Global phosphoproteomic analysis in nerve terminal during exocytosis reveals 252 uniquely regulated phosphosites, highlighting complex regulation of active zone proteins at multiple sites and the role of specific kinases/phosphatases.

Myristoylation of a secreted protein, identified in a global myristoylation analysis of the eukaryotic parasite Toxoplasma gondii, is important for host cell invasion.

Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.

A chemically unstable ostrich eggshell peptide survives for at least 3.8 million years at the equator, stabilized by strong mineral interactions.

The extra dimensions in protein sequence space open up indirect paths of adaptation and alleviate the constraint on the selective accessibility to high fitness genotypes.

A cell-sized fully confined space significantly controls the emergence and stability of a protein wave, resulting in intracellular spatiotemporal regulation driven by a reaction-diffusion mechanism.

De novo protein nanoparticles were designed from scratch to present viral glycoprotein antigens, providing a systematic way to study the influence of antigen presentation geometry on immune response.

Viruses drive adaptation at the scale of the whole proteome and not only in antiviral proteins in mammalian hosts.

Motif length plays a critical role in the specification of biological function within a conserved family of RNA-binding proteins.

The heme and HRI-mediated eIF2aP–ATF4 integrated stress response in erythropoiesis has a major global impact, especially under the stress condition of iron deficiency.