J. A. M. Bard

The paper studies how stress-induced biomolecular condensation adapts to thermal environments across three yeast species, showing species-specific temperature tuning and conserved molecular features.

During stress, molecular chaperones preserve 'orphan' ribosomal proteins in liquid-like condensates, maintaining them in a usable form and enabling efficient recovery from stress.

This study uses single-molecule FRET to show ubiquitin chains regulate proteasome conformational dynamics, enhancing substrate degradation by stabilizing engagement-competent states.

This study shows that the yeast disaggregation system efficiently disperses heat-induced Pab1 condensates, revealing distinct molecular requirements compared to model substrates.