Evidence map›Paper›PMID 26729457›Full record

ArticleJournal of the American Society for Mass Spectrometry2016

The Art of Destruction: Optimizing Collision Energies in Quadrupole-Time of Flight (Q-TOF) Instruments for Glycopeptide-Based Glycoproteomics.

Hannes Hinneburg, Kathrin Stavenhagen, Ulrike Schweiger-Hufnagel, Stuart Pengelley, Wolfgang Jabs, Peter H Seeberger, Daniel Varón Silva, Manfred Wuhrer, Daniel Kolarich

Open access · hybridAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed, 1 pooled it
8.4field-weighted citation impact, top 2% 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

79 citing papers in PubMed, 1 synthesis or guideline pooled it, 137 citations in OpenAlex.

  1. Pooled it
  2. Glycopeptide Mass Spectrometry Data Analysis Using Protein Prospector.Methods in molecular biology (Clifton, N.J.) · 2027
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  13. Can We BoostJournal of the American Society for Mass Spectrometry · 2024
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19 more citing papers are in PubMed but not listed here.

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

9 authors at 4 institutions in 2 countries.

Hannes HinneburgDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Kathrin StavenhagenDivision of BioAnalytical Chemistry, VU University Amsterdam, Amsterdam, The Netherlands.
Ulrike Schweiger-HufnagelBruker Daltonik GmbH, Bremen, Germany.
Stuart PengelleyBruker Daltonik GmbH, Bremen, Germany.
Wolfgang JabsBruker Daltonik GmbH, Bremen, Germany.
Peter H SeebergerDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Daniel Varón SilvaDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany.
Manfred WuhrerDivision of BioAnalytical Chemistry, VU University Amsterdam, Amsterdam, The Netherlands.
Daniel KolarichDepartment of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424, Potsdam, Germany. daniel.kolarich@mpikg.mpg.de.ORCID http://orcid.org/0000-0002-8452-1350
Max Planck Institute of Colloids and Interfaces · DEBruker (Germany) · DENetherlands Metabolomics Centre · NLVrije Universiteit Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In-depth site-specific investigations of protein glycosylation are the basis for understanding the biological function of glycoproteins. Mass spectrometry-based N- and O-glycopeptide analyses enable determination of the glycosylation site, site occupancy, as well as glycan varieties present on a particular site. However, the depth of information is highly dependent on the applied analytical tools, including glycopeptide fragmentation regimes and automated data analysis. Here, we used a small set of synthetic disialylated, biantennary N-glycopeptides to systematically tune Q-TOF instrument parameters towards optimal energy stepping collision induced dissociation (CID) of glycopeptides. A linear dependency of m/z-ratio and optimal fragmentation energy was found, showing that with increasing m/z-ratio, more energy is required for glycopeptide fragmentation. Based on these optimized fragmentation parameters, a method combining lower- and higher-energy CID was developed, allowing the online acquisition of glycan and peptide-specific fragments within a single tandem MS experiment. We validated this method analyzing a set of human immunoglobulins (IgA1+2, sIgA, IgG1+2, IgE, IgD, IgM) as well as bovine fetuin. These optimized fragmentation parameters also enabled software-assisted glycopeptide assignment of both N- and O-glycopeptides including information about the most abundant glycan compositions, peptide sequence and putative structures. Twenty-six out of 30 N-glycopeptides and four out of five O-glycopeptides carrying >110 different glycoforms could be identified by this optimized LC-ESI tandem MS method with minimal user input. The Q-TOF based glycopeptide analysis platform presented here opens the way to a range of different applications in glycoproteomics research as well as biopharmaceutical development and quality control.

Indexed as

Amino Acid SequenceAnimalsCarbohydrate SequenceCattleFetuinsGlycopeptidesHumansImmunoglobulinsProteomicsSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryFetuinsGlycopeptidesImmunoglobulinsCollision energy stepping CIDGlycopeptideGlycoproteomicsImmunoglobulinN-glycanO-glycanQ-TOFSynthetic glycopeptides

Identifiers

PMID26729457
PMCPMC4756043
OpenAlexW2223966355

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.