Evidence map›Paper›PMID 27966990›Full record

ArticleJournal of proteome research2017

Site-Specific N-Glycosylation of Endothelial Cell Receptor Tyrosine Kinase VEGFR-2.

Kevin Brown Chandler, Deborah R Leon, Rosana D Meyer, Nader Rahimi, Catherine E Costello

Abstract read
In one paragraph

Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 51 citations in OpenAlex.

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  17. ST6Gal1: Oncogenic signaling pathways and targets.Frontiers in molecular biosciences · 2022
    Review
  18. Article
  19. CD209L/L-SIGN and CD209/DC-SIGN act as receptors for SARS-CoV-2.bioRxiv : the preprint server for biology · 2021
    Article
  20. 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

5 authors at 1 institution in 1 country.

Kevin Brown ChandlerCenter for Biomedical Mass Spectrometry, Department of Biochemistry and ‡Department of Pathology and Laboratory Medicine, Boston University School of Medicine , Boston, Massachusetts 02118, United States.ORCID 0000-0001-5514-9652
Deborah R LeonCenter for Biomedical Mass Spectrometry, Department of Biochemistry and ‡Department of Pathology and Laboratory Medicine, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Rosana D MeyerCenter for Biomedical Mass Spectrometry, Department of Biochemistry and ‡Department of Pathology and Laboratory Medicine, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Nader RahimiCenter for Biomedical Mass Spectrometry, Department of Biochemistry and ‡Department of Pathology and Laboratory Medicine, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Catherine E CostelloCenter for Biomedical Mass Spectrometry, Department of Biochemistry and ‡Department of Pathology and Laboratory Medicine, Boston University School of Medicine , Boston, Massachusetts 02118, United States.ORCID 0000-0003-1594-5122
Boston University · US

Funding

Mass Spectrometry Resource for Biology and MedicineP41GM104603 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2017
$10.4M
MALDI-TOF/TOF MS TO SUPPORT BIOMEDICAL RESEARCHS10OD010724 · OD · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2012 to 2012
$590k
Overcoming the resistance to anti-angiogenesis therapyR21CA191970 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAHIMI, NADER · 2015 to 2016
$392k
Impaired Glycosylation of Vascular Endothelial Growth Factor Receptor 2 in Tumor AngiogenesisF32CA196157 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CHANDLER, KEVIN BROWN · 2015 to 2017
$168k
NCI NIH HHS F32 CA196157NCI NIH HHS R21 CA191970NIGMS NIH HHS P41 GM104603NIH HHS S10 OD010724
6 · The paper itself

Abstract

Vascular endothelial growth factor receptor-2 (VEGFR-2) is an important receptor tyrosine kinase (RTK) that plays critical roles in both physiologic and pathologic angiogenesis. The extracellular domain of VEGFR-2 is composed of seven immunoglobulin-like domains, each with multiple potential N-glycosylation sites (sequons). N-glycosylation plays a central role in RTK ligand binding, trafficking, and stability. However, despite its importance, the functional role of N-glycosylation of VEGFR-2 remains poorly understood. The objectives of the present study were to characterize N-glycosylation sites in VEGFR-2 via enzymatic release of the glycans and concomitant incorporation of

Indexed as

Amino Acid SequenceAnimalsAortaEndothelial CellsGlycopeptidesGlycosylationHumansPeptidesPolysaccharidesProtein BindingSwineTandem Mass SpectrometryVascular Endothelial Growth Factor Receptor-2GlycopeptidesPeptidesPolysaccharidesVascular Endothelial Growth Factor Receptor-2N-glycosylationreceptor tyrosine kinaseRTKvascular endothelial growth factor receptor-2VEGFR-2

Identifiers

PMID27966990
PMCPMC5291786
OpenAlexW2564163541

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.