Tetiana Serdiuk

This study shows that alpha-synuclein fibrils cause mitochondrial-derived vesicle budding and structural changes in mitochondria, linking alpha-synuclein aggregation to mitochondrial toxicity.

This paper develops a method to quantitatively analyze the structural states of alpha-synuclein in vitro and in situ, revealing conformational changes in yeast and human neurons.

This study identifies structural and functional differences in alpha-synuclein fibrils from Parkinson's disease, Dementia with Lewy Bodies, and Multiple System Atrophy, linking these differences to disease-specific cellular responses and potential therapeutic targets.

This study systematically identifies structure-specific protein-protein interactions using LiP-MS, demonstrating its application to alpha-synuclein in Parkinson's disease.

The paper identifies transcription factors that regulate β-glucocerebrosidase activity, showing that USF2 and ONECUT2 have opposing effects on GCase levels and function.

This paper shows that ASC controls AA amyloidosis by interacting with SAA and that anti-ASC antibodies reduce amyloid loads in mice.