Yuri L. Lyubchenko

This study shows that Aβ42 removes cholesterol from membranes, accelerating its aggregation and contributing to Alzheimer's disease pathology.

This study uses AFM to analyze the nanoscale structure and dynamics of CENP-A and canonical H3 nucleosomes, revealing differences in internucleosomal interactions and DNA unwrapping behavior.

This study investigates how NF-κB interacts with H3nuc and CENP-Anuc, finding that it unravels H3nuc but not CENP-Anuc.

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.

This study investigates the structure of CENP-A nucleosomes on different DNA sequences using Atomic Force Microscopy, finding that -satellite DNA supports more stable nucleosome complexes compared to non-specific DNA.

The paper compares neurotoxicity of human A53T and mouse α-synuclein variants, finding mouse aSyn is less toxic due to C-terminal substitutions reducing membrane-induced aggregation and vesicle permeabilization.

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.

The paper develops a molecular model explaining how surface interactions accelerate protein aggregation, validated through experiments with synuclein and APOBEC3G.