Mohtadin Hashemi

This study uses molecular dynamics simulations to show that membrane curvature influences Aβ42 aggregation by altering peptide-lipid interactions and conformational dynamics.

This study uses molecular dynamics simulations to show that early α-synuclein association with Aβ42 oligomers depends on their initial configuration, with distinct interaction patterns observed based on Aβ42's oligomeric state.

This study compares membrane structural properties across different system sizes and hydration levels, and evaluates four analysis software tools for their performance and consistency.

This study uses atomic force microscopy to visualize APE1-DNA interactions, revealing APE1's affinity for G-rich DNA and its ability to form loops between DNA segments.

The paper shows that Aβ42 monomers at lipid membranes self-assemble into aggregates at low concentrations, with the membrane acting as a catalyst.

This study shows phospholipid bilayers catalyze α-synuclein aggregation from monomers, with efficiency depending on membrane composition and leading to dissociable aggregates.