L. Gheber

This study investigates how the structural features of kinesin-5, specifically tail-motor domain interactions and minifilament length, influence microtubule sliding motility and spindle organization.

This study reveals that directionality switching of kinesin-5 Cin8 motors is caused by an asymmetric response to drag forces, identified through cluster-motility analysis and biophysical modeling.

This study shows that flexibility of the neck-linker during docking is essential for the function of bi-directional kinesin motors.

This study shows the kinesin-5 tail domain regulates motor activity by modulating ATP hydrolysis and microtubule sliding, leading to slow motility and force generation.