Elizabeth R. Rhoades

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.

Tau Aggregation Results in an Impaired Ability to Counteract Microtubule Destabilization via Specific Combinatorial Tau Phosphorylation Patterns

This study shows that tau phosphorylation patterns influence microtubule stability, with specific phosphorylations impairing tau's ability to counteract destabilization, suggesting phosphorylation may respond to, rather than precede, MT instability.

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.

Structural Insights into the Role of the Proline Rich Region in Tau Function

This study investigates how phosphomimic mutations in tau's proline-rich region affect tubulin dimer binding and microtubule polymerization.

A novel small molecule screening platform for disrupting toxic tau oligomers in cells

The paper develops a FRET-based biosensor platform to screen small molecules targeting toxic tau oligomers, identifying MK-886 as a compound that disrupts tau oligomers and reduces cytotoxicity.