W. O. Hancock

This study uses single-molecule fluorescence microscopy to show that lignin impairs Cel7A degradation of cellulose by blocking access and hindering enzyme movement, rather than acting as a sink.

This study uses single-molecule tracking to show that cellobiose inhibits Cel7A cellulase by binding to both the product release site and the substrate binding tunnel.

The paper resolves a debate on microtubule dynamics by showing that interfacial nucleotides determine tubulin:tubulin interaction strength through experimental and simulation studies.

The paper investigates how kinesin-1, -2, and -3 motors compete with dynein during bidirectional transport and finds that all three families can withstand hindering loads through distinct kinetic strategies.

This study shows that the net charge of the K-loop in KIF1A enhances microtubule affinity in the one-head-bound state, increasing run length and processivity.

The paper uses simulations to study kinesin and dynein motor dynamics in bidirectional transport, finding that matched stall forces and independent detachment rates best replicate experimental velocity distributions.

This study uses optical tweezers to show KIF1A generates higher force and sustains longer attachment under hindering loads compared to KIF5B, with rapid microtubule reengagement.

The paper measures microtubule growth dynamics using interference reflection microscopy and models the effects of GTP hydrolysis, revealing that GDP exposure at the microtubule end increases growth fluctuations and suggests slow association kinetics.

The paper introduces a multimodal microscope combining IRM and TIRFM to image processive enzymes with high precision.

This study uses single-molecule tracking to analyze the dynamics of TrCel7A cellulase binding and movement along cellulose, revealing a three-state model with static and processive states.

This study elucidates the chemomechanical cycle of KIF1A, revealing that it predominantly resides in a one-head-bound state during its cycle, with fast rear head detachment and tethered head attachment as key rate-limiting steps.

The paper measures the microtubule binding kinetics of membrane-bound kinesin-1 motors and finds that motor reattachment is not limited by diffusion but by intrinsic binding rates, predicting high motor copy numbers for long-range vesicle transport.

This study investigates the function of kinesin-2 motors in C. reinhardtii, showing that FLA8/10 is auto-inhibited and activated by KAP subunit heterotrimerization for fast intraflagellar transport.

The paper uses iSCAT microscopy to analyze dynein-dynactin-BicD2 motility, finding that p150 reduces diffusive behavior and enhances processive movement.

This study identifies Eg5 as a microtubule polymerase that promotes microtubule growth by inducing a curved-to-straight transition in tubulin.

This study shows that PAKRP2, an orphan kinesin in Arabidopsis, moves processively along microtubules using a noncanonical stepping mechanism with small steps and lateral movements.

The paper directly measures tubulin on- and off-rates at growing microtubule tips using interferometric scattering microscopy and computational modeling.

The paper introduces a curvature distribution method to measure the persistence length of cytoskeletal filaments, showing it is more accurate for small datasets and applicable to both in vitro and in vivo data.

This study investigates how motor reattachment kinetics influence multi-motor-driven cargo transport, finding that kinesin-2's faster reattachment rate enhances cargo movement and navigation.