Evidence map›Paper›PMID 23321313›Full record

ArticleBiochemical and biophysical research communications2013

Filamentous fungal-specific septin AspE is phosphorylated in vivo and interacts with actin, tubulin and other septins in the human pathogen Aspergillus fumigatus.

Praveen Rao Juvvadi, Detti Belina, Erik J Soderblom, M Arthur Moseley, William J Steinbach

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  8. Article
  9. Caspofungin exposure alters the core septin AspB interactome of Aspergillus fumigatus.Biochemical and biophysical research communications · 2017
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Septins and Generation of Asymmetries in Fungal Cells.Annual review of microbiology · 2015
    Review
  18. Article
  19. Article
  20. 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

5 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.
Detti Belina
Erik J Soderblom
M Arthur Moseley
William J Steinbach
Duke University · USDuke Medical Center · US

Funding

Identification of calcineurin-binding proteins in A. fumigatus septum formationR21AI097541 · NIAID · DUKE UNIVERSITY · PI STEINBACH, WILLIAM J · 2012 to 2013
$420k
NIAID NIH HHS 1R21AI097541-01A1NIAID NIH HHS R21 AI097541
6 · The paper itself

Abstract

We previously analyzed the differential localization patterns of five septins (AspA-E), including a filamentous fungal-specific septin, AspE, in the human pathogen Aspergillus fumigatus. Here we utilized the A. fumigatus strain expressing an AspE-EGFP fusion protein and show that this novel septin with a tubular localization pattern in hyphae is phosphorylated in vivo and interacts with the other septins, AspA, AspB, AspC and AspD. The other major proteins interacting with AspE included the cytoskeletal proteins, actin and tubulin, which may be involved in the organization and transport of the septins. This is the first report analyzing the phosphorylation of AspE and localizing the sites of phosphorylation, and opens opportunities for further analysis on the role of post-translational modifications in the assembly and organization of A. fumigatus septins. This study also describes the previously unknown interaction of AspE with the actin-microtubule network. Furthermore, the novel GFP-Trap® affinity purification method used here complements widely-used GFP localization studies in fungal systems.

Indexed as

Protein Processing, Post-TranslationalActinsAmino Acid SequenceAspergillus fumigatusConserved SequenceGreen Fluorescent ProteinsHumansMolecular Sequence DataPhosphorylationProtein Structure, TertiarySeptinsTubulinActinsenhanced green fluorescent proteinGreen Fluorescent ProteinsSeptinsTubulin

Identifiers

PMID23321313
PMCPMC3587984
OpenAlexW2048167612

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.