Evidence map›Paper›PMID 24300896›Full record

ArticleScience signaling2013

Lysine methylation promotes VEGFR-2 activation and angiogenesis.

Edward J Hartsough, Rosana D Meyer, Vipul Chitalia, Yan Jiang, Victor E Marquez, Irina V Zhdanova, Janice Weinberg, Catherine E Costello, Nader Rahimi

Abstract read
In one paragraph

Article in Science signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Context-dependent regulation of receptor tyrosine kinases: Insights from systems biology approaches.Wiley interdisciplinary reviews. Systems biology and medicine · 2019
    Review
  5. Observational
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Systems biology of the microvasculature.Integrative biology : quantitative biosciences from nano to macro · 2015
    Review
  18. Review
  19. Review
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

9 authors at 2 institutions in 1 country.

Edward J Hartsough1Departments of Pathology and Ophthalmology, School of Medicine, Boston University Medical Campus, Boston, MA 02118, USA.
Rosana D Meyer
Vipul Chitalia
Yan Jiang
Victor E Marquez
Irina V Zhdanova
Janice Weinberg
Catherine E Costello
Nader Rahimi
Boston University · USMassachusetts Institute of Technology · US

Funding

XI INTERNATIONAL SYMPOSIUM ON AMYLOIDOSISP41RR010888 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 1996 to 2011
$18.6M
Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
Role of Protein Ubiquitination in AngiogenesisR01EY017955 · NEI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAHIMI, NADER · 2008 to 2010
$1.2M
Role of Wnt signaling in uremia-induced entothelial dysfunctionK08DK080946 · NIDDK · BOSTON MEDICAL CENTER · PI CHITALIA, VIPUL C · 2009 to 2013
$746k
LTQ MASS SPECTROMETER: STRUCTURAL BIOLOGYS10RR020946 · NCRR · BOSTON UNIVERSITY MEDICAL CAMPUS · PI ZAIA, JOSEPH · 2006 to 2006
$497k
Intramural NIH HHSNCRR NIH HHS P41 RR010888NCRR NIH HHS S10 RR020946NEI NIH HHS R01 EY017955NEI NIH HHS R01EY017955NIDDK NIH HHS DK080946NIDDK NIH HHS K08 DK080946NIGMS NIH HHS GM104603NIGMS NIH HHS P41 GM104603PHS HHS N01 HHSN268201000031C
6 · The paper itself

Abstract

Activation of vascular endothelial growth factor receptor-2 (VEGFR-2), an endothelial cell receptor tyrosine kinase, promotes tumor angiogenesis and ocular neovascularization. We report the methylation of VEGFR-2 at multiple Lys and Arg residues, including Lys(1041), a residue that is proximal to the activation loop of the kinase domain. Methylation of VEGFR-2 was independent of ligand binding and was not regulated by ligand stimulation. Methylation of Lys(1041) enhanced tyrosine phosphorylation and kinase activity in response to ligands. Additionally, interfering with the methylation of VEGFR-2 by pharmacological inhibition or by site-directed mutagenesis revealed that methylation of Lys(1041) was required for VEGFR-2-mediated angiogenesis in zebrafish and tumor growth in mice. We propose that methylation of Lys(1041) promotes the activation of VEGFR-2 and that similar posttranslational modification could also regulate the activity of other receptor tyrosine kinases.

Indexed as

Protein Processing, Post-TranslationalAnimalsCell Line, TumorHEK293 CellsHeterograftsHumansLysineMethylationMiceNeoplasm ProteinsNeoplasmsNeoplasm TransplantationNeovascularization, PathologicVascular Endothelial Growth Factor Receptor-2ZebrafishZebrafish ProteinsKDR protein, humanLysineNeoplasm ProteinsVascular Endothelial Growth Factor Receptor-2Zebrafish Proteins

Identifiers

PMID24300896
PMCPMC4108444
OpenAlexW2020151154

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.