Evidence map›Paper›PMID 15107818›Full record

ArticleOncogene2004

Substitution of C-terminus of VEGFR-2 with VEGFR-1 promotes VEGFR-1 activation and endothelial cell proliferation.

Rosana D Meyer, Amrik Singh, Fredric Majnoun, Catharina Latz, Kameran Lashkari, Nader Rahimi

Open access · greenAbstract read
In one paragraph

Article in Oncogene, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 33% 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

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
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  15. Review
  16. Article
  17. VEGFR-1 and VEGFR-2: two non-identical twins with a unique physiognomy.Frontiers in bioscience : a journal and virtual library · 2006
    Review
  18. Activation of hypoxia-inducible factors in hyperoxia through prolyl 4-hydroxylase blockade in cells and explants of primate lung.Proceedings of the National Academy of Sciences of the United States of America · 2005
    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

6 authors at 2 institutions in 1 country.

Rosana D MeyerDepartments of Ophthalmology and Biochemistry, School of Medicine, Boston University, 715 Albany Street, Boston, MA 02118, USA.
Amrik Singh
Fredric Majnoun
Catharina Latz
Kameran Lashkari
Nader Rahimi
Boston University · USMassachusetts Eye and Ear Infirmary · 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 0137061NEI NIH HHS R01 EY012997NEI NIH HHS R03 EY013706
6 · The paper itself

Abstract

VEGFR-1 is devoid of ligand-dependent tyrosine autophosphorylation and its activation is not associated with proliferation of endothelial cells. The molecular mechanism responsible for this characteristic of VEGFR-1 is not known. In this study, we show that VEGFR-1 is devoid of ligand-dependent downregulation and failed to stimulate intracellular calcium release, cell migration and angiogenesis in vitro. To understand the molecular mechanisms responsible for the poor tyrosine autophosphorylation of VEGFR-1, we have either deleted the carboxyl terminus of VEGFR-1 or exchanged it with the carboxyl terminus of VEGFR-2. The deletion of carboxyl terminus of VEGFR-1 did not reverse its defective ligand-dependent autophosphorylation. The carboxyl terminus-swapped VEGFR-1, however, displayed ligand-dependent autophosphorylation, downregulation and also conveyed strong mitogenic responses. Thus, the carboxyl tail of VEGFR-1 restrains the ligand-dependent kinase activation and downregulation of VEGFR-1 and its ability to convey the angiogenic responses in endothelial cells.

Indexed as

AnimalsCell DivisionDown-RegulationEndothelial CellsHumansLigandsPhosphorylationVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2LigandsVascular Endothelial Growth Factor Receptor-1Vascular Endothelial Growth Factor Receptor-2

Identifiers

PMID15107818
PMCPMC1472702
OpenAlexW2041328797

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.