G. A. Voth

This study uses molecular dynamics simulations to explain the structural basis for the asymmetric polymerization rates of actin filament ends.

This study determines the structure of human ESCRT-I and shows it forms a helical assembly that scaffolds and mechanically drives membrane scission during HIV-1 budding.

The paper uses molecular dynamics to study how the HIV-1 Gag matrix domain binds to lipid membranes, focusing on Myr insertion and interactions with PIP2 and PS lipids.

This study uses molecular dynamics simulations to show how capsid inhibitors disrupt HIV-1 capsid assembly, leading to structural defects and disassembly, and highlights the importance of dynamic mechanisms in drug design.

The paper develops a computational model to study how integrin nanoscale properties influence adhesion assembly and stability.

The paper investigates how mechanical and kinetic factors influence the sorting of F-actin crosslinkers on bundles, showing a non-monotonic dependence on polymerization rate.

This study shows Ena/VASP tetramers enhance processivity on fascin-bundled actin filaments through avidity, increasing run length with more filaments and arms.

This paper shows that entropic forces drive M2 protein clustering and spatial localization during influenza viral budding, contributing to membrane curvature and scission.

This paper develops a multiscale UCG model to study ATP hydrolysis and Pi release in actin filaments, showing cooperativity affects filament dynamics near critical monomer concentrations.

This study identifies two gating mechanisms by which formin FH2 domains regulate actin filament elongation rates through steric blockage and helical flattening.

This paper shows that cell spreading on soft substrates is inhibited by reduced adhesion formation in the lamellipodium, independent of myosin II activity.

This study investigates how HIV-1 Gag polyprotein assembly is regulated by RNA and the plasma membrane using computational and experimental methods, revealing scaffolding roles for these components.