Evidence map›Paper›PMID 26729242›Full record

ArticleGlycoconjugate journal2016

O-glycosylation sites identified from mucin core-1 type glycopeptides from human serum.

Zsuzsanna Darula, Farkas Sarnyai, Katalin F Medzihradszky

Open access · greenAbstract read
In one paragraph

Article in Glycoconjugate journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-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

16 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
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  4. Plasma/Serum Proteomics based on Mass Spectrometry.Protein and peptide letters · 2024
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  10. Optimal Dissociation Methods Differ forJournal of proteome research · 2020
    Article
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  13. Review
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  15. Article
  16. Characterizing theBlood advances · 2017
    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

3 authors at 2 institutions in 2 countries.

Zsuzsanna DarulaLaboratory of Proteomics Research, Biological Research Centre of the Hungarian Academy of Sciences, Institute of Biochemistry, Szeged, Hungary. darula.zsuzsanna@brc.mta.hu.
Farkas SarnyaiLaboratory of Proteomics Research, Biological Research Centre of the Hungarian Academy of Sciences, Institute of Biochemistry, Szeged, Hungary.
Katalin F MedzihradszkyLaboratory of Proteomics Research, Biological Research Centre of the Hungarian Academy of Sciences, Institute of Biochemistry, Szeged, Hungary.
Hungarian Academy of Sciences · HUInstitute of Biochemistry · HU

Funding

Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM103481
6 · The paper itself

Abstract

In this work O-linked glycopeptides bearing mucin core-1 type structures were enriched from human serum. Since about 70 % of the O-glycans in human serum bind to the plant lectin Jacalin, we tested a previously successful protocol that combined Jacalin affinity enrichment on the protein- and peptide-level with ERLIC chromatography as a further enrichment step in between, to eliminate the high background of unmodified peptides. In parallel, we developed a simpler and significantly faster new workflow that used two lectins sequentially: wheat germ agglutinin and then Jacalin. The first lectin provides general glycopeptide enrichment, while the second specifically enriches O-linked glycopeptides with Galβ1-3GalNAcα structures. Mass spectrometric analysis of enriched samples showed that the new sample preparation method is more selective and sensitive than the former. Altogether, 52 unique glycosylation sites in 20 proteins were identified in this study.

Indexed as

Protein Processing, Post-TranslationalBinding SitesGlycosylationHumansMass SpectrometryMucin-1Plant LectinsMucin-1Plant LectinsAutomated glycopeptide identificationETDHCDHuman serumO-glycosylation

Identifiers

PMID26729242
PMCPMC4892982
OpenAlexW2230799130

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.