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 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 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 …

Septins are an example of subtle molecular recognition whereby different paralogues must
correctly assemble into functional filaments important for essential cellular events such as …

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 conserved guanine nucleotide-binding proteins that polymerize into filaments at
the cell cortex or in association with other cytoskeletal proteins, such as actin or …

Septins belong to a family of proteins that is highly conserved in eukaryotes and is
increasingly recognized as a novel component of the cytoskeleton. All septins are GTP …

Septins are a family of GTP-binding proteins that assemble into cytoskeletal filaments.
Unlike other cytoskeletal components, septins form ordered arrays of defined stoichiometry …

Protein-protein interactions play a critical role in promoting the stability of protein quaternary
structure and in the assembly of large macromolecular complexes. What drives the …

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