Evidence map›Paper›PMID 27888154›Full record

ReviewPharmacological research2017

Modulation of VEGF receptor 2 signaling by protein phosphatases.

Federico Corti, Michael Simons

Open access · greenAbstract readReview
In one paragraph

Review in Pharmacological research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
2.6field-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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Activin A Limits VEGF-Induced Permeability via VE-PTP.International journal of molecular sciences · 2023
    Article
  10. KIF13B mediates VEGFR2 recycling to modulate vascular permeability.Cellular and molecular life sciences : CMLS · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. In Vitro Angiogenesis Inhibition and Endothelial Cell Growth and Morphology.International journal of molecular sciences · 2022
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Federico CortiYale Cardiovascular Research Center, Department of Internal Medicine and Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA. Electronic address: federico.corti@yale.edu.
Michael SimonsYale Cardiovascular Research Center, Department of Internal Medicine and Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA. Electronic address: michael.simons@yale.edu.
Yale University · US

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Angiogensis and ischemiaR01HL053793 · NHLBI · YALE UNIVERSITY · PI SIMONS, MICHAEL · 1996 to 2017
$7.3M
Arteriogenesis and BranchingR01HL084619 · NHLBI · YALE UNIVERSITY · PI SIMONS, MICHAEL · 2007 to 2018
$6.7M
NCATS NIH HHS UL1 TR001863NHLBI NIH HHS R01 HL053793NHLBI NIH HHS R01 HL084619
6 · The paper itself

Abstract

Phosphorylation of serines, threonines, and tyrosines is a central event in signal transduction cascades in eukaryotic cells. The phosphorylation state of any particular protein reflects a balance of activity between kinases and phosphatases. Kinase biology has been exhaustively studied and is reasonably well understood, however, much less is known about phosphatases. A large body of evidence now shows that protein phosphatases do not behave as indiscriminate signal terminators, but can function both as negative or positive regulators of specific signaling pathways. Genetic models have also shown that different protein phosphatases play precise biological roles in health and disease. Finally, genome sequencing has unveiled the existence of many protein phosphatases and associated regulatory subunits comparable in number to kinases. A wide variety of roles for protein phosphatase roles have been recently described in the context of cancer, diabetes, hereditary disorders and other diseases. In particular, there have been several recent advances in our understanding of phosphatases involved in regulation of vascular endothelial growth factor receptor 2 (VEGFR2) signaling. The receptor is the principal signaling molecule mediating a wide spectrum of VEGF signal and, thus, is of paramount significance in a wide variety of diseases ranging from cancer to cardiovascular to ophthalmic. This review focuses on the current knowledge about protein phosphatases' regulation of VEGFR2 signaling and how these enzymes can modulate its biological effects.

Indexed as

AnimalsHumansPhosphoprotein PhosphatasesPhosphorylationSignal TransductionVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2Phosphoprotein PhosphatasesVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2AngiogenesisBlood vesselsEndothelial cellsProtein phosphatasesVEGFR2 signaling

Identifiers

PMID27888154
PMCPMC5205541
OpenAlexW2551372671

What OpenQuestion holds

Textmetadata
LicenceTDM
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.