M. P. M. H. Benoit

The paper presents high-resolution cryo-EM structures of KIF1A-microtubule complexes, revealing the mechanism of processivity and the impact of the P305L mutation on microtubule binding.

This study defines the mechanism of kinesin-8 dual activity by showing how loop-2 regulates motor domain conformation based on tubulin protofilament shape.

This study determines cryo-EM structures of KIF14 bound to microtubules with nucleotide analogues, revealing conformational changes linked to ATP hydrolysis and motor function.

The paper uses cryo-EM to determine the structure of Drosophila kinesin-13 KLP10A bound to tubulin, revealing how it induces microtubule depolymerization through conformational changes.