P. Arosio

α-Synuclein Aggregation is Triggered by Amyloid-β Oligomers via Heterogeneous Primary Nucleation

This study shows that soluble amyloid-β oligomers trigger α-synuclein aggregation via heterogeneous primary nucleation, forming fibrils with α-synuclein cores and associated amyloid-β.

The interface of condensates of the hnRNPA1 low complexity domain promotes formation of amyloid fibrils

This study shows that amyloid fibrils form at the interface of hnRNPA1 condensates, not uniformly within them, and that surfactants can inhibit this process.

A conserved mechanism regulates reversible amyloids via pH-sensing regions

This study identifies a conserved mechanism by which pH-sensing regions regulate reversible amyloid formation in pyruvate kinase across yeast and human cells.

Dynamic arrest and aging of biomolecular condensates are regulated by low-complexity domains, RNA and biochemical activity

This study uses DDM to analyze how material properties of P-body condensates are regulated by RNA structure, enzymatic activity, and other factors.

Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide

This study investigates the dynamics of Aβ42 oligomers during amyloid fibril formation, revealing that most oligomers dissociate into monomers rather than forming fibrils.

Thermodynamic and kinetic design principles for protein aggregation inhibitors

This study develops a kinetic theory to identify thermodynamic and kinetic signatures of effective protein aggregation inhibitors.

Pat1 promotes processing body assembly by enhancing the phase separation of the DEAD-box ATPase Dhh1 and RNA

This study shows Pat1 promotes PB assembly by enhancing Dhh1 and RNA phase separation, opposing Not1's inhibitory effect.