Evidence map›Paper›PMID 25825981›Full record

ArticleOncotarget2015

EMMPRIN/CD147 is a novel coreceptor of VEGFR-2 mediating its activation by VEGF.

Farah Khayati, Laura Pérez-Cano, Kamel Maouche, Aurélie Sadoux, Zineb Boutalbi, Marie-Pierre Podgorniak, Uwe Maskos, Niclas Setterblad, Anne Janin, Fabien Calvo and 4 more

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. CD147/Basigin: From Integrative Molecular Hub to Translational Therapeutic Target.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Review
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  7. Article
  8. SARS-CoV-2 uptake and inflammatory response in senescent endothelial cells are regulated by the BSG/VEGFR2 pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Article
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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

14 authors at 8 institutions in 2 countries.

Farah KhayatiINSERM UMR-S 976, Hôpital Saint-Louis, Paris, France.
Laura Pérez-CanoJoint BSC-IRB Research Program in Computational Biology, Life Sciences Department, Barcelona Supercomputing Center, Barcelona, Spain.
Kamel MaoucheDépartement de Neurosciences, Institut Pasteur, Unité de Neurobiologie Intégrative des Systèmes Cholinergiques, Paris, France.
Aurélie SadouxINSERM UMR-S 976, Hôpital Saint-Louis, Paris, France.
Zineb BoutalbiINSERM UMR-S 976, Hôpital Saint-Louis, Paris, France.
Marie-Pierre PodgorniakINSERM UMR-S 976, Hôpital Saint-Louis, Paris, France.
Uwe MaskosDépartement de Neurosciences, Institut Pasteur, Unité de Neurobiologie Intégrative des Systèmes Cholinergiques, Paris, France.
Niclas SetterbladUniversité Paris-Diderot, Sorbonne Paris Cité, Paris, France.
Anne JaninUniversité Paris-Diderot, Sorbonne Paris Cité, Paris, France.
Fabien CalvoINSERM UMR-S 976, Hôpital Saint-Louis, Paris, France.
Céleste LebbéUniversité Paris-Diderot, Sorbonne Paris Cité, Paris, France.
Suzanne MenashiCNRS-UMR 7149, Laboratoire CRRET, Créteil, France.
Juan Fernandez-RecioJoint BSC-IRB Research Program in Computational Biology, Life Sciences Department, Barcelona Supercomputing Center, Barcelona, Spain.
Samia MourahINSERM UMR-S 976, Hôpital Saint-Louis, Paris, France.
Inserm · FRSorbonne Paris Cité · FRBarcelona Supercomputing Center · ESInstitut Pasteur · FRAssistance Publique – Hôpitaux de Paris · FRCentre National de la Recherche Scientifique · FRDélégation Paris 7 · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

EMMPRIN/CD147 is mainly known for its protease inducing function but a role in promoting tumor angiogenesis has also been demonstrated. This study provides evidence that EMMPRIN is a new coreceptor for the VEGFR-2 tyrosine kinase receptor in both endothelial and tumor cells, as it directly interacts with it and regulates its activation by its VEGF ligand, signalling and functional consequences both in vitro and in vivo. Computational docking analyses and mutagenesis studies identified a molecular binding site in the extracellular domain of EMMPRIN located close to the cell membrane and containing the amino acids 195/199. EMMPRIN is overexpressed in cancer and hence is able to further potentiate VEGFR-2 activation, suggesting that a combinatory therapy of an antiangiogenic drug together with an inhibitor of EMMPRIN/VEGFR-2 interaction may have a greater impact on inhibiting angiogenesis and malignancy.

Indexed as

Gene Expression Regulation, NeoplasticAngiogenesis InhibitorsAnimalsBasiginBinding SitesCell-Free SystemCell LineCell Line, TumorCell MembraneCell MovementComputer SimulationFemaleGene SilencingHumansLigandsMiceAngiogenesis InhibitorsBasiginBSG protein, humanKDR protein, humanLigandsRecombinant ProteinsRNA, Small InterferingVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2VEGFA protein, humancoreceptorEMMPRIN/CD147interaction/activationVEGFR-2

Identifiers

PMID25825981
PMCPMC4496396
OpenAlexW1595994845

What OpenQuestion holds

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LicenceCC BY
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.