The intrinsically-disordered protein MEG-3 recruits mRNAs to P granules by forming gel-like condensates with ribosome-depleted mRNAs.

The resurrection of ancient ancestral intrinsically disordered proteins reveals the evolution of a protein-protein interaction in molecular detail.

A combination of NMR, fluorescence, and molecular dynamics simulations reveals the recognition mechanism for the intrinsically disordered regulator of protein kinase A, highlighting the enzyme's nuclear export process.

Computational modeling and theoretical analysis reveal how disordered linkers determine whether linear multivalent proteins undergo gelation with or without phase separation.

A statistical model systematically associates functions of intrinsically disordered regions with sequence-distributed molecular features such as charge, residue composition, or repeat content.

Simple biophysical considerations explain the collective behavior of molecularly diverse complex protein assemblies that regulate transport between the nucleus and the cytoplasm in eukaryotic organisms.

Two small, energy independent stress effectors are able to counteract all of the major insults imposed by severe water loss.

The MEG (maternal-effect germline defective) proteins, MEG-1, 2, 3 and 4, regulate RNA granule dynamics in vivo.

A structure-function analysis of the YAP:TEAD interaction permits a thermodynamic mapping of this interface.

A competition for RNA drives the localized assembly of RNA granules in the C. elegans embryo.