Evidence map›Paper›PMID 21219860›Full record

ArticleBiochemical and biophysical research communications2011

Differential localization patterns of septins during growth of the human fungal pathogen Aspergillus fumigatus reveal novel functions.

Praveen Rao Juvvadi, Jarrod R Fortwendel, Luise E Rogg, William J Steinbach

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Cell Biology of Hyphal Growth.Microbiology spectrum · 2017
    Review
  8. Caspofungin exposure alters the core septin AspB interactome of Aspergillus fumigatus.Biochemical and biophysical research communications · 2017
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
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  18. Article
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

4 authors at 2 institutions in 1 country.

Praveen Rao JuvvadiDivision of Pediatric Infectious Diseases, Department of Pediatrics, Duke University Medical Center, Durham, NC 27710, USA.
Jarrod R Fortwendel
Luise E Rogg
William J Steinbach
Duke Medical Center · USDuke University Hospital · US

Funding

Identification of calcineurin-binding proteins in A. fumigatus septum formationR21AI097541 · NIAID · DUKE UNIVERSITY · PI STEINBACH, WILLIAM J · 2012 to 2013
$420k
Calcineurin Inhibition to Halt Aspergillus fumigatus Hyphae and VirulenceR56AI077648 · NIAID · DUKE UNIVERSITY · PI STEINBACH, WILLIAM J · 2010 to 2010
$393k
NIAID NIH HHS R21 AI097541NIAID NIH HHS R56 AI077648
6 · The paper itself

Abstract

Septins, a conserved family of GTPases, are heteropolymeric filament-forming proteins that associate with the cell membrane and cytoskeleton and serve essential functions in cell division and morphogenesis. Their roles in fungal cell wall chitin deposition, septation, cytokinesis, and sporulation have been well established and they have recently been implicated in tissue invasion and virulence in Candida albicans. Septins have never been investigated in the human pathogenic fungus, Aspergillus fumigatus, which is a leading cause of death in immunocompromised patients. Here we localize all the five septins (AspA-E) from A. fumigatus for the first time, and show that each of the five septins exhibit varied patterns of distribution. Interestingly AspE, which is unique to filamentous fungi, and AspD, belonging to the CDC10 class of septins, localized prominently to tubular structures which were dependent on actin and microtubule networks. Localization of AspD and AspE has never been reported in filamentous fungi. Taken together these results suggest that septins in A. fumigatus might have unique functions in morphogenesis and pathogenicity.

Indexed as

Aspergillus fumigatusFungal ProteinsHumansHyphaeMicrotubulesSeptinsFungal ProteinsSeptins

Identifiers

PMID21219860
PMCPMC3045080
OpenAlexW2054036430

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.