Joan‐Emma Shea

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 paper introduces HydroMap and FastHydroMap models to predict hydrophobicity from water features, enabling rapid and accurate computation of dewetting free energy for proteins and surfaces.

This paper identifies I-PDBs as BAG2-driven organelles that link proteostasis to CD8+ T cell surveillance by processing pathological tau into antigenic peptides.

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 identifies a tau peptide fragment that forms seeding-competent fibrils and shows how the P301L mutation facilitates its aggregation into 4R tauopathy-like structures.

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 uses information theory to model epistasis in ribozymes, predicting high-activity mutants that were validated experimentally and revealed an evolutionary bridge between ribozyme families.

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.