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