Tomoki Kita

The paper identifies KLP-6 as a kinesin-3 resistant to ADP inhibition, showing its unique ATP selectivity through sequence and molecular dynamics analysis.

The paper develops a photostable DNA block to study how a pathogenic kinesin mutant affects collective transport with wild-type kinesin, revealing velocity dynamics.

This study shows that the monomeric kinesin-3 motor KLP-6 moves processively along microtubules via its tail domain, explained by a Brownian ratchet model involving conformational changes rather than asymmetric potentials.

This study characterizes KIF1Bβ motor activity using single-molecule assays and C. elegans genetics, showing reduced activity due to a disease mutation.

This study shows that Kid (KIF22) forms a homodimer, moves processively along microtubules, and transports double-stranded DNA, reclassifying it as a processive and dimeric motor.