Evidence map›Paper›PMID 29231704›Full record

ArticleAnalytical chemistry2018

Site-Specific Glycan Heterogeneity Characterization by Hydrophilic Interaction Liquid Chromatography Solid-Phase Extraction, Reversed-Phase Liquid Chromatography Fractionation, and Capillary Zone Electrophoresis-Electrospray Ionization-Tandem Mass Spectrometry.

Yanyan Qu, Liangliang Sun, Zhenbin Zhang, Norman J Dovichi

Abstract read
In one paragraph

Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. [Simultaneous determination of five lignans fromSe pu = Chinese journal of chromatography · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Towards structure-focused glycoproteomics.Biochemical Society transactions · 2021
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
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

4 authors at 2 institutions in 1 country.

Yanyan QuDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Liangliang SunDepartment of Chemistry, Michigan State University , East Lansing, Michigan 48824, United States.ORCID 0000-0001-8939-5042
Zhenbin ZhangDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Norman J DovichiDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.ORCID 0000-0002-1331-3191
University of Notre Dame · USMichigan State University · US

Funding

Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
Technology for single cell proteomics and its application to the analysis of single Xenopus blastomeresR01GM096767 · NIGMS · UNIVERSITY OF NOTRE DAME · PI DOVICHI, NORMAN J · 2011 to 2019
$2.5M
NIGMS NIH HHS R01 GM096767NIGMS NIH HHS U54 GM105816
6 · The paper itself

Abstract

Reversed-phase chromatographic separation of glycopeptides tends to be dominated by the peptide composition. In contrast, capillary zone electrophoresis separation of glycopeptides is particularly sensitive to the sialic acid composition of the glycan. In this paper, we combine the two techniques to achieve superior N-glycopeptide analysis. Glycopeptides were first isolated from a tryptic digest using hydrophilic interaction liquid chromatography (HILIC) solid-phase extraction. The glycopeptides were separated using reversed-phase ultra high-performance liquid chromatography (UHPLC) to generate four fractions corresponding to different peptide backbones. Capillary zone electrophoresis-electrospray ionization-tandem mass spectrometry (CZE-ESI-MS/MS) was used to analyze the fractions. We applied this method for the analysis of alpha-1-acid glycoprotein (AGP). A total of 268 site-specific N-glycopeptides were detected, representing eight different glycosylation sites from two isomers of AGP. Glycans included tetra-sialic acids with multi N-acetyllactosamine (LacNAc) repeats and unusual pentasialylated terminal sialic acids. Reversed-phase UHPLC coupled with CZE generated ∼35% more N-glycopeptides than direct reversed-phase UHPLC-ESI-MS/MS analysis and ∼70% more N-glycopeptides than direct CZE-ESI-MS/MS analysis. This approach is a promising tool for global, site-specific glycosylation analysis of highly heterogeneous glycoproteins with mass-limited samples.

Indexed as

AnimalsCattleChromatography, High Pressure LiquidChromatography, Reverse-PhaseElectrophoresis, CapillaryGlycopeptidesGlycoproteinsGlycosylationHumansHydrophobic and Hydrophilic InteractionsOrosomucoidPolysaccharidesSolid Phase ExtractionSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryGlycopeptidesGlycoproteinsOrosomucoidPolysaccharides

Identifiers

PMID29231704
PMCPMC5771954
OpenAlexW2772801344

What OpenQuestion holds

Textmetadata
LicenceTDM
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.