Analysis of protein interfaces suggests cotranslational assembly can be an adaptive process, likely serving to minimise non-specific interactions with other proteins in the cell.

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.

The fatty acid binding protein (FABP) family of proteins plays a role in multiple myeloma cell survival and disease progression in vitro and in silico, and thus blocking the FABPs could have anti-cancer effects and prove beneficial for myeloma patients.

Ribosomal proteins Rps27 (eS27) and Rps27l (eS27L) are an ancient pair of duplicated genes that encode functionally interchangeable proteins, yet have been evolutionarily retained because both copies are necessary to achieve protein expression across cell types.

mRNA profiling alone provides an incomplete picture of molecular aging and examination of changes in proteins is essential to understand aging processes that are not transcriptionally regulated.

The dimer destabilizers cause a dimer-to-monomer equilibrium shift favoring the human thymidylate synthase monomer more degradable by the proteasome, thus breaking the long-standing link between inhibition and enhanced expression of the protein to fight cancer drug resistance.

An alternative iron storage system based on a 9.6 megadalton microbial protein compartment is able to sequester and store large amounts of iron.

Proteases from diverse viruses, the first described pathogen-encoded activators of human NLRP1, cleave NLRP1 at a sequence that mimics the viral polyprotein, resulting in inflammasome activation and pro-inflammatory cytokine release.

Interactions in protein complexes can be predicted from evolutionary information from genomic sequences.

In Thermoplasma acidophilum, an archaeon without histones, a DNA-binding protein acquired from bacteria via horizontal gene transfer mediates histone-like chromatin architecture.