Evidence map›Paper›PMID 32544320›Full record

ArticleAnalytical chemistry2020

Isomeric Separation of N-Glycopeptides Derived from Glycoproteins by Porous Graphitic Carbon (PGC) LC-MS/MS.

Rui Zhu, Yifan Huang, Jingfu Zhao, Jieqiang Zhong, Yehia Mechref

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  5. Analytical and bioanalytical chemistry · 2024
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  20. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    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 at 1 institution in 1 country.

Rui ZhuDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, United States.
Yifan HuangDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, United States.
Jingfu ZhaoDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, United States.
Jieqiang ZhongDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, United States.
Yehia MechrefDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, Texas 79409-1061, United States.ORCID 0000-0002-6661-6073
Texas Tech University · US

Funding

Sensitive and Quantitative MS-bases Glycomic Mapping PlatformR01GM112490 · NIGMS · TEXAS TECH UNIVERSITY · PI MECHREF, YEHIA · 2014 to 2024
$3.2M
Quantitative Characterization of Glycopeptide IsomersR01GM130091 · NIGMS · TEXAS TECH UNIVERSITY · PI Yehia Mechref · 2019 to 2026
$2.5M
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
NCI NIH HHS U01 CA225753NIGMS NIH HHS R01 GM112490NIGMS NIH HHS R01 GM130091
6 · The paper itself

Abstract

Protein glycosylation is involved in many biological processes and physiological functions. Despite the recent advances in LC-MS/MS methodologies, the profiling of site-specific glycosylation is one of the major analytical challenges of glycoprotein analysis. Herein, we report that the separation of glycopeptide isomers on porous graphitic carbon (PGC)-LC was significantly improved by elevating the separation temperature under basic mobile phases. These findings permitted the isomeric separation of glycopeptides resulting from highly specific enzymatic digestions. The selectivity for different glycan types was studied using bovine fetuin, asialofetuin, IgG, ribonuclease B, and alpha-1 acid glycoprotein (AGP) by PGC-LC-MS. Comprehensive structural isomeric separation of glycopeptides was observed by high-resolution MS and confirmed by MS/MS. The specific structures of the glycopeptide isomers were identified and confirmed through exoglycosidase digestions. Glycosylation analysis of human AGP revealed the potential use of PGC-LC-MS for extensive glycoprotein analysis for biomarker discovery. This newly developed separation technique was shown as a reproducible and useful analytical method to study site-specific isomeric glycosylation.

Indexed as

CarbonChemical FractionationChromatography, LiquidFetuinsGlycopeptidesGlycoproteinsPeptide HydrolasesTandem Mass SpectrometryCarbonFetuinsGlycopeptidesGlycoproteinsPeptide Hydrolases

Identifiers

PMID32544320
PMCPMC7815195
OpenAlexW3034221577

What OpenQuestion holds

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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.