Evidence map›Paper›PMID 25437919›Full record

ArticleJournal of proteome research2015

Glycomic analysis of membrane glycoproteins with bisecting glycosylation from ovarian cancer tissues reveals novel structures and functions.

Heba Allam, Kazuhiro Aoki, Benedict B Benigno, John F McDonald, Samuel G Mackintosh, Michael Tiemeyer, Karen L Abbott

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Systematic synthesis of bisectedChemical science · 2022
    Article
  5. Review
  6. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  7. Review
  8. Neural glycomics: the sweet side of nervous system functions.Cellular and molecular life sciences : CMLS · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020
    Review
  14. Article
  15. 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

7 authors at 3 institutions in 1 country.

Heba AllamComplex Carbohydrate Research Center and Department of Biochemistry and Molecular Biology, University of Georgia , 315 Riverbend Road, Athens, Georgia 30602, United States.
Kazuhiro Aoki
Benedict B Benigno
John F McDonald
Samuel G Mackintosh
Michael Tiemeyer
Karen L Abbott
University of Arkansas for Medical Sciences · USOvarian Cancer Institute · USUniversity of Georgia · US

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Glycomics Laboratory for the Early Detection of Epithelial Ovarian CancerU01CA168870 · NCI · UNIV OF ARKANSAS FOR MED SCIS · PI ABBOTT, KAREN L. · 2012 to 2016
$2.0M
NCI NIH HHS U01 CA168870NCI NIH HHS UO1CA168870NIGMS NIH HHS P41 GM103490
6 · The paper itself

Abstract

Biomarkers capable of detecting and targeting epithelial ovarian cancer cells for diagnostics and therapeutics would be extremely valuable. Ovarian cancer is the deadliest reproductive malignancy among women in the U.S., killing over 14 000 women each year. Both the lack of presenting symptoms and high mortality rates illustrate the need for earlier diagnosis and improved treatment of this disease. The glycosyltransferase enzyme GnT-III encoded by the Mgat3 gene is responsible for the addition of GlcNAc (N-acetylglucosamine) to form bisecting N-linked glycan structures. GnT-III mRNA expression is amplified in ovarian cancer tissues compared with normal ovarian tissue. We use a lectin capture strategy coupled to nano-ESI-RPLC-MS/MS to isolate and identify the membrane glycoproteins and unique glycan structures associated with GnT-III amplification in human ovarian cancer tissues. Our data illustrate that the majority of membrane glycoproteins with bisecting glycosylation are common to both serous and endometrioid histological subtypes of ovarian cancer, and several have been reported to participate in signaling pathways such as Notch, Wnt, and TGFβ.

Indexed as

Biomarkers, TumorChromatography, High Pressure LiquidFemaleGlycomicsGlycosylationHumansMembrane GlycoproteinsN-AcetylglucosaminyltransferasesOvarian NeoplasmsRNA, Small InterferingTandem Mass Spectrometrybeta-1,4-mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferaseBiomarkers, TumorMembrane GlycoproteinsN-AcetylglucosaminyltransferasesRNA, Small Interferingbiomarkersbisecting N-linked glycansglycoproteinshuman tissuemass spectrometryovarian cancer

Identifiers

PMID25437919
PMCPMC4286206
OpenAlexW2319036125

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.