G. de Prat Gay

The paper shows that the viral protein P undergoes phase separation driven by a molten globule domain and self-downmodulation, forming viral factories through nucleation-condensation with nucleoprotein N.

This paper shows p53 forms liquid-like droplets that can aggregate, and HPV E2C interacts with p53 to modulate its phase separation and aggregation behavior.

The paper identifies conformational buffering as a mechanism that conserves spatial dimensions in disordered protein regions despite sequence variation, enabling functional selection.