P. St George-Hyslop

This study quantifies collective interactions in biomolecular phase separation by analyzing dilute phase concentrations and free energy, revealing how salts and small molecules modulate condensate formation.

The paper shows that FUS condensates during aging exhibit solid/liquid coexistence, with the transition initiated at the interface between dense and dilute phases.

The paper develops a method to determine tie-line gradients in ternary LLPS systems using dilute phase concentration measurements, revealing interaction types and compositions in biomolecular condensates.

This paper shows that multiphase biomolecular condensates form due to kinetic trapping during phase transitions, not thermodynamic stability, and explains how this leads to internal sub-compartments.

The paper shows that proteins forming liquid condensates can reenter a phase-separated state at high salt concentrations due to hydrophobic and non-ionic interactions, distinct from low-salt electrostatic-driven phase separation.

The paper shows wild-type sTREM2 inhibits Aβ aggregation and neurotoxicity, while the R47H variant promotes Aβ aggregation and neurotoxicity.

The paper shows that protein condensates undergo a liquid-to-solid transition under mechanical shear, revealing hydrogen bonding as a key factor.

This paper introduces a microdroplet platform to rapidly generate high-resolution phase diagrams of biomolecular condensates and demonstrates its application in studying phase transitions.