Evidence map›Paper›PMID 29889908›Full record

ArticlePloS one2018

Binding of EphrinA5 to RET receptor tyrosine kinase: An in vitro study.

Yixin Liu, Heidi Kaljunen, Ana Pavić, Tuulia Saarenpää, Juha P Himanen, Dimitar B Nikolov, Adrian Goldman

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 59% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Structural basis for pseudokinase-mediated regulation of GCN2 in the integrated stress response.Proceedings of the National Academy of Sciences of the United States of America · 2026
    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

7 authors at 3 institutions in 3 countries.

Yixin LiuMolecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.ORCID 0000-0003-1135-2805
Heidi KaljunenMolecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
Ana PavićMolecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
Tuulia SaarenpääMolecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
Juha P HimanenStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, United States.
Dimitar B NikolovStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, United States.
Adrian GoldmanMolecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
University of Helsinki · FIMemorial Sloan Kettering Cancer Center · USUniversity of Leeds · GB

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
STRUCTURAL STUDY OF EPH RECEPTORS AND EPHRINSR01NS038486 · NINDS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI NIKOLOV, DIMITAR B · 1999 to 2018
$5.9M
Biotechnology and Biological Sciences Research Council BB/M021610/1NCI NIH HHS P30 CA008748NINDS NIH HHS R01 NS038486
6 · The paper itself

Abstract

Eph/Ephrin signaling pathways are crucial in regulating a large variety of physiological processes during development, such as cell morphology, proliferation, migration and axonal guidance. EphrinA (efn-A) ligands, in particular, can be activated by EphA receptors at cell-cell interfaces and have been proposed to cause reverse signaling via RET receptor tyrosine kinase. Such association has been reported to mediate spinal motor axon navigation, but conservation of the interactive signaling pathway and the molecular mechanism of the interaction are unclear. Here, we found Danio rerio efn-A5b bound to Mus musculus EphA4 with high affinity, revealing structurally and functionally conserved EphA/efn-A signaling. Interestingly, we observed no interaction between efn-A5b and RET from zebrafish, unlike earlier cell-based assays. Their lack of association indicates how complex efn-A signaling is and suggests that there may be other molecules involved in efn-A5-induced RET signaling.

Indexed as

Signal TransductionAnimalsCell LineEphrin-A5In Vitro TechniquesMiceMotor NeuronsProtein BindingProto-Oncogene Proteins c-retReceptor, EphA4Sf9 CellsZebrafishZebrafish ProteinsEfnA5b protein, zebrafishEphrin-A5Proto-Oncogene Proteins c-retReceptor, EphA4Ret protein, zebrafishZebrafish Proteins

Identifiers

PMID29889908
PMCPMC5995387
OpenAlexW2808642814

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.