Evidence map›Paper›PMID 26593774›Full record

ArticleAnalytical chemistry2015

Identification and Validation of Atypical N-Glycosylation Sites.

Shisheng Sun, Hui Zhang

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. International journal of molecular sciences · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
  11. Review
  12. Article
  13. Article
  14. Clinical proteomics · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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.

Shisheng SunDepartment of Pathology, Johns Hopkins University , 400 North Broadway, Smith Building, Room 4001, Baltimore, Maryland 21287, United States.
Hui ZhangDepartment of Pathology, Johns Hopkins University , 400 North Broadway, Smith Building, Room 4001, Baltimore, Maryland 21287, United States.
Johns Hopkins University · US

Funding

Shared Resource CoresP01HL107153 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI HART, GERALD WARREN · 2011 to 2017
$16.8M
Proteome Characterization Center: A Genoproteomics Pipeline for Cance ResearchU24CA160036 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI, ZHANG, HUI · 2011 to 2016
$10.7M
Clinical and Analytical Validation of Cancer BiomarkersU24CA115102 · NCI · JOHNS HOPKINS UNIVERSITY · PI CHAN, DANIEL WANYUI · 2005 to 2021
$7.4M
Glycoprotein biomarkers for the early detection of aggressive prostate cancerU01CA152813 · NCI · JOHNS HOPKINS UNIVERSITY · PI ZHANG, HUI · 2010 to 2021
$6.2M
Probing the Connections between Monosaccharide Analogs, Sialic Acid Metabolism, aR01CA112314 · NCI · JOHNS HOPKINS UNIVERSITY · PI YAREMA, KEVIN J · 2005 to 2022
$4.5M
NCI NIH HHS R01 CA112314NCI NIH HHS R01CA112314NCI NIH HHS U01 CA152813NCI NIH HHS U24 CA115102NCI NIH HHS U24CA115102NCI NIH HHS U24 CA160036NCI NIH HHS U24CA160036NHLBI NIH HHS N01-HV-00240NHLBI NIH HHS P01 HL107153NHLBI NIH HHS P01HL107153
6 · The paper itself

Abstract

It is well-known that N-linked glycans usually attach to asparagine residues in the N-X-S/T motifs of proteins. However, accumulating evidence indicates that N-glycosylation could also possibly occur at other atypical motifs. In this study, we tried to identify atypical N-glycosylation sites using our recently developed solid-phase extraction of the N-linked Glycans And Glycosite-containing peptides (NGAG) method. Peptides with deamidation sites at asparagine residues but lacking a typical asparagine-X-serine/threonine sequons (N-X-S/T, X is any amino acid except proline) motif were identified from deglycosylated peptide data as potentially atypical glycosite-containing peptides. These atypical glycosites were verified by the presence of glycans on their intact glycopeptides and further confirmed by specific inhibition of cells with an N-linked glycosylation inhibitor, tunicamycin. From this study, two atypical N-linked glycosylation sites with N-X-C and N-X-V motifs were identified and validated from an ovarian cancer cell line (OVCAR-3).

Indexed as

Amino Acid SequenceAsparagineBinding SitesChemistry Techniques, AnalyticalGlycosylationMass SpectrometryModels, MolecularMolecular Sequence DataPolysaccharidesReproducibility of ResultsSolid Phase ExtractionAsparaginePolysaccharides

Identifiers

PMID26593774
PMCPMC4721579
OpenAlexW2299732859

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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.