William Olaf Hancock

This study measures detachment kinetics of kinesin-1, -2, and -3 under parallel forces using a DNA tensiometer, revealing load-dependent behavior and competition with dynein.

This study investigates the bidirectional motility of Cin8 kinesin-5 dimers, finding a plus-end bias and weak inter-head coordination, suggesting directional switching is regulated by coordination levels.

This study shows that the carbohydrate-binding module (CBM1) of TrCel7A improves enzyme binding and navigation on complex plant cell wall substrates.

The paper generalizes Michaelis-Menten theory to account for substrate heterogeneity, showing that apparent parameters depend on mean and variance of energy distributions.

This study identifies a new tubulin binding state on microtubule ends using single-molecule measurements and shows nucleotide effects on stability are allosteric.

The paper demonstrates that motor clustering enhances kinesin-driven vesicle transport efficiency, reducing the required number of motors for long-distance transport.

The paper investigates how different cargo adaptors influence the kinetics and mechanism of dynein-dynactin complex formation, revealing distinct assembly pathways and stable tripartite complexes.

This paper develops a single-molecule microscopy assay to measure PETase enzyme kinetics, revealing distinct binding dynamics between wild-type and a hyperactive mutant.

This study uses single-molecule microscopy to show that xylan inhibits cellulase binding and processivity on cellulose fibrils, highlighting the need for xylan removal in biomass processing.