Septin GTP-binding proteins contribute essential biological functions that range from the
establishment of cell polarity to animal tissue morphogenesis. Human septins in cells form …

Septins are GTP-binding and membrane-interacting proteins with a highly conserved
domain structure involved in various cellular processes, including cytoskeleton organization …

Septins are members of a conserved family of cytoskeletal GTPases present in organisms as
diverse as yeast and mammals. Unlike lower eukaryotic cells, the physiological significance …

The septins are filament‐forming proteins found in diverse eukaryotes from fungi to
vertebrates, with roles in cytokinesis, shaping of membranes and modifying cytoskeletal …

Septins are filament-forming proteins important for organizing the cortex of animal and
fungal cells. In mammals, 13 septin paralogues were recently shown to assemble into core …

Septin-family proteins assemble into rod-shaped heteromeric complexes that form higher-
order arrangements at the cell cortex, where they serve apparently conserved functions as …

Septins are a cytosolic GTP-binding protein family first characterized in yeast, but gaining
increasing recognition as critical protagonists in higher eukaryotic cellular events …

Septins are conserved GTP-binding proteins that assemble into lateral diffusion barriers and
molecular scaffolds. Vertebrate genomes contain 9–17 septin genes that encode both …

Septins are a conserved family of polymerizing guanine nucleotide binding proteins
associated with diverse processes in dividing and non-dividing cells. In humans, 12 septin …

Septins are a family of proteins highly conserved in eukaryotes that have been under
intense scrutiny lately because they appear to comprise a novel component of the …