Evidence map›Paper›PMID 16146773›Full record

ReviewFrontiers in bioscience : a journal and virtual library2006

VEGFR-1 and VEGFR-2: two non-identical twins with a unique physiognomy.

Nader Rahimi

Open access · bronzeAbstract readReview
In one paragraph

Review in Frontiers in bioscience : a journal and virtual library, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

104 citing papers in PubMed, 214 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Vascular changes and their implications in lipedema.Frontiers in cell and developmental biology · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
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  12. Article
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  14. Review
  15. Article
  16. Review
  17. Regulation of the Blood-Brain Barrier in Health and Disease.Cold Spring Harbor perspectives in medicine · 2023
    Article
  18. Article
  19. Article
  20. Review

44 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

1 author at 1 institution in 1 country.

Nader RahimiDepartment of Ophthalmology, School of Medicine, Boston University, Boston, MA 02118, USA. nrahimi@bu.edu
Boston University · US

Funding

VEGFR-1 and VEGFR-2 in angiogenesisR01EY012997 · NEI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAHIMI, NADER · 2002 to 2006
$1.6M
Anti-angiogenic signaling molecules in retinal cellsR03EY013706 · NEI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAHIMI, NADER · 2002 to 2004
$485k
NEI NIH HHS EY012997NEI NIH HHS EY0137061NEI NIH HHS R01 EY012997NEI NIH HHS R03 EY013706
6 · The paper itself

Abstract

Angiogenesis involves endothelial cell differentiation, proliferation, migration and cord formation, which lead to tubulogenesis to form vessels. One group of growth factor receptors implicated in angiogenesis is the VEGFR family of receptor tyrosine kinases. VEGFR-1 and VEGFR-2 are closely related receptor tyrosine kinases and have both common and specific ligands. VEGFR-1 is a kinase-impaired RTK whereas VEGFR-2 is a highly active kinase. Despite their differential kinase activation potentials, both VEGFR-1 and VEGFR-2 are required for normal development and angiogenesis. VEGFR-1 regulates angiogenesis by mechanisms that involve ligand-trapping, receptor homo- and heterodimerization. VEGFR-2 stimulates variety of signaling pathways and broad biological responses in vitro. The mechanisms that govern VEGFR-2 activation, its ability to recruit signaling proteins and to undergo downregulation are highly regulated by its carboxyl terminus. This review highlights recent insights into the mechanism of activation of VEGFR-1 and VEGFR-2, and focuses on the signaling pathways employed by VEGFR-1 and VEGFR-2 that regulate angiogenesis.

Indexed as

AnimalsDimerizationDown-RegulationGene Expression RegulationHumansLigandsModels, BiologicalNeovascularization, PathologicPhosphatidylinositol 3-KinasesProtein Kinase CProtein Structure, TertiarySignal Transductionsrc-Family KinasesUbiquitinVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2LigandsPhosphatidylinositol 3-KinasesProtein Kinase Csrc-Family KinasesUbiquitinVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2

Identifiers

PMID16146773
PMCPMC1360224
OpenAlexW2056019080

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.