Roland Brandt

The paper designs and characterizes PTX analogues to separate MT stabilization from structural changes, showing that compound 1b preserves native MT structure and physiological Tau dynamics.

This paper designs a synthetic peptide mimicking Hsp90-Tau interaction to inhibit Tau aggregation and restore its microtubule binding, showing efficacy in vitro and in cells.

This study shows hydrogen peroxide modulates axonal microtubule dynamics and induces distinct phosphorylation patterns in microtubule proteins through specific signaling pathways.

This paper uses peptidomimetic foldamers to study tau misfolding by inducing specific conformations of PHF6 and PHF6* sequences, showing that extended conformations drive aggregation while β-hairpins prevent it.

The paper uses live-cell imaging to identify a drug candidate that restores microtubule regulation by targeting tau aggregation and phosphorylation in a tauopathy model.

This study shows that tau and α-synuclein regulate microtubule organization and transport in neuronal dendrites, with tau deficiency increasing dendritic complexity and transport efficiency.