Evidence map›Paper›PMID 27139140›Full record

ArticleScientific reports2016

pGlyco: a pipeline for the identification of intact N-glycopeptides by using HCD- and CID-MS/MS and MS3.

Wen-Feng Zeng, Ming-Qi Liu, Yang Zhang, Jian-Qiang Wu, Pan Fang, Chao Peng, Aiying Nie, Guoquan Yan, Weiqian Cao, Chao Liu and 5 more

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
–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

49 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  10. Can We BoostJournal of the American Society for Mass Spectrometry · 2024
    Article
  11. Plasma/Serum Proteomics based on Mass Spectrometry.Protein and peptide letters · 2024
    Review
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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

15 authors.

Wen-Feng ZengKey Lab of Intelligent information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Ming-Qi LiuInstitutes of Biomedical Sciences, Fudan University, Shanghai, China.
Yang ZhangInstitutes of Biomedical Sciences, Fudan University, Shanghai, China.
Jian-Qiang WuKey Lab of Intelligent information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Pan FangInstitutes of Biomedical Sciences, Fudan University, Shanghai, China.
Chao PengNational Center for Protein Science (Shanghai), Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
Aiying NieThermo Fisher Scientific Co., Ltd, Shanghai, China.
Guoquan YanInstitutes of Biomedical Sciences, Fudan University, Shanghai, China.
Weiqian CaoInstitutes of Biomedical Sciences, Fudan University, Shanghai, China.
Chao LiuKey Lab of Intelligent information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Hao ChiKey Lab of Intelligent information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Rui-Xiang SunKey Lab of Intelligent information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Catherine C L WongNational Center for Protein Science (Shanghai), Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.
Si-Min HeKey Lab of Intelligent information Processing of Chinese Academy of Sciences (CAS), Institute of Computing Technology, CAS, Beijing, China.
Pengyuan YangInstitutes of Biomedical Sciences, Fudan University, Shanghai, China.

Funding

Hepatic Encephalopathy in Alcoholic Cirrhosis: A Systems Biology ApproachR01AA020203 · NIAAA · VIRGINIA COMMONWEALTH UNIVERSITY · PI BAJAJ, JASMOHAN S · 2010 to 2012
$1.0M
NIAAA NIH HHS R01 AA020203
6 · The paper itself

Abstract

Confident characterization of the microheterogeneity of protein glycosylation through identification of intact glycopeptides remains one of the toughest analytical challenges for glycoproteomics. Recently proposed mass spectrometry (MS)-based methods still have some defects such as lack of the false discovery rate (FDR) analysis for the glycan identification and lack of sufficient fragmentation information for the peptide identification. Here we proposed pGlyco, a novel pipeline for the identification of intact glycopeptides by using complementary MS techniques: 1) HCD-MS/MS followed by product-dependent CID-MS/MS was used to provide complementary fragments to identify the glycans, and a novel target-decoy method was developed to estimate the false discovery rate of the glycan identification; 2) data-dependent acquisition of MS3 for some most intense peaks of HCD-MS/MS was used to provide fragments to identify the peptide backbones. By integrating HCD-MS/MS, CID-MS/MS and MS3, intact glycopeptides could be confidently identified. With pGlyco, a standard glycoprotein mixture was analyzed in the Orbitrap Fusion, and 309 non-redundant intact glycopeptides were identified with detailed spectral information of both glycans and peptides.

Indexed as

GlycopeptidesMass SpectrometryWorkflowGlycopeptides

Identifiers

PMID27139140
PMCPMC4853738

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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.