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Formation and cell pole-localization of chemotactic signaling-arrays is a coupled process mediated by ParP, which drives localized array-assembly and regulates the localization-dynamics of its network constituents.

CryoEM reveals the structure of a two-component archaeal S-layer, which sheds new light on archaeal cell biology.

Chronic bacteriophages are induced by the supplement of polysaccharide in the deep-sea Lentisphaerae strains, and these bacteriophages potentially reprogram host polysaccharide metabolism through the auxiliary metabolic genes.

Computational analyses and biochemical measurements redefine the mechanisms by which pyrin-only-proteins specifically target and regulate the assembly of inflammasomes.

Bacterial cytoplasmic chemoreceptors assemble into a sandwich of two hexagonally packed arrays.

Proteins locked into the immature HIV lattice can exploit its incomplete structure to form the essential protease dimer needed for viral maturation.

Precise control of microtubule architecture greatly increases the force that the spindle can exert on chromosomes.

A general mechanism for how powerful forces of assembly and protein mobility can emerge from phase transitions is established.

Actin is incorporated into the thin-filament arrays of skeletal muscle sarcomeres in discrete steps, and Fhos, the Drosophila homolog of FHOD-family formins, is an essential player in the process.

The Bipolar Assembly domain of kinesin-5 comprises an anti-parallel four-helix bundle, which explains how kinesin-5 subunits assemble into bipolar tetramers with two motile ends that transmit forces while crosslinking and sliding adjacent microtubules during mitosis.