Evidence map›Paper›PMID 31572782›Full record

ArticleACS central science2019

Glycoprofile Analysis of an Intact Glycoprotein As Inferred by NMR Spectroscopy.

Luca Unione, Maria Pia Lenza, Ana Ardá, Pedro Urquiza, Ana Laín, Juan Manuel Falcón-Pérez, Jesús Jiménez-Barbero, Oscar Millet

Abstract read
In one paragraph

Article in ACS central science, 2019. 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
–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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Chemical Shift Analysis of Oligosaccharides.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020
    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

8 authors.

Luca UnioneCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.
Maria Pia LenzaCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.
Ana ArdáCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.
Pedro UrquizaCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.
Ana LaínCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.
Juan Manuel Falcón-PérezCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.
Jesús Jiménez-BarberoCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.
Oscar MilletCIC bioGUNE, Bizkaia Technology Park, Bld 800, 48170 Derio, Spain.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein N-glycosylation stands out for its intrinsic and functionally related heterogeneity. Despite its biomedical interest, Glycoprofile analysis still remains a major scientific challenge. Here, we present an NMR-based strategy to delineate the N-glycan composition in intact glycoproteins and under physiological conditions. The employed methodology allowed dissecting the glycan pattern of the IgE high-affinity receptor (FcεRIα) expressed in human HEK 293 cells, identifying the presence and relative abundance of specific glycan epitopes. Chemical shifts and differences in the signal line-broadening between the native and the unfolded states were integrated to build a structural model of FcεRIα that was able to identify intramolecular interactions between high-mannose N-glycans and the protein surface. In turn, complex type N-glycans reflect a large solvent accessibility, suggesting a functional role as interaction sites for receptors. The interaction between intact FcεRIα and the lectin hGal3, also studied here, confirms this hypothesis and opens new avenues for the detection of specific N-glycan epitopes and for the studies of glycoprotein-receptor interactions mediated by N-glycans.

Identifiers

PMID31572782
PMCPMC6764210

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.