Thomas Gronemeyer

This study identifies a nucleotide-triggered mechanism that stabilizes the G-interface and enables NC-interface assembly in septins, revealing unidirectional allosteric signaling during filament formation.

The paper identifies a conserved arginine residue critical for maintaining interface integrity in septin protofilaments across species using molecular dynamics simulations and experimental validation.

This study identifies a Myo2-Pea2 complex that anchors Myo2 at the yeast cell cortex, influencing polarisome formation and cell shape.

The paper identifies SEPT9's interaction network using quantitative proteomics, revealing its role in vesicle transport and actin stress fiber attachment.