Evidence map›Paper›PMID 23628727›Full record

ReviewBiochimica et biophysica acta2013

Eph/ephrin recognition and the role of Eph/ephrin clusters in signaling initiation.

Dimitar B Nikolov, Kai Xu, Juha P Himanen

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.1field-weighted citation impact, top 3% 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

54 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Normal muscle fiber type distribution is recapitulated in aged ephrin-A3American journal of physiology. Cell physiology · 2023
    Article
  9. Geometric Control of Cell Behavior by Biomolecule Nanodistribution.ACS biomaterials science & engineering · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Eph Receptors and Ephrins in Retinal Diseases.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Discoidin domain receptors: Micro insights into macro assemblies.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Dimitar B NikolovStructural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA. Electronic address: nikolovd@mskcc.org.
Kai Xu
Juha P Himanen
Memorial Sloan Kettering Cancer Center · US

Funding

STRUCTURAL STUDY OF EPH RECEPTORS AND EPHRINSR01NS038486 · NINDS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI NIKOLOV, DIMITAR B · 1999 to 2018
$5.9M
NINDS NIH HHS R01 NS038486NINDS NIH HHS R01NS038486
6 · The paper itself

Abstract

The Eph receptors and their ephrin ligands play crucial roles in a large number of cell-cell interaction events, including those associated with axon pathfinding, neuronal cell migration and vasculogenesis. They are also involved in the patterning of most tissues and overall cell positioning in the development of the vertebrate body plan. The Eph/ephrin signaling system manifests several unique features that differentiate it from other receptor tyrosine kinases, including initiation of bi-directional signaling cascades and the existence of ligand and receptor subclasses displaying promiscuous intra-subclass interactions, but very rare inter-subclass interactions. In this review we briefly discuss these features and focus on recent studies of the unique and expansive high-affinity Eph/ephrin assemblies that form at the sites of cell-cell contact and are required for Eph signaling initiation. This article is part of a Special Issue entitled: Emerging recognition and activation mechanisms of receptor tyrosine kinases.

Indexed as

Signal TransductionCell AdhesionCell CommunicationCell LineCell MovementCluster AnalysisEphrinsGene Expression RegulationHumansLigandsModels, MolecularProtein BindingReceptors, Eph FamilyEphrinsLigandsReceptors, Eph FamilyEphEphrinKinaseReceptorSignaling

Identifiers

PMID23628727
PMCPMC3777820
OpenAlexW2031967537

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.