Evidence map›Paper›PMID 39402214›Full record

ArticleNature methods2024

Restoring protein glycosylation with GlycoShape.

Callum M Ives, Ojas Singh, Silvia D'Andrea, Carl A Fogarty, Aoife M Harbison, Akash Satheesan, Beatrice Tropea, Elisa Fadda

Abstract read
In one paragraph

Article in Nature methods, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Site-specific O-glycans influence lacritin structure and multimerization in tears.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Article
  4. Unraveling the Glycosylation Machinery ofInternational journal of molecular sciences · 2026
    Article
  5. Automating Model Building for SPM Images of Biomolecules Using MISO.Journal of chemical information and modeling · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Guidelines for Comparing Circular Dichroism Spectroscopy and Molecular Dynamics Simulations for Biomolecules.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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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.

Callum M Ives *Department of Chemistry, Maynooth University, Maynooth, Ireland.ORCID http://orcid.org/0000-0003-0511-1220
Ojas Singh *Department of Chemistry, Maynooth University, Maynooth, Ireland.ORCID http://orcid.org/0000-0002-2586-2542
Silvia D'AndreaDepartment of Chemistry, Maynooth University, Maynooth, Ireland.
Carl A FogartyDepartment of Chemistry, Maynooth University, Maynooth, Ireland.
Aoife M HarbisonDepartment of Chemistry, Maynooth University, Maynooth, Ireland.
Akash SatheesanHamilton Institute, Maynooth University, Maynooth, Ireland.
Beatrice TropeaHamilton Institute, Maynooth University, Maynooth, Ireland.
Elisa FaddaSchool of Biological Sciences, University of Southampton, Southampton, UK. elisa.fadda@soton.ac.uk.ORCID http://orcid.org/0000-0002-2898-7770

Funding

Irish Research Council (An Chomhairle um Thaighde in Éirinn) GOIPG/201912212
6 · The paper itself

Abstract

Despite ground-breaking innovations in experimental structural biology and protein structure prediction techniques, capturing the structure of the glycans that functionalize proteins remains a challenge. Here we introduce GlycoShape ( https://glycoshape.org ), an open-access glycan structure database and toolbox designed to restore glycoproteins to their native and functional form in seconds. The GlycoShape database counts over 500 unique glycans so far, covering the human glycome and augmented by elements from a wide range of organisms, obtained from 1 ms of cumulative sampling from molecular dynamics simulations. These structures can be linked to proteins with a robust algorithm named Re-Glyco, directly compatible with structural data in open-access repositories, such as the Research Collaboratory for Structural Bioinformatics Protein Data Bank (RCSB PDB) and AlphaFold Protein Structure Database, or own. The quality, performance and broad applicability of GlycoShape is demonstrated by its ability to predict N-glycosylation occupancy, scoring a 93% agreement with experiment, based on screening all proteins in the PDB with a corresponding glycoproteomics profile, for a total of 4,259 N-glycosylation sequons.

Indexed as

Databases, ProteinGlycoproteinsPolysaccharidesAlgorithmsComputational BiologyGlycosylationHumansMolecular Dynamics SimulationProtein ConformationSoftwareGlycoproteinsPolysaccharides

Identifiers

PMID39402214
PMCPMC11541215

What OpenQuestion holds

Textmetadata
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.