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Originally published by Rice University , at https://medicalxpress.com , on April 15, 2025   Schematic diagram of RibbonFold. Credit: Proceedings of the National Academy of Sciences (2025). DOI: 10.1073/pnas.2501321122 A novel artificial intelligence (AI) tool has revealed how disease-linked proteins misfold into harmful structures, a key advance in understanding neurodegenerative disorders such as Alzheimer's and Parkinson's. The study , led by Mingchen Chen of the Changping Laboratory and Rice University's Peter Wolynes , i ntroduces RibbonFold , a new computational method capable of predicting the structures of amyloids —long, twisted fibers that accumulate in the brains of patients suffering from neurological decline . The study is published in the Proceedings of the National Academy of Sciences . Read more  

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...