Evidence map›Paper›PMID 27649061›Full record

ArticleAnalytical chemistry2016

Data Independent Analysis of IgG Glycoforms in Samples of Unfractionated Human Plasma.

Miloslav Sanda, Radoslav Goldman

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Calculating Glycoprotein Similarities From Mass Spectrometric Data.Molecular & cellular proteomics : MCP · 2021
    Review
  17. The Role of Data-Independent Acquisition for Glycoproteomics.Molecular & cellular proteomics : MCP · 2021
    Review
  18. Review
  19. Article
  20. Why Glycosylation Matters in Building a Better Flu Vaccine.Molecular & cellular proteomics : MCP · 2019
    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

2 authors at 2 institutions in 1 country.

Miloslav SandaDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University , Washington, District of Columbia 20057, United States.
Radoslav GoldmanDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University , Washington, District of Columbia 20057, United States.
Georgetown University · USGeorgetown University Medical Center · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI Louis M Weiner · 1990 to 2026
$71.5M
Glycans in Hepatocellular CarcinomaR01CA135069 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2009 to 2019
$4.1M
Alliance of Glycobiologists for Detection of CancerU01CA168926 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2012 to 2016
$2.0M
Basic Cancer Research in Cancer Health DisparitiesU01CA171146 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2012 to 2016
$1.5M
NCI NIH HHS P30 CA051008NCI NIH HHS R01 CA135069NCI NIH HHS U01 CA168926NCI NIH HHS U01 CA171146
6 · The paper itself

Abstract

Glycosylation regulates functional responses mediated by the interaction of IgG with their receptors. Multiple analytical methods have been designed for the determination of the IgG N-glycan microheterogeneity, including MS methods for the analysis of site specific glycoforms of IgG. However, measurement of low abundant glycoforms remains challenging in complex samples like serum without enrichment of the IgG. We present a workflow for quantitative analysis of site specific glycoforms of IgG based on data independent acquisition (DIA) of Y-ions generated under "minimal" fragmentation conditions. The adjusted collision induced dissociation (CID) conditions generate specific Y-ions in the yield of up to 60% precursor ion intensity. These selective fragments, measured in high resolution, improve specificity of detection compared to the typically quantified B-ions which have higher overall intensity but lower signal-to-noise ratios. Under optimized conditions, we achieve label-free quantification of the majority of previously reported glycoforms of IgG (26 glycoforms of IgG1, 22 glycoforms of IgG 2/3, and 19 glycoforms of IgG4) directly in unfractionated samples of human plasma and we detect traces of previously unreported glycoforms of IgG1, including doubly fucosylated glycoforms. The SWATH data independent quantification of IgG glycoforms in pooled plasma samples of patients with liver cirrhosis detects reliably the expected changes in the quantity of major glycoforms compared to healthy controls. Our results show that optimized CID fragmentation enables DIA of IgG glycoforms and suggest that such workflow may enable quantitative analyses of the glycoproteome in complex matrixes.

Indexed as

Chromatography, LiquidGlycopeptidesGlycosylationHumansImmunoglobulin GMolecular StructureTandem Mass SpectrometryGlycopeptidesImmunoglobulin G

Identifiers

PMID27649061
PMCPMC5803558
OpenAlexW2523232993

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.