
(© Image: Fotolia) Exploring the post-translational modifications of a key protein in Parkinson's disease, researchers at EPFL and USC uncover potential pathways for future therapies in neurodegenerative diseases in general. Neurodegenerative diseases, such as Alzheimer's and Parkinson's, present a significant health challenge, affecting over 50 million people globally. One common feature of these diseases is the accumulation of misfolded protein aggregates in the brain, known as amyloid fibrils, which disrupt normal cell function and eventually lead to cell death. In a new study, scientists led by Hilal Lashuel at EPFL and Matthew R. Pratt at USC have made a significant advancement in understanding how post-translational modifications (PTMs) - changes that happen to proteins after they are synthesized in the cell - can influence the formation and pathogenicity of these amyloid fibrils. The researchers studied the protein alpha-synuclein, which is linked to the formation of amyloid fibrils in Parkinson's disease. The researchers looked at a specific modification that the protein undergoes, technically known as "O-linked -N-acetylglucosamine" or O-GlcNAc for short. O-GlcNAc is a kind of modification that adds a single sugar molecule, to specific serine or threonine residues in the protein, thereby altering its function and properties.
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