Francesco Simone Ruggeri

The paper redesigns TALE proteins to assemble linear protein-DNA complexes on double-stranded DNA templates, enabling controlled length and application in antigen display.

The paper investigates the formation of amyloid loops in brain tissues and finds that protofibril flexibility, not hydrogen bonding, enables loop formation and disease-related toxicity.

The paper develops a multiplex reverse genetics platform to identify genetic modifiers of protein misfolding in neurodegenerative diseases and identifies DNAJB6 as a modifier of toxicity and solubility of ALS/FTD-linked RNA-binding proteins.

This study shows that the Nt17 domain regulates Httex1 aggregation, toxicity, and cellular uptake through its conformation and interaction with polyQ repeats.

The paper examines soluble Aβ aggregates in CSF from AD, MCI, and healthy controls, finding stage-specific differences in aggregate size and toxicity mechanisms.

This study investigates how phosphorylation at S13 and S16 of Httex1 affects its structure, aggregation, and subcellular localization, revealing a phosphorylation-dependent switch that regulates its function.