Microtubule streaming driven by molecular motors covers characteristic times that span several orders of magnitude from fast, single-microtubule sliding on molecular scales to slow, collective motion on cellular scales.

The small molecule EMD 57033 is one of a new class of pharmacological chaperones that stabilize, enhance the activity of, and correct stress-induced misfolding of myosin proteins.

Single molecule imaging reveals how the molecular motor myosin 5 walks in a compass-like spinning motion along its actin track resulting in efficient, robust and unidirectional motion on the nanoscale.

The motor protein kinesin utilizes its fuel molecule by active and concerted motions of its subdomains, while it rapidly interacts with the microtubule track by forming a wet and dynamic interface.

A general framework for gating reveals that inter-head tension is not essential for coordinating kinesin stepping, and that neck-linker length is tuned to enhance processivity and velocity.

Unlike other cytoskeletal motors that produce torque in a specific direction, cytoplasmic dynein generates torque in either direction, resulting in bidirectional helical motility along microtubules.

Microtubule networks in frog egg extracts can spontaneously contract in a manner that can be quantitatively described by an active fluid model.

Conditional deletion of the DYT1 dystonia protein torsinA causes selective cell autonomous neurodegeneration of striatal and brainstem cholinergic neurons, and severe motor behavioral abnormalities.

In vitro reconstitution of mRNA motility reveals the basis of directionally biased motion by groups of motors, their response to potential obstacles, and the consequences of reaching microtubule ends.

Force generation by kinesin motor proteins requires formation of both a 2-stranded cover-neck bundle and an asparagine-based latch for transport of membrane-bound cargoes in cells.