Evidence map›Paper›PMID 22242939›Full record

ArticleBiochemistry2012

Cancer somatic mutations disrupt functions of the EphA3 receptor tyrosine kinase through multiple mechanisms.

Erika M Lisabeth, Carlos Fernandez, Elena B Pasquale

Abstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024
    Review
  3. Therapeutic advances of targeting receptor tyrosine kinases in cancer.Signal transduction and targeted therapy · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Eph Receptors in Cancer.Biomedicines · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Erika M LisabethSanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, California 92037, United States.
Carlos Fernandez
Elena B Pasquale
Sanford Burnham Prebys Medical Discovery Institute · US

Funding

Targeting Eph receptors in cancerP01CA138390 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2010 to 2014
$7.3M
Trans-disciplinary Postdoctoral Training in Cancer BiologyT32CA121949 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RONAI, ZEEV A. · 2007 to 2011
$1.8M
NCI NIH HHS P01 CA138390NCI NIH HHS P01CA138390NCI NIH HHS T32 CA121949NCI NIH HHS T32CA121949
6 · The paper itself

Abstract

The Eph receptor tyrosine kinases make up an important family of signal transduction molecules that control many cellular processes, including cell adhesion and movement, cell shape, and cell growth. All of these are important aspects of cancer progression, but the relationship between Eph receptors and cancer is complex and not fully understood. Genetic screens of tumor specimens from cancer patients have revealed somatic mutations in many Eph receptors. The most highly mutated Eph receptor is EphA3, but its functional role in cancer is currently not well established. Here we show that many EphA3 mutations identified in lung, colorectal, and hepatocellular cancers, melanoma, and glioblastoma impair kinase activity or ephrin ligand binding and/or decrease the level of receptor cell surface localization. These results suggest that EphA3 has ephrin- and kinase-dependent tumor suppressing activities, which are disrupted by somatic cancer mutations.

Indexed as

Gene Expression Regulation, NeoplasticMutationCell MembraneDisease ProgressionEphrin-A3FibronectinsHEK293 CellsHumansImmunoblottingModels, BiologicalModels, GeneticNeoplasmsProtein ConformationProtein KinasesProtein Structure, TertiaryReceptor, EphA3EPHA3 protein, humanEphrin-A3FibronectinsProtein KinasesReceptor, EphA3Receptor Protein-Tyrosine Kinases

Identifiers

PMID22242939
PMCPMC3471792
OpenAlexW2029784998

What OpenQuestion holds

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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.