A. Avni

Single-Molecule FRET Illuminates Structural Subpopulations and Dissects Crucial Molecular Events During Phase Separation of a Prion-Like Low Complexity Domain

The paper uses single-molecule techniques to study phase separation of a prion-like domain, revealing structural subpopulations and molecular events involved in condensate formation and disease-related aggregation.

ATP modulates self-perpetuating conformational conversion generating structurally distinct yeast prion amyloids that limit autocatalytic amplification

This study shows ATP modulates yeast prion amyloid formation and limits autocatalytic amplification by altering aggregate structure and fragmentation.

Heterotypic electrostatic interactions control complex phase separation of tau and prion into multiphasic condensates and co-aggregates

This study shows that tau and prion proteins form dynamic condensates through electrostatic interactions, which can transition into solid-like co-aggregates with age.

TOR coordinates Cytokinin and Gibberellin signals mediating development and defense

This study shows TOR coordinates cytokinin and gibberellin signals to regulate plant development and defense, with differential effects based on developmental status and hormone ratios.

Single-Droplet Surface-Enhanced Raman Scattering Decodes the Molecular Language of Liquid-Liquid Phase Separation

This study uses single-droplet SERS to analyze molecular interactions in FUS condensates, revealing conformational heterogeneity and RNA effects.

Spatiotemporal Modulations in Heterotypic Condensates of Prion and α-Synuclein Control Phase Transitions and Amyloid Conversion

This study investigates how prion protein and α-synuclein form dynamic condensates that influence phase transitions and amyloid conversion through electrostatic interactions and RNA effects.

An Intrinsically Disordered Pathological Variant of the Prion Protein Y145Stop Transforms into Self-Templating Amyloids via Liquid-Liquid Phase Separation

This study shows that the Y145Stop variant of the prion protein undergoes liquid-liquid phase separation and transitions into amyloid-like aggregates, highlighting a potential role for intrinsically disordered regions in neurodegenerative diseases.