Giovanni Dietler

The Nt17 domain and its helical conformation regulate the aggregation, cellular properties and neurotoxicity of mutant huntingtin exon 1

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

N-terminal phosphorylation of Huntingtin: A molecular switch for regulating Htt aggregation, helical conformation, internalization and nuclear targeting.

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.