Evidence map›Paper›PMID 40072232›Full record

ArticleCytoskeleton (Hoboken, N.J.)2025

The PP2A-B56 Binding Site LxxIxE Contributes to Asp-Mediated Spindle Pole Stability.

Margaux Quiniou, Maria C Burns, Aynsley McDermott, Karolina Jaworek, Stacey J Scott, James G Wakefield, Lori Borgal

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
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

7 authors.

Margaux QuiniouDepartment of Biosciences, University of Exeter, Living Systems Institute, Exeter, UK.
Maria C BurnsBiology Department, Mount Saint Vincent University, Halifax, Canada.
Aynsley McDermottBiology Department, Mount Saint Vincent University, Halifax, Canada.
Karolina JaworekDepartment of Biosciences, University of Exeter, Living Systems Institute, Exeter, UK.
Stacey J ScottDepartment of Biosciences, University of Exeter, Living Systems Institute, Exeter, UK.
James G WakefieldDepartment of Biosciences, University of Exeter, Living Systems Institute, Exeter, UK.
Lori BorgalBiology Department, Mount Saint Vincent University, Halifax, Canada.

Funding

Canada Foundation for InnovationMount Saint Vincent UniversityNatural Sciences and Engineering Research Council of CanadaResearch Nova ScotiaRoyal Society
6 · The paper itself

Abstract

The organization of microtubules into a mitotic spindle is critical for animal cell proliferation and involves the cooperation of hundreds of proteins whose molecular roles and regulation are not fully understood. The protein product of the Drosophila gene abnormal spindle, Asp, is a microtubule-associated protein required for correct mitotic spindle formation. To better understand the contribution of Asp to microtubule organization during spindle formation, we reverse-engineered flies to express a version of Asp (Asp

Indexed as

Drosophila ProteinsMicrotubule-Associated ProteinsProtein Phosphatase 2Spindle ApparatusSpindle PolesAnimalsBinding SitesDrosophila melanogasterMicrotubulesDrosophila ProteinsMicrotubule-Associated ProteinsProtein Phosphatase 2aspdrosophilamicrotubulemitosisPP2AspindleWdb

Identifiers

PMID40072232
PMCPMC12701367

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.