Evidence map›Paper›PMID 33188984›Full record

ReviewCurrent opinion in cell biology2021

The state of the septin cytoskeleton from assembly to function.

Benjamin L Woods, Amy S Gladfelter

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
7.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

76 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Local RhoA activation induces septin recruitment.bioRxiv : the preprint server for biology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Septin complexes: Ahead of the curve.Cytoskeleton (Hoboken, N.J.) · 2025
    Article
  19. Animal septins contain functional transmembrane domains.bioRxiv : the preprint server for biology · 2025
    Article
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Benjamin L WoodsBiology Department, University of North Carolina, Chapel Hill, NC, 27599, USA.
Amy S GladfelterBiology Department, University of North Carolina, Chapel Hill, NC, 27599, USA; Marine Biological Laboratory, Woods Hole, MA, 02543, USA. Electronic address: amyglad@unc.edu.
Marine Biological Laboratory · USUniversity of North Carolina at Chapel Hill · US

Funding

Tri-Institutional Molecular Mycology and Pathogenesis Training ProgramT32AI052080 · NIAID · DUKE UNIVERSITY · PI ANDREW ALSPAUGH, JOSEPH HEITMAN · 2003 to 2026
$8.7M
Geometry-dependent assembly of the septin cytoskeletonR01GM130934 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GLADFELTER, AMY S · 2019 to 2022
$1.2M
NIAID NIH HHS T32 AI052080NIGMS NIH HHS R01 GM130934
6 · The paper itself

Abstract

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 microtubules. As integral players in many morphogenic and signaling events, septins form scaffolds important for the recruitment of the cytokinetic machinery, organization of the plasma membrane, and orientation of cell polarity. Mutations in septins or their misregulation are associated with numerous diseases. Despite growing appreciation for the importance of septins in different aspects of cell biology and disease, septins remain relatively poorly understood compared with other cytoskeletal proteins. Here in this review, we highlight some of the recent developments of the last two years in the field of septin cell biology.

Indexed as

ActinsAnimalsCell MembraneCell PolarityCytoplasmCytoskeletonEukaryotic CellsFungiHumansMicrotubulesMultiprotein ComplexesPolymerizationSeptinsActinsMultiprotein ComplexesSeptinsAmphipathic helix (AH) domain

Identifiers

PMID33188984
PMCPMC7952027
OpenAlexW3103409224

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.