F. A. Aprile

This study shows that C9orf72 hexanucleotide repeat expansions form RNA condensates via multimolecular G-quadruplexes, suggesting a therapeutic target for ALS/FTD.

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.

This paper presents a method to produce N-terminally truncated α-synuclein without extra terminal residues, revealing the first six residues' role in amyloid formation.

The paper introduces a method to maintain amyloidogenic proteins soluble during chemical mutagenesis, demonstrating it by mimicking phosphorylation and acetylation of amyloid-beta peptide.

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