ESCRT-III heteropolymers utilize non-specific lateral electrostatic interactions to recognize one another, which may enable the polymers to slide along one another and adapt to different curvatures.

Theoretical scenario for prebiotic polymers capable of nonenzymatic replication to acquire an early catalytic function, specifically cleavage activity.

Electron microscopy on native membranes reveals the shape and potential function of protein machinery responsible for budding vesicles and viruses away from the cytoplasm.

Laterally associating specific ESCRT-III subunits can replace one another with simple modifications, providing insights into the design principles of ESCRT-III heteropolymerization.

Post-phosphoryl modification of α-dystroglycan requires the glucuronyltransferase B4GAT1; this enzyme synthesizes the acceptor glycan that serves as a primer for the glycosyltransferase LARGE to synthesize the laminin-binding glycan.

A colloid fractal cluster model provides a quantitative link between the atomistic features of an intrinsically disordered polypeptide and the spatial organization of the biomolecular condensate it forms.

By partitioning promiscuous enzymes across multiple Golgi compartments, eukaryotic cells can tightly control the synthesis of complex sugar oligomers.

The corkscrew-like motility of Spirochete bacteria is enabled by a unique, asymmetrically constructed flagellum that wraps around the cell body within the periplasm.

Mycobacteria employ plasma membrane compartments to organize their cell wall synthesis, and the finalized cell wall compartmentalizes the plasma membrane to promote an environment conducive to its own synthesis.