Septins constitute a group of GTP-binding proteins involved in cytokinesis and other
essential cellular functions. They form heterooligomeric complexes that polymerize into …

Septins form oligomeric complexes consisting of septins from different subgroups, which
form filaments that are involved in a number of biological processes. They are GTP-binding …

Septin proteins bind GTP and heterooligomerize into filaments with conserved functions
across a wide range of eukaryotes. Most septins hydrolyze GTP, altering the oligomerization …

Septins are conserved GTP-binding proteins that assemble into hetero-oligomeric
complexes and higher-order structures such as filaments, rings, hourglasses or gauzes …

Septins form a conserved family of filament forming GTP binding proteins found in a wide
range of eukaryotic cells. They share a common structural architecture consisting of an N …

Septins are a conserved family of eukaryotic GTP-binding, filament-forming proteins. In
Saccharomyces cerevisiae, five septins (Cdc3p, Cdc10p, Cdc11p, Cdc12p, and Shs1p) form …

Septins comprise a conserved family of GTPases important in cytokinesis. These proteins
polymerize into filaments from rod-shaped heteromeric septin complexes. Septins interact …

Septins are GTP-binding proteins that form ordered, rod-like multimeric complexes and
polymerize into filaments, but how such supramolecular structure is related to septin function …

Septins are GTP-binding proteins that assemble into homo-and hetero-oligomers and
filaments. Although they have key roles in various cellular processes, little is known …

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 …