Codon optimization through biased synonymous substitutions is a characteristic feature of the genomes of generalist fungal parasites and is associated with the colonization of multiple hosts.

Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.

Common ancestries, activities and structural determinants of a modular (bi-)polarization control system encoded in free-living and obligate intracellular α-proteobacteria, including the rickettsial pathogens, are described.

The synthesis capability of some amino acids is lost during the insect evolution, and hymenopteran parasitoids can make up for these deficiencies by altering free amino acid concentrations in host.

The scaffold protein Kidins220 regulates the development of λLC B cells by supporting B cell precursor survival and optimizing pre‑BCR and BCR signaling.

Robust NMR approach allowed simultaneous detection of substrate cleavage site and real-time kinetics of hydrolysis for Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM, and revealed D-alanyl-glycine activity for LytM.

The centromeric protein CENP-T assembles the microtubule-binding interface of kinetochores through direct recruitment of two Ndc80 complexes and indirect recruitment of a third one through the Mis12 complex.

Hepsin is the first protease identified to modulate specific cleavage and secretion of a Zona Pellucida domain protein, uromodulin.

Transcriptomic and genomic analysis provides a resource of 50 primate-specific genes preferentially expressed in neural progenitors of fetal human neocortex, 15 of which are specific to humans.

Centromeric protein M (CENP-M) is required for the stabilization of a quaternary complex that plays a crucial role in kinetochore organization and function.