Septins, a highly conserved family of GTP-binding proteins, were originally identified in a
genetic screen for S. cerevisiae mutants defective in cytokinesis [1, 2]. In yeast, septins …

Septins, a conserved family of GTP-binding proteins with a conserved role in cytokinesis, are
present in eukaryotes ranging from yeast to mammals. Septins are also highly expressed in …

Septins are GTP-binding proteins that polymerize into heteromeric filaments and form
microscopic bundles or ring structures in vitro and in vivo. Because of these properties and …

The septins constitute a family of GTPase proteins that are involved in many cytological
processes such as cytokinesis and exocytosis. Previous studies have indicated that …

The septins are GTPase enzymes with multiple roles in cytokinesis, cell polarity or
exocytosis. The proteins from the mammalian septin genes are called Sept1–10. Most are …

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 a conserved eukaryotic family of GTP-binding filament-forming proteins with
functions in cytokinesis and other processes. In the budding yeast Saccharomyces …

Septins are a family of conserved proteins that have been implicated in a variety of cellular
functions involving specialized regions of the cell cortex and changes in cell shape. The …

Septins are GTP-binding proteins that form filaments and higher-order structures on the cell
cortex of eukaryotic cells and associate with actin and microtubule cytoskeletal networks …

Septins are a family of conserved guanosine triphosphate/guanosine diphosphate-binding
proteins implicated in a variety of cellular functions such as cell cycle control and …