Chung-Ta Han

In a minimal tau fibril model, residue 300/301 binds incoming peptide first and carries the most release-prone hydration water. Spin-labelling site 300 impairs locking and suppresses seeded growth.

This study identifies tRNA-derived fragments (tRFs) as key regulators of Tau aggregation in Alzheimer's disease and shows their potential as therapeutic targets.

This study shows blue light or high pressure activates AsLOV2 by expelling structured water, causing conformational changes and suggesting hydration water drives protein mechanics.

This study uses NMR to show phosphoryl groups in tau fibrils form ordered 1D wires that stabilize pathological aggregation.