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Analytical techniques and computational models reveal novel post-translational modifications on β-myosin heavy chain in the human hearts and highlight their potential as therapeutic targets.

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.

Resolving parallel and concurrent cytokine secretion is essential to studying polyfunctional cytokine-secreting cells, and to differentiating immune response granularity from unwinding the complexity and heterogeneity of cytokine responses.

During hibernation, animals remodel the structure of their relaxed muscle via a protein called myosin and this enables vast temperature changes.

Individual nonmuscle myosin 2 filaments in cells may differ their mechanical and kinetic properties depending on the myosin paralog composition giving the cells a mechanism for fine tuning the output of a given nonmuscle myosin filament.

Shifts in the balance between nucleotide-favorable and nucleotide-unfavorable conformations of myosin motors encode duty ratios and ADP release rates, demonstrating the power of an ensemble perspective for uncovering sequence-function relationships.

Integrative analysis of a Drosophila model of hypertrophic cardiomyopathy demonstrates that prolonged binding of the myosin cross-bridge to actin is a root cause of the disorder.

Class VIII myosins mediate crosstalk between actin and microtubules to position cell division in plants.

The tail domain of Myosin III binds to and cross-links actin bundling protein Espin1 and thus modulates higher order actin bundle structures in cellular processes such as stereocilia and microvilli.

Actin networks form clusters under myosin-induced contractility, while high actin filament treadmilling speed can reshape actin networks into ring-like structures with lower mechanical energy.