F. S. Ruggeri

This study characterizes the aging behavior of FUS condensates using microfluidic technology and surface-based techniques, revealing phase transitions and structural changes associated with material properties.

This study investigates how Aβ42 amyloid fibrils change over time, showing increased length, thickness, and cross-β sheet content, which affects their ability to seed new aggregates.

This study shows ANXA11 biomolecular condensates couple protein and lipid phase states on lysosomal membranes through interactions with ALG2 and CALC.

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

This paper develops a lab-on-a-chip method for analyzing biomolecular processes with high sensitivity and single molecule resolution in physiological conditions.

This study shows the Hsc70-DnaJB1-Apg2 chaperone system removes monomer units directly from α-synuclein fibril ends, reversing aggregation without intermediate fragmentation.

This paper identifies a small molecule that binds and sequesters monomeric amyloid-β, inhibiting its aggregation and rescuing toxicity in a C. elegans model.

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

This study uses infrared nanospectroscopy to directly measure how bexarotene interacts with Aβ42 oligomers and fibrils, revealing a single hydrogen bond between the compound's carbonyl group and the aggregates.