Evidence map›Paper›PMID 16713597›Full record

ReviewExperimental eye research2006

Vascular endothelial growth factor receptors: molecular mechanisms of activation and therapeutic potentials.

Nader Rahimi

Open access · greenAbstract readReview
In one paragraph

Review in Experimental eye research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.9field-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

47 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Polymorphisms inBiomedicines · 2025
    Review
  3. Review
  4. 18Beta-Glycyrrhetinic Acid Attenuates HAntioxidants (Basel, Switzerland) · 2024
    Article
  5. A case report of low-dose apatinib in the treatment of advanced triple-negative breast cancer.Translational breast cancer research : a journal focusing on translational research in breast cancer · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Medicinal Properties and Active Constituents ofEvidence-based complementary and alternative medicine : eCAM · 2019
    Review
  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

1 author at 1 institution in 1 country.

Nader RahimiDepartments of Ophthalmology and Biochemistry, 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 EY 012997NEI NIH HHS EY 013706 1NEI NIH HHS R01 EY012997NEI NIH HHS R03 EY013706
6 · The paper itself

Abstract

Angiogenesis-associated eye diseases are among the most common cause of blindness in the United States and worldwide. Recent advances in the development of angiogenesis-based therapies for treatment of angiogenesis-associated diseases have provided new hope in a wide variety of human diseases ranging from eye diseases to cancer. One group of growth factor receptors critically implicated in angiogenesis is vascular endothelial growth factor receptors (VEGFR), a subfamily of receptor tyrosine kinases (RTKs). 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 and its kinase activity is suppressed by a single amino acid substitution in its kinase domain and by its carboxyl terminus. VEGFR-2 is highly active kinase, stimulates a variety of signaling pathways and broad biological responses in endothelial cells. The mechanisms that govern VEGFR-2 activation, its ability to recruit signaling proteins and to undergo downregulation are highly regulated by phosphorylation activation loop tyrosines and its carboxyl terminus. Despite their differential potentials to undergo tyrosine phosphorylation and kinase activation, both VEGFR-1 and VEGFR-2 are required for normal embryonic development and pathological angiogenesis. VEGFR-1 regulates angiogenesis by mechanisms that involve ligand trapping, receptor homodimerization and heterodimerization. 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 and their therapeutic potentials in angiogenesis-associated diseases.

Indexed as

AnimalsEndothelial CellsEnzyme ActivationEyeEye DiseasesHumansModels, BiologicalNeovascularization, PathologicPhosphatidylinositol 3-KinasesPhospholipase C gammaPhosphorylationReceptors, Vascular Endothelial Growth FactorSerineSignal Transductionsrc-Family KinasesVascular Endothelial Growth Factor Receptor-1Phosphatidylinositol 3-KinasesPhospholipase C gammaReceptors, Vascular Endothelial Growth FactorSerinesrc-Family KinasesVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2

Identifiers

PMID16713597
PMCPMC1576298
OpenAlexW1964717422

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.