Evidence map›Paper›PMID 22942711›Full record

ReviewInternational journal of molecular sciences2012

Function and 3D structure of the N-glycans on glycoproteins.

Masamichi Nagae, Yoshiki Yamaguchi

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.5field-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

63 citing papers in PubMed, 129 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. IntegratingMolecular omics · 2025
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Structural Prediction and Characterization ofMolecules (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Article
  17. Glycoprotein molecular dynamics analysis: SARS-CoV-2 spike glycoprotein case study.Advances in protein chemistry and structural biology · 2022
    Article
  18. Article
  19. Improvement of the Force Field forMolecules (Basel, Switzerland) · 2021
    Article
  20. Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021
    Review

3 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Masamichi NagaeStructural Glycobiology Team, RIKEN, Advanced Science Institute, 2-1 Hirosawa, Wako-City, Saitama 351-0198, Japan.
Yoshiki YamaguchiStructural Glycobiology Team, RIKEN, Advanced Science Institute, 2-1 Hirosawa, Wako-City, Saitama 351-0198, Japan.ORCID 0000-0003-0100-5439
RIKEN Advanced Science Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is one of the most common post-translational modifications in eukaryotic cells and plays important roles in many biological processes, such as the immune response and protein quality control systems. It has been notoriously difficult to study glycoproteins by X-ray crystallography since the glycan moieties usually have a heterogeneous chemical structure and conformation, and are often mobile. Nonetheless, recent technical advances in glycoprotein crystallography have accelerated the accumulation of 3D structural information. Statistical analysis of "snapshots" of glycoproteins can provide clues to understanding their structural and dynamic aspects. In this review, we provide an overview of crystallographic analyses of glycoproteins, in which electron density of the glycan moiety is clearly observed. These well-defined N-glycan structures are in most cases attributed to carbohydrate-protein and/or carbohydrate-carbohydrate interactions and may function as "molecular glue" to help stabilize inter- and intra-molecular interactions. However, the more mobile N-glycans on cell surface receptors, the electron density of which is usually missing on X-ray crystallography, seem to guide the partner ligand to its binding site and prevent irregular protein aggregation by covering oligomerization sites away from the ligand-binding site.

Indexed as

AnimalsCarbohydrate ConformationGlycoproteinsGlycosylationHumansModels, MolecularPolysaccharidesProtein Processing, Post-TranslationalProtein StabilityGlycoproteinsPolysaccharidesglycoformglycoproteinN-glycanprotein crystallography

Identifiers

PMID22942711
PMCPMC3430242
OpenAlexW2074910307

What OpenQuestion holds

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LicenceCC BY
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.