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Originally published by Kumamoto University on November 1, 2024 T he trigger for neurodegeneration is the assembly of G4 structures driven by increased intracellular calcium ions (Ca2+) due to cellular stress. α -Synuclein binds directly to G4, shifting into an aggregate-prone structure that employs G4 as a scaffold to form harmful clusters. Therefore, inhibiting G4 assembly can prevent α -synuclein aggregation, helping to protect against neuronal function loss. Credit: Cell (2024). DOI: 10.1016/j.cell.2024.09.037 A team of researchers at Kumamoto University has uncovered a mechanism in the f ormation of harmful protein aggregates that lead to neurodegenerative diseases such as Parkinson's disease. The team, led by Professor Norifumi Shioda and Associate Professor Yasushi Yabuki, identified for the first time that unique RNA structures called G-quadruplexes (G4s) play a central role in promoting the aggregation of α -synuclein , a protein associated with neurodegen

  Originally published by University of Sydney on August 24, 2023 Nanoscale scan image showing protein condensate interaction. Credit: The University of Sydney Many diseases affecting the brain and nervous system are linked to the formation of protein aggregates , or solid condensates , in cells from their liquid form condensate, but little is known about this process . This liquid-to-solid transition can trigger the formation of what are called amyloid fibrils . These can further form plaques in neurons causing neurodegenerative diseases such as Alzheimer's . Biomedical engineers at the University of Sydney , in collaboration with scientists at the University of Cambridge and Harvard University , have now developed sophisticated optical techniques to monitor at close range the process by which these protein aggregates form. By testing a protein associated with amyotrophic lateral sclerosis—ALS disease, which affected astrophysicist Professor Stephen Hawking—