Evidence map›Paper›PMID 17442480›Full record

ArticleBiophysical chemistry2007

Dimerization of VEGF receptors and implications for signal transduction: a computational study.

Feilim Mac Gabhann, Aleksander S Popel

Open access · greenAbstract read
In one paragraph

Article in Biophysical chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

70 citing papers in PubMed, 134 citations in OpenAlex.

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  16. Exploring the signaling space of a GPCR using bivalent ligands with a rigid oligoproline backbone.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  17. VEGFR1 signaling in retinal angiogenesis and microinflammation.Progress in retinal and eye research · 2021
    Review
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10 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

2 authors at 1 institution in 1 country.

Feilim Mac GabhannDepartment of Biomedical Engineering, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA. feilim@jhu.edu
Aleksander S Popel
Johns Hopkins University · US

Funding

Systems Biology of Angiogenesis in Peripheral Arterial DiseaseR01HL101200 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI POPEL, ALEKSANDER S. · 2010 to 2022
$10.7M
Quantitative Analysis of Angiogenesis in Skeletal MuscleR01HL079653 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI POPEL, ALEKSANDER S. · 2005 to 2009
$1.5M
Systems Biology of Angiogenesis: Molecules to therapyR33HL087351 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI POPEL, ALEKSANDER S. · 2006 to 2008
$1.3M
NHLBI NIH HHS R01 HL079653NHLBI NIH HHS R01 HL101200NHLBI NIH HHS R33 HL087351
6 · The paper itself

Abstract

Vascular endothelial growth factor (VEGF) is a potent cytokine involved in the induction of neovascularization. Secreted as a cysteine-linked dimer, it has two binding sites at opposite poles through which it may bind VEGF receptors (VEGFRs), receptor tyrosine kinases found on the surface of endothelial and other cells. The binding of a VEGF molecule to two VEGFR molecules induces transphosphorylation of the intracellular domains of the receptors, leading to signal transduction. The dominant mechanism of receptor dimerization is not clear: the receptors may be present in an inactive pre-dimerized form, VEGF binding first to one of the receptors, the second receptor then ideally located for dimerization; or VEGF may bind receptor monomers on the cell surface, which then diffuse and bind to available unligated receptor monomers to complete the activation. Both processes take place and one or other may dominate on different cell types. We demonstrate the impact of dimerization mechanism on the binding of VEGF to the cell surface and on the formation of active signaling receptor complexes. We describe two methods to determine which process dominates, based on binding and phosphorylation assays. The presence of two VEGF receptor populations, VEGFR1 and VEGFR2, can result in receptor heterodimer formation. Our simulations predict that heterodimers will comprise 10-50% of the active, signaling VEGF receptor complexes, and that heterodimers will form at the expense of homodimers of VEGFR1 when VEGFR2 populations are larger. These results have significant implications for VEGF signal transduction and interpretation of experimental studies. These results may be applicable to other ligand-receptor pairs, in particular PDGF.

Indexed as

Computer SimulationSignal TransductionModels, MolecularProtein ConformationVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2

Identifiers

PMID17442480
PMCPMC2711879
OpenAlexW1982383741

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.