Evidence map›Paper›PMID 34824474›Full record

ArticleNature methods2021

Precise, fast and comprehensive analysis of intact glycopeptides and modified glycans with pGlyco3.

Wen-Feng Zeng, Wei-Qian Cao, Ming-Qi Liu, Si-Min He, Peng-Yuan Yang

Open access · hybridAbstract read
In one paragraph

Article in Nature methods, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

117 citing papers in PubMed, 215 citations in OpenAlex.

  1. Glycopeptide Mass Spectrometry Data Analysis Using Protein Prospector.Methods in molecular biology (Clifton, N.J.) · 2027
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  7. Deep Learning Prediction of O-Glycopeptide Tandem Mass Spectra Enhances O-Glycoproteomics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  17. UnderstandingJournal of the American Society for Mass Spectrometry · 2026
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57 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Wen-Feng Zeng *Key Laboratory of Intelligent Information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China. wzeng@biochem.mpg.de.ORCID http://orcid.org/0000-0003-4325-2147
Wei-Qian Cao *Shanghai Fifth People's Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.ORCID http://orcid.org/0000-0002-1007-4607
Ming-Qi LiuShanghai Fifth People's Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
Si-Min HeKey Laboratory of Intelligent Information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Peng-Yuan YangShanghai Fifth People's Hospital and Institutes of Biomedical Sciences, Fudan University, Shanghai, China.ORCID http://orcid.org/0000-0001-5779-1008
Fudan University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Great advances have been made in mass spectrometric data interpretation for intact glycopeptide analysis. However, accurate identification of intact glycopeptides and modified saccharide units at the site-specific level and with fast speed remains challenging. Here, we present a glycan-first glycopeptide search engine, pGlyco3, to comprehensively analyze intact N- and O-glycopeptides, including glycopeptides with modified saccharide units. A glycan ion-indexing algorithm developed for glycan-first search makes pGlyco3 5-40 times faster than other glycoproteomic search engines without decreasing accuracy or sensitivity. By combining electron-based dissociation spectra, pGlyco3 integrates a dynamic programming-based algorithm termed pGlycoSite for site-specific glycan localization. Our evaluation shows that the site-specific glycan localization probabilities estimated by pGlycoSite are suitable to localize site-specific glycans. With pGlyco3, we confidently identified N-glycopeptides and O-mannose glycopeptides that were extensively modified by ammonia adducts in yeast samples. The freely available pGlyco3 is an accurate and flexible tool that can be used to identify glycopeptides and modified saccharide units.

Indexed as

ProteomeAlgorithmsAnimalsComputational BiologyFirefliesGlycopeptidesGlycosylationHEK293 CellsHumansMannosePolysaccharidesProbabilityProteomicsReproducibility of ResultsSaccharomyces cerevisiaeSchizosaccharomycesGlycopeptidesMannosePolysaccharidesProteome

Identifiers

PMID34824474
PMCPMC8648562
OpenAlexW3214881753

What OpenQuestion holds

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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.