David H. Johnson

This study shows cholesterol's effect on α-synuclein binding depends on membrane packing state, with cholesterol reducing, enhancing, or having little effect based on lipid composition and curvature.

This paper introduces a recombinant protein platform to measure binding affinity of inducible amphipathic helices to membranes using fluorescence anisotropy.

This study shows that α-Synuclein's structured N-terminal domain and disordered C-terminal domain work together to enhance membrane remodeling through synergistic electrostatic and curvature effects.

The paper develops a bilayer continuum model to predict how lipid composition affects protein curvature sensing in membranes.

This study shows that N-terminal acetylation of alpha-synuclein reduces its dependence on anionic lipids for membrane binding, demonstrating that membrane packing defects alone can drive binding.