Tyler Tittle

The paper investigates whether α-synuclein seeding from host tissue contributes to Lewy pathology in dopaminergic neuron grafts in Parkinson's disease patients.

Proximity proteomics in PFF-seeded mouse olfactory bulb shows aggregated phospho-S129 alpha-synuclein mostly reprioritizes existing interactions toward axon-glia, myelin and proteostasis proteins, with a conserved 107-protein signature.

The paper maps physiological alpha-synuclein S129 phosphorylation interactomes in the human brain and confirms their presence in healthy non-human primates.

This study compares alpha-synuclein-interactomes in multiple system atrophy and Parkinson's disease to identify unique and shared pathological features.

This study shows that alpha-synuclein aggregates are resistant to phosphatase dephosphorylation and introduces a method using calf intestinal phosphatase (CIAP) to specifically detect aggregated PSER129 in biological samples.

The study tests whether GBA1 mutations or mouse genotype affect alpha-synuclein seeding in mice, finding no significant influence on seeding efficacy or pathology spread.

The paper identifies PSER129 accumulation in healthy olfactory bulb mitral cells and links it to synucleinopathy pathogenesis through protein interactome analysis.