Marie Shimogawa

Genetic Code Expansion, Enzymatic Modification, and C-Terminal Labeling Enable Facile Production of Highly Modified α-Synuclein

This study develops a method to produce highly modified α-synuclein with defined post-translational modifications and a fluorescent label to study their effects on structure and function.

Genetic Code Expansion and Enzymatic Modifications as Accessible Methods for Studying Site-Specific Post-Translational Modifications of Alpha-Synuclein and Tau

The paper provides methods for site-specific post-translational modification of alpha-synuclein and tau using genetic code expansion and enzymatic approaches, enabling studies of their structural dynamics and aggregation.

Investigation of Disease-Relevant Lysine Acetylation Sites in α-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis

This study investigates how acetylation of specific lysine sites in α-synuclein affects aggregation and function, identifying K80 acetylation as a potential therapeutic target.