Arne Gennerich

The paper investigates how the P3018S mutation in dynein affects its function, revealing that the trailing motor in multi-dynein assemblies dictates ensemble velocity.

The paper identifies a conserved salt bridge between KIF1A R350 and -tubulin E415, whose disruption in pathogenic variants correlates with altered motor function.

This study identifies amino acid substitutions in KIF5A from giraffes and pythons that enhance axonal transport speed, revealing convergent evolutionary adaptations for long-distance transport.

The paper examines how different amino acid substitutions at the same KIF1A residue lead to distinct clinical and molecular outcomes in KIF1A-associated neurological disorders.

This study identifies a two-heads-bound state in KIF1A that enhances processivity and is critical for neuronal transport, contrasting with Kinesin-1's one-head-bound state.

The paper shows that mechanical tension recruits a third dynein motor to DDB complexes, enhancing force production and stability under load.

This study shows that KIF5A ΔExon27 mutant causes neuronal toxicity through gain of function by forming aggregates and increasing motor activity.

This study links KIF1A variants to clinical severity in KAND by analyzing transport defects and protein dysfunction.