In mice, cyclic di-GMP is an effective mucosal pneumococcal vaccine adjuvant that stimulates the immune response via two distinct mechanisms.

A newfound signaling enzyme that diverged from a protein family ubiquitous in bacteria provides mechanistic insights into how new signaling activity emerges to control distinct cellular function and physiology.

Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.

Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.

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 flip of the dimer asymmetry following the first ATP hydrolysis provides a mechanistic model for client remodeling by the mitochondrial Hsp90, TRAP1.

Subpopulations of polysaccharide producer and surface explorer cells play specialized roles in early Pseudomonas aeruginosa biofilm formation.

High resolution SthK channel cryo-EM structures in different ligand-bound states combined with single-channel functional data in the same conditions constrain a gating mechanism for CNG channels.

Cell-penetrating peptide drugs prevent adrenergic regulation of pacemaker channels without altering the overall response of the cell to cAMP.

The entire biosynthetic pathway for the diterpenoid forskolin in Coleus forskohlii has been reconstituted in yeast.