Evidence map›Paper›PMID 24006841›Full record

ArticleAnalytical chemistry2013

Concurrent automated sequencing of the glycan and peptide portions of O-linked glycopeptide anions by ultraviolet photodissociation mass spectrometry.

James A Madsen, Byoung Joon Ko, Hua Xu, Jeremy A Iwashkiw, Scott A Robotham, Jared B Shaw, Mario F Feldman, Jennifer S Brodbelt

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 72 citations in OpenAlex.

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  15. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  16. Review
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  18. Article
  19. Review
  20. Precision Mapping of O-LinkedJournal of the American Chemical Society · 2020
    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

8 authors at 3 institutions in 2 countries.

James A MadsenDepartment of Chemistry, The University of Texas at Austin , 1 University Station A5300, Austin, Texas, 78712 United States.
Byoung Joon Ko
Hua Xu
Jeremy A Iwashkiw
Scott A Robotham
Jared B Shaw
Mario F Feldman
Jennifer S Brodbelt
The University of Texas at Austin · USAlberta Glycomics Centre · CACase Western Reserve University · US

Funding

UV Photodissociation for Acidic and Basic Proteome CharacterizationR21GM099028 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2011 to 2012
$384k
CIHRNIGMS NIH HHS R21 GM099028NIGMS NIH HHS R21GM099028
6 · The paper itself

Abstract

O-Glycopeptides are often acidic owing to the frequent occurrence of acidic saccharides in the glycan, rendering traditional proteomic workflows that rely on positive mode tandem mass spectrometry (MS/MS) less effective. In this report, we demonstrate the utility of negative mode ultraviolet photodissociation (UVPD) MS for the characterization of acidic O-linked glycopeptide anions. This method was evaluated for a series of singly and multiply deprotonated glycopeptides from the model glycoprotein kappa casein, resulting in production of both peptide and glycan product ions that afforded 100% sequence coverage of the peptide and glycan moieties from a single MS/MS event. The most abundant and frequent peptide sequence ions were a/x-type products which, importantly, were found to retain the labile glycan modifications. The glycan-specific ions mainly arose from glycosidic bond cleavages (B, Y, C, and Z ions) in addition to some less common cross-ring cleavages. On the basis of the UVPD fragmentation patterns, an automated database searching strategy (based on the MassMatrix algorithm) was designed that is specific for the analysis of glycopeptide anions by UVPD. This algorithm was used to identify glycopeptides from mixtures of glycosylated and nonglycosylated peptides, sequence both glycan and peptide moieties simultaneously, and pinpoint the correct site(s) of glycosylation. This methodology was applied to uncover novel site-specificity of the O-linked glycosylated OmpA/MotB from the "superbug" A. baumannii to help aid in the elucidation of the functional role that protein glycosylation plays in pathogenesis.

Indexed as

Ultraviolet RaysAcinetobacter baumanniiAnionsAutomationBacterial Outer Membrane ProteinsBacterial ProteinsChromatography, LiquidGlycopeptidesMass SpectrometryModels, MolecularPolysaccharidesAnionsBacterial Outer Membrane ProteinsBacterial ProteinsGlycopeptidesMotB protein, BacteriaOMPA outer membrane proteinsPolysaccharides

Identifiers

PMID24006841
PMCPMC3816934
OpenAlexW2093208477

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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.