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.

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.

X-ray crystallography reveals how kinesin-1 recognises a novel class of cargo adaptor motifs in an isoform-specific manner.

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.

In the microbe Chlamydomonas reinhardtii, a disassembly rate which depends on flagellar length provides an effective method to regulate the length of its two flagella.

The self-organised beat of cilia and flagella is dynamically regulated by curvature.

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.

Microtubule attachment fundamentally modifies kinesin's behavior by triggering a ‘clamshell’ opening of the nucleotide cleft, subsequently reversed by ATP binding, that couples to cargo translocation.