Evidence map›Paper›PMID 34010560›Full record

ArticleJournal of proteome research2021

GlycoHybridSeq: Automated Identification of N-Linked Glycopeptides Using Electron Transfer/High-Energy Collision Dissociation (EThcD).

Rui Zhang, Jianhui Zhu, David M Lubman, Yehia Mechref, Haixu Tang

Abstract read
In one paragraph

Article in Journal of proteome research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–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

8 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. A Boltzmann model predicts glycan structures from lectin binding.bioRxiv : the preprint server for biology · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Review
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

5 authors.

Rui ZhangDepartment of Computer Science, Luddy School of Informatics, Computing, and Engineering, Indiana University, Bloomington, Indiana 47405, United States.ORCID 0000-0003-0083-1165
Jianhui ZhuDepartment of Surgery, University of Michigan Medical Center, Ann Arbor, Michigan 48109, United States.ORCID 0000-0002-0051-7777
David M LubmanDepartment of Surgery, University of Michigan Medical Center, Ann Arbor, Michigan 48109, United States.ORCID 0000-0001-7731-0232
Yehia MechrefDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409, United States.ORCID 0000-0002-6661-6073
Haixu TangDepartment of Computer Science, Luddy School of Informatics, Computing, and Engineering, Indiana University, Bloomington, Indiana 47405, United States.

Funding

Supplemental for Detection of Glycopeptides of MCI in Patient SerumR01CA160254 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI David M. Lubman · 2012 to 2026
$5.4M
Sensitive and Quantitative MS-bases Glycomic Mapping PlatformR01GM112490 · NIGMS · TEXAS TECH UNIVERSITY · PI MECHREF, YEHIA · 2014 to 2024
$3.2M
Microsequencing in an Ion Trap/reTOF DeviceR01GM049500 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LUBMAN, DAVID M. · 1994 to 2016
$3.0M
Screening of Glycan Markers in Serum for Early Detection of HCC in Different Etiologies of DiseaseU01CA225753 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LUBMAN, DAVID M., MECHREF, YEHIA · 2018 to 2021
$2.0M
Developing high-throughput IMS-MS and IMS-IMS-MS techniques for glycomics analysiR01GM093322 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., MECHREF, YEHIA · 2010 to 2013
$1.1M
NCI NIH HHS R01 CA160254NCI NIH HHS U01 CA225753NIGMS NIH HHS R01 GM049500NIGMS NIH HHS R01 GM093322NIGMS NIH HHS R01 GM112490
6 · The paper itself

Abstract

Glycosylation is one of the most common post-translational modifications (PTM) occurring in a large variety of proteins with important biological functions in human and other higher organisms. Liquid chromatography tandem mass spectrometry (LC-MS/MS) has been routinely used to characterize site-specific protein glycosylation at high throughput in complex glycoproteomic samples. Recently, electron transfer/high-energy collision dissociation (EThcD) was introduced for glycopeptide identification, which offers rich structural information on glycopepides with the fragment ions from the cleavages of both the glycan and the peptide backbone. Herein, we present the software GlycoHybridSeq for automated interpretation of EThcD-MS/MS spectra from glycoproteomic data using a customized scoring function, which enables the functionalities of identifying glycopeptides, characterizing glycosylation sites, and distinguishing some isomeric glycans. We evaluate GlycoHybridSeq on glycoproteomic data collected for cancer biomarker discovery. The results showed that it achieved comparable or better performance than that of Byonic and MSFragger. GlycoHybridSeq is released as an open source software and is ready to be used in large-scale glycoproteomic data analyses.

Indexed as

GlycopeptidesTandem Mass SpectrometryChromatography, LiquidElectronsGlycosylationHumansGlycopeptidesalgorithmEThcDGlycoHybridSeqglycopeptide identificationglycoproteomicssoftware tooltandem mass spectrometry

Identifiers

PMID34010560
PMCPMC8185882

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.