Evidence map›Paper›PMID 31406248›Full record

ReviewOncogene2019

Eph receptor signalling: from catalytic to non-catalytic functions.

Lung-Yu Liang, Onisha Patel, Peter W Janes, James M Murphy, Isabelle S Lucet

Open access · hybridAbstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 1 synthesis or guideline pooled it, 143 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Modulating pseudokinase conformation from the ATP-binding site.Structure (London, England : 1993) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. The Eph-ephrin system in neuropsychiatric and neurodevelopmental disorders.Journal of psychiatry & neuroscience : JPN · 2026
    Review
  14. Article
  15. Article
  16. The functional landscape of the human ubiquitinome.bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Review

34 more citing papers are in PubMed but not listed here.

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.

Lung-Yu LiangThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.
Onisha PatelThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.
Peter W JanesOlivia Newton-John Cancer Research Institute, 145 Studley Road, Heidelberg, VIC, 3084, Australia.
James M MurphyThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia. jamesm@wehi.edu.au.ORCID http://orcid.org/0000-0003-0195-3949
Isabelle S LucetThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia. lucet.i@wehi.edu.au.ORCID http://orcid.org/0000-0002-8563-8753
The University of Melbourne · AUOlivia Newton-John Cancer Wellness & Research Centre · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eph receptors, the largest subfamily of receptor tyrosine kinases, are linked with proliferative disease, such as cancer, as a result of their deregulated expression or mutation. Unlike other tyrosine kinases that have been clinically targeted, the development of therapeutics against Eph receptors remains at a relatively early stage. The major reason is the limited understanding on the Eph receptor regulatory mechanisms at a molecular level. The complexity in understanding Eph signalling in cells arises due to following reasons: (1) Eph receptors comprise 14 members, two of which are pseudokinases, EphA10 and EphB6, with relatively uncharacterised function; (2) activation of Eph receptors results in dimerisation, oligomerisation and formation of clustered signalling centres at the plasma membrane, which can comprise different combinations of Eph receptors, leading to diverse downstream signalling outputs; (3) the non-catalytic functions of Eph receptors have been overlooked. This review provides a structural perspective of the intricate molecular mechanisms that drive Eph receptor signalling, and investigates the contribution of intra- and inter-molecular interactions between Eph receptors intracellular domains and their major binding partners. We focus on the non-catalytic functions of Eph receptors with relevance to cancer, which are further substantiated by exploring the role of the two pseudokinase Eph receptors, EphA10 and EphB6. Throughout this review, we carefully analyse and reconcile the existing/conflicting data in the field, to allow researchers to further the current understanding of Eph receptor signalling.

Indexed as

Signal TransductionAmino Acid SequenceAnimalsCatalysisHumansLigandsReceptors, Eph FamilySequence Homology, Amino AcidEPHA10 protein, humanEPHB6 protein, humanLigandsReceptors, Eph Family

Identifiers

PMID31406248
OpenAlexW2967079898

What OpenQuestion holds

Textmetadata
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.