Songi Han

This paper demonstrates that a magnetic field modulates the formation of a covalent photoadduct in AsLOV2, enhancing signaling through spin-selective radical-pair reactions.

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 paper develops a method to reconstruct time-resolved inter-residue distance distributions in proteins during functional dynamics using rs-TiGGER spectra and applies it to AsLOV2.

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

The paper designs synthetic tau fibrils that mimic AD and CTE structures, showing strong seeding ability and catalytic effects in vitro and in cells.

This study introduces DEER spectroscopy to analyze the supramolecular packing of amyloid fibrils, showing that heparin-induced fibrils are mispacked while seeded aggregation improves packing order.

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 paper develops a protein-like polymer that inhibits tau fibril propagation in human-derived models of neurodegeneration by targeting a specific structural motif of 4R tau isoforms.

This paper introduces SF-SVD and WavPDS methods to accurately reconstruct distance distributions from DEER data of biopolymers, resolving broad and mixed features without prior knowledge.

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

The paper designs a 19-residue peptide that selectively induces aggregation of 4R tau over 3R tau, revealing structural and amino acid determinants of tauopathy propagation.

The paper shows that cell-passaged tau fibrils from CBD and PSP patients generate heterogeneous fibrils with a subpopulation resembling the original disease fold.

The paper identifies the proline-rich domain (PRD) of tau as a driver of liquid-liquid phase separation (LLPS) in cells, showing its phosphorylation-dependent behavior and interaction with microtubules.