Deciphering the Tau/14-3-3 Interaction via Artificial Intelligence and Chemical Cross-Linking
| Autoři | |
|---|---|
| Rok publikování | 2026 |
| Druh | Další prezentace na konferencích |
| Fakulta / Pracoviště MU | |
| Citace | |
| Popis | The aggregation of tau protein plays a crucial role in several neurodegenerative diseases, including Alzheimer’s disease, Chronic traumatic encephalopathy and others. The diseases are characterized by the presence of tau fibrils with specific morphologies. Different phosphorylation patterns have been observed in diseases, indicating that morphology is dependent on the posttranslational modifications. With the release of AlphaFold3 allowing the structure prediction of posttranslationally modified proteins, we examined the differences in the predicted structures of several tau constructs with different phosphorylations. Still, the exact cause and mechanism of tau aggregation remain unknown. However, the interaction with 14-3-3 proteins modulates the aggregation properties of tau protein. On this poster, we also evaluate models of tau/14-3-3 interactions validated by chemical cross-linking. |
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