Evidence map›Paper›PMID 22040918›Full record

ReviewSeminars in cell & developmental biology2012

Eph/ephrin signaling: genetic, phosphoproteomic, and transcriptomic approaches.

Jeffrey O Bush, Philippe Soriano

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Understanding craniosynostosis as a growth disorder.Wiley interdisciplinary reviews. Developmental biology · 2016
    Review
  10. Article
  11. Article
  12. Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".BioEssays : news and reviews in molecular, cellular and developmental biology · 2015
    Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Eph receptor signaling and ephrins.Cold Spring Harbor perspectives in biology · 2013
    Review
  18. Article
  19. 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

2 authors.

Jeffrey O BushDepartment of Cell and Tissue Biology and Program in Craniofacial and Mesenchymal Biology, University of California at San Francisco, San Francisco, CA 94143, USA. jeffrey.bush@ucsf.edu
Philippe Soriano

Funding

SIGNAL TRANSDUCTION AND MOUSE DEVELOPMENTR37HD025326 · NICHD · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI SORIANO, PHILIPPE M · 2001 to 2010
$4.9M
Eph/ephrin signaling in craniofacial development and diseaseR00DE020855 · NIDCR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BUSH, JEFFREY OHMANN · 2011 to 2013
$726k
NICHD NIH HHS R37 HD025326NICHD NIH HHS R37HD25326NIDCR NIH HHS R00 DE020855NIDCR NIH HHS R00DE020855
6 · The paper itself

Abstract

The Eph receptor tyrosine kinases and their ephrin partners compose a large and complex family of signaling molecules involved in a wide variety of processes in development, homeostasis, and disease. The complexity inherent to Eph/ephrin signaling derives from several characteristics of the family. First, the large size and functional redundancy/compensation by family members presents a challenge in defining their in vivo roles. Second, the capacity for bidirectional signaling doubles the potential complexity, since every member has the ability to act both as a ligand and a receptor. Third, Ephs and ephrins can utilize a wide array of signal transduction pathways with a tremendous diversity of cell biological effect. The daunting complexity of Eph/ephrin signaling has increasingly prompted investigators to resort to multiple technological approaches to gain mechanistic insight. Here we review recent progress in the use of advanced mouse genetics in combination with proteomic and transcriptomic approaches to gain a more complete understanding of signaling mechanism in vivo. Integrating insights from such disparate approaches provides advantages in continuing to advance our understanding of how this multifarious group of signaling molecules functions in a diverse array of biological contexts.

Indexed as

Signal TransductionTranscriptomeAnimalsEphrinsGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsNeuronsPhosphoproteinsProteomicsReceptors, Eph FamilyEphrinsIntracellular Signaling Peptides and ProteinsPhosphoproteinsReceptors, Eph Family

Identifiers

PMID22040918
PMCPMC3288612

What OpenQuestion holds

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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.