Evidence map›Paper›PMID 10570155›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

An Eph receptor regulates integrin activity through R-Ras.

J X Zou, B Wang, M S Kalo, A H Zisch, E B Pasquale, E Ruoslahti

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

72 citing papers in PubMed, 191 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Cells · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Eph- and ephrin-dependent mechanisms in tumor and stem cell dynamics.Cellular and molecular life sciences : CMLS · 2014
    Review
  17. Review
  18. Review
  19. Eph receptors and ephrins as targets for cancer therapy.Journal of cellular and molecular medicine · 2012
    Review
  20. Review

12 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

6 authors at 2 institutions in 2 countries.

J X ZouCancer Research Center, The Burnham Institute, La Jolla, CA 92037, USA.
B Wang
M S Kalo
A H Zisch
E B Pasquale
E Ruoslahti
Cancer Research Center · USSanford Burnham Prebys Medical Discovery Institute · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
Tissue CultureP01HD025938 · NICHD · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RANSCHT, BARBARA · 1989 to 2011
$13.6M
INTEGRIN REGULATION BY R-RASR01CA079984 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI RUOSLAHTI, ERKKI I · 1999 to 2002
$820k
CELL-MATRIX INTERACTIONST32CA009579 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI ENGVALL, EVA S · 1987 to 2001
$306k
STRUCTURAL FEATURES IMPORTANT FOR EPH RECEPTOR FUNCTIONF32CA073195 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI KALO, MATTHEW S · 1997 to 1999
–
NCI NIH HHS CA09579NCI NIH HHS CA79984NCI NIH HHS F32 CA073195NCI NIH HHS P30 CA030199NCI NIH HHS T32 CA009579NICHD NIH HHS HD25938NICHD NIH HHS P01 HD025938
6 · The paper itself

Abstract

The ability of integrins to mediate cell attachment to extracellular matrices and to blood proteins is regulated from inside the cell. Increased ligand-binding activity of integrins is critical for platelet aggregation upon blood clotting and for leukocyte extravasation to inflamed tissues. Decreased adhesion is thought to promote tumor cell invasion. R-Ras, a small intracellular GTPase, regulates the binding of integrins to their ligands outside the cell. Here we show that the Eph receptor tyrosine kinase, EphB2, can control integrin activity through R-Ras. Cells in which EphB2 is activated become poorly adherent to substrates coated with integrin ligands, and a tyrosine residue in the R-Ras effector domain is phosphorylated. The R-Ras phosphorylation and loss of cell adhesion are causally related, because forced expression of an R-Ras variant resistant to phosphorylation at the critical site made cells unresponsive to the anti-adhesive effect of EphB2. This is an unusual regulatory pathway among the small GTPases. Reduced adhesiveness induced through the Eph/R-Ras pathway may explain the repulsive effect of the Eph receptors in axonal pathfinding and may facilitate tumor cell invasion and angiogenesis.

Indexed as

3T3 CellsAnimalsCell AdhesionCell Line, TransformedChickensHumansIntegrinsMiceMutagenesis, Site-DirectedPhosphorylationras ProteinsReceptor, EphB2Receptor Protein-Tyrosine KinasesRecombinant Fusion ProteinsSignal TransductionIntegrinsras ProteinsReceptor, EphB2Receptor Protein-Tyrosine KinasesRecombinant Fusion Proteins

Identifiers

PMID10570155
PMCPMC24147
OpenAlexW2053281522

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.