Evidence map›Paper›PMID 19836338›Full record

ArticleStructure (London, England : 1993)2009

Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling.

Thomas A Bowden, A Radu Aricescu, Joanne E Nettleship, Christian Siebold, Nahid Rahman-Huq, Raymond J Owens, David I Stuart, E Yvonne Jones

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

60 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Review
  3. Inhibition of EphA4 reduces vasogenic edema after experimental stroke in mice by protecting the blood-brain barrier integrity.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Role of EphA4 in Mediating Motor Neuron Death in MND.International journal of molecular sciences · 2021
    Review
  8. Article
  9. Review
  10. The EphB6 Receptor: Kinase-Dead but Very Much Alive.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Thomas A BowdenDivision of Structural Biology, University of Oxford, Henry Wellcome Building of Genomic Medicine, Roosevelt Drive, Oxford, UK.
A Radu Aricescu
Joanne E Nettleship
Christian Siebold
Nahid Rahman-Huq
Raymond J Owens
David I Stuart
E Yvonne Jones
Centre for Human Genetics · GBUniversity of Oxford · GB

Funding

Cancer Research UK 10976Cancer Research UK C375/A3964Medical Research Council G0500365Medical Research Council G0700232Medical Research Council G0701506Wellcome Trust
6 · The paper itself

Abstract

The EphA4 tyrosine kinase cell surface receptor regulates an array of physiological processes and is the only currently known class A Eph receptor that binds both A and B class ephrins with high affinity. We have solved the crystal structure of the EphA4 ligand binding domain alone and in complex with (1) ephrinB2 and (2) ephrinA2. This set of structures shows that EphA4 has significant conformational plasticity in its ligand binding face. In vitro binding data demonstrate that it has a higher affinity for class A than class B ligands. Structural analyses, drawing on previously reported Eph receptor structures, show that EphA4 in isolation and in complex with ephrinA2 resembles other class A Eph receptors but on binding ephrinB2 assumes structural hallmarks of the class B Eph receptors. This interactive plasticity reveals EphA4 as a structural chameleon, able to adopt both A and B class Eph receptor conformations, and thus provides a molecular basis for EphA-type cross-class reactivity.

Indexed as

Signal TransductionAmino Acid SequenceBinding SitesEphrinsLigandsModels, MolecularMolecular Sequence DataPhylogenyProtein ConformationReceptor, EphA4Structure-Activity RelationshipEphrinsLigandsReceptor, EphA4

Identifiers

PMID19836338
PMCPMC2832735
OpenAlexW2163393645

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.