ArticleFrontiers in cell and developmental biology2022
Biochemical Characterization of a Human Septin Octamer.
Article in Frontiers in cell and developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Interface integrity in septin protofilaments is maintained by an arginine residue conserved from yeast to man.Molecular biology of the cell · 2025Article
- Dysregulation of septin cytoskeletal organization in the trabecular meshwork contributes to ocular hypertension.JCI insight · 2024Article
- The structure of a tetrameric septin complex reveals a hydrophobic element essential for NC-interface integrity.Communications biology · 2024Article
- Septin and actin contributions to endothelial cell-cell junctions and monolayer integrity.Cytoskeleton (Hoboken, N.J.)Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Septins are part of the cytoskeleton and polymerize into non-polar filaments of heteromeric hexamers or octamers. They belong to the class of P-loop GTPases but the roles of GTP binding and hydrolysis on filament formation and dynamics are not well understood. The basic human septin building block is the septin rod, a hetero-octamer composed of SEPT2, SEPT6, SEPT7, and SEPT9 with a stoichiometry of 2:2:2:2 (2-6-7-9-9-7-6-2). Septin rods polymerize by end-to-end and lateral joining into linear filaments and higher ordered structures such as rings, sheets, and gauzes. We purified a recombinant human septin octamer from
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Registered trials
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