Evidence map›Paper›PMID 20652609›Full record

ArticleAmino acids2011

Improved identification of O-linked glycopeptides from ETD data with optimized scoring for different charge states and cleavage specificities.

Zsuzsa Darula, Robert J Chalkley, Aenoch Lynn, Peter R Baker, Katalin F Medzihradszky

Abstract readComparative Study
In one paragraph

Article in Amino acids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Optimal Dissociation Methods Differ forJournal of proteome research · 2020
    Article
  4. Article
  5. Article
  6. Review
  7. Chemical Glycoproteomics.Chemical reviews · 2016
    Review
  8. Article
  9. Article
  10. Glycan side reaction may compromise ETD-based glycopeptide identification.Journal of the American Society for Mass Spectrometry · 2014
    Article
  11. Article
  12. Unusual fragmentation pathways in collagen glycopeptides.Journal of the American Society for Mass Spectrometry · 2013
    Article
  13. Article
  14. Targeting the glycoproteome.Glycoconjugate journal · 2013
    Article
  15. 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

5 authors.

Zsuzsa DarulaProteomics Research Group, Biological Research Center, 62 Temesvari krt, Szeged, 6726, Hungary.
Robert J Chalkley
Aenoch Lynn
Peter R Baker
Katalin F Medzihradszky

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SZOKA, FRANCIS C. · 1985 to 2011
$24.1M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
NCRR NIH HHS P41 RR001614NCRR NIH HHS P41RR001614NIGMS NIH HHS P41 GM103481
6 · The paper itself

Abstract

This article describes the effect of re-interrogation of electron-transfer dissociation (ETD) data with newly developed analytical tools. MS/MS-based characterization of O-linked glycopeptides is discussed using data acquired from a complex mixture of O-linked glycopeptides, featuring mucin core 1-type carbohydrates with and without sialic acid, as well as after partial deglycosylation to leave only the core GalNAc units (Darula and Medzihradszky in Mol Cell Proteomics 8:2515, 2009). Information content of collision-induced dissociation spectra generated in collision cell (in QqTOF instruments) and in ion traps is compared. Interpretation of the corresponding ETD data using Protein Prospector is also presented. Search results using scoring based on the frequency of different fragment ions occurring in ETD spectra of tryptic peptides are compared with results obtained after ion weightings were adjusted to accommodate differential ion frequencies in spectra of differing charge states or cleavage specificities. We show that the improved scoring is more than doubled the glycopeptide assignments under very strict acceptance criteria. This study illustrates that "old" proteomic data may yield significant new information when re-interrogated with new, improved tools.

Indexed as

Amino Acid SequenceAnimalsCattleDatabases, ProteinData Interpretation, StatisticalElectrochemistryGlycopeptidesMolecular Sequence DataPeptide FragmentsSearch EngineSerumTandem Mass SpectrometryGlycopeptidesPeptide Fragments

Identifiers

PMID20652609
PMCPMC3102200

What OpenQuestion holds

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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.