S. Niwa

The paper investigates the role of the FHA domain in regulating dimerization of DmUNC-104 and links abnormal dimerization to human diseases.

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

This paper develops mathematical models to explain the motility of KIF1A heterodimers, showing that a coordinated head model better predicts experimental results than an independent head model.

This study compares KLP-6 and UNC-104, two Caenorhabditis elegans kinesin-3 proteins, revealing that autoinhibition release triggers dimerization and processive movement in UNC-104 but not in KLP-6.

The paper demonstrates that recombinant H2 monoclonal antibody performs equivalently to hybridoma-derived H2 in detecting KHCs and ALS-associated aggregates.

This study shows that an ALS-associated KIF5A mutant forms oligomers and aggregates, leading to neuronal toxicity rather than loss of function.

The paper reports the crystal structure of KLP-12-tubulin complex, revealing how KLP-12 inhibits microtubule dynamics by altering tubulin curvature.

The paper applies extreme-value analysis to study motor protein transport in C. elegans neurons, finding differences in distribution shape parameters between anterograde and retrograde transport.

This study establishes C. elegans models for KIF1A-associated neuronal disorder and shows that disease mutations inhibit wild-type KIF1A function in heterodimers.

The paper measures how dynarrestin affects motor protein transport by estimating force-producing units in hippocampal neurons.

This study reconstitutes kinesin-1 activation in vitro, revealing that KLC-based inhibition and cargo-adaptor binding regulate motor activity, with a third non-motor MAP required for robust motility.

The paper shows CAMSAP2 nucleates microtubules from soluble β-tubulin without γ-tubulin, reducing the nucleation barrier and forming aster-like structures.

This study identifies a conserved 310-helix in KIF1A critical for motor function and human health, showing that the P305L mutation disrupts microtubule association and motor performance.

This study shows that disease-associated KIF1A mutations hyperactivate motor activity, leading to increased anterograde axonal transport of synaptic vesicle precursors and contributing to motor neuron disease.