In order to fully understand any complex biochemical system from a mechanistic point of
view, it is necessary to have access to the three-dimensional structures of the molecular …

Septins are conserved from yeast to mammals, but their functions are far better understood
in yeast than in animal cells. This is in part due to the powerful genetic approaches that can …

Septins are a family of conserved cytoskeletal GTPases implicated in a variety of cellular
functions such as cytokinesis and vesicle trafficking. Here, we report identification of an yet …

Septins are GTP binding proteins considered to be novel components of the cytoskeleton.
They polymerize into filaments based on hexameric or octameric core particles in which two …

Septins are able to polymerize into long apolar filaments and have long been considered to
be a component of the cytoskeleton alongside intermediate filaments (which are also apolar …

Septins are an evolutionarily conserved protein family whose members form hetero-
oligomeric complexes that assemble into filaments and higher-order structures. In this issue …

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 …

A Ala alanine I Ile isoleucine R Arg arginine C Cys cysteine K Lys lysine S Ser serine D Asp
aspartate L Leu leucine T Thr threonine E Glu glutamate M Met methionine V Val valine F …

The first identified members of the septin family of cytoskeletal GTPases were originally
discovered in the budding yeast Saccharomyces cerevisiae as crucial regulators of mother …