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.

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.

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.

Computer simulations of model proteins with sticker-and-spacer architectures shed light on the formation of biomolecular condensates in cells.

Simultaneous phosphorylation of multiple substrate motifs drives switch-like target recognition and monoubiquitylation by an E3 ligase during metazoan development.

Certain types of 3D chromatin loops are easy to predict from existing or easily obtainable 2D information, which benefits gene expression studies in tissues/cells/organisms without extensive pre-existing 3D information.