Evidence map›Paper›PMID 36201757›Full record

ArticleJournal of proteome research2022

Diversity Matters: Optimal Collision Energies for Tandem Mass Spectrometric Analysis of a Large Set of N-Glycopeptides.

Helga Hevér, Kinga Nagy, Andrea Xue, Simon Sugár, Kinga Komka, Károly Vékey, László Drahos, Ágnes Révész

Open access · hybridAbstract read
In one paragraph

Article in Journal of proteome research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

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  10. Can We BoostJournal of the American Society for Mass Spectrometry · 2024
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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 4 institutions in 2 countries.

Helga HevérMS Proteomics Research Group, Eötvös Loránd Research Network, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, Budapest H-1117, Hungary.
Kinga NagyMS Proteomics Research Group, Eötvös Loránd Research Network, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, Budapest H-1117, Hungary.ORCID 0000-0002-0582-7133
Andrea XueMS Proteomics Research Group, Eötvös Loránd Research Network, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, Budapest H-1117, Hungary.
Simon SugárMS Proteomics Research Group, Eötvös Loránd Research Network, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, Budapest H-1117, Hungary.
Kinga KomkaDepartment of Chemical and Environmental Process Engineering, Budapest University of Technology and Economics, Budapest H-1111, Hungary.
Károly VékeyMS Proteomics Research Group, Eötvös Loránd Research Network, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, Budapest H-1117, Hungary.
László DrahosMS Proteomics Research Group, Eötvös Loránd Research Network, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, Budapest H-1117, Hungary.ORCID 0000-0001-9589-6652
Ágnes RévészMS Proteomics Research Group, Eötvös Loránd Research Network, Research Centre for Natural Sciences, Magyar Tudósok körútja 2, Budapest H-1117, Hungary.ORCID 0000-0002-6221-1239
Research Network (United States) · USBudapest University of Technology and Economics · HUEötvös Loránd University · HUGedeon Richter (Hungary) · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identification and characterization of N-glycopeptides from complex samples are usually based on tandem mass spectrometric measurements. Experimental settings, especially the collision energy selection method, fundamentally influence the obtained fragmentation pattern and hence the confidence of the database search results ("score"). Using standards of naturally occurring glycoproteins, we mapped the Byonic and pGlyco search engine scores of almost 200 individual N-glycopeptides as a function of collision energy settings on a quadrupole time of flight instrument. The resulting unprecedented amount of peptide-level information on such a large and diverse set of N-glycopeptides revealed that the peptide sequence heavily influences the energy for the highest score on top of an expected general linear trend with

Indexed as

GlycopeptidesProteomicsGlycoproteinsGlycosylationPeptidesTandem Mass SpectrometryGlycopeptidesGlycoproteinsPeptidesbottom-up proteomicscollision energy optimizationglycopeptide fragmentationidentification scoreN-glycosylationsearch enginetandem mass spectrometrytransferability

Identifiers

PMID36201757
PMCPMC9639208
OpenAlexW4302774644

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.