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

A new and general mechanism describes the organization of membrane proteins and their cytoplasmic ligands into micrometer-scale clusters, based on polymerization and concomitant phase separation of multivalent proteins.

Intersectin counterparts in yeast recruit WASP and WIP to endocytic sites to establish a robust multivalent SH3 domain-PRM interaction network which gives actin assembly onset a switch-like behavior in vivo.

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.

Binding of multiple LC8 copies to the intrinsically disordered region of the transcription factor ASCIZ exemplifies a new and potentially widespread molecular mechanism for negative feedback regulation.

Binding of a multivalent RNA-binding protein to mRNAs that are able to form pervasive RNA–RNA interactions induces formation of mesh-like condensates, whereas binding of mostly structured mRNAs induces sphere-like condensates.

Nucleolar protein localization involves the phase separation within the nucleolar matrix via three types of multivalent features: acidic tracts, nucleic acid binding domains and arginine-rich low complexity sequences.

Multi-scale simulations reveal a potential, ATP-independent mechanism resulting in the formation of the long-living multi-droplet state by multi-valent, spacer-sticker proteins.

The cryo-EM structure of the human transcription-export THO–UAP56 complex reveals mechanisms of mRNA nuclear export licensing.

The chromosome architectural protein, CTCF, is phosphorylated at Ser²²⁴ in a cell-cycle-dependent manner and abrogation of phosphorylation leads to a cell growth defect.