Evidence map›Paper›PMID 38864493›Full record

ArticleeLife2024

Role of N343 glycosylation on the SARS-CoV-2 S RBD structure and co-receptor binding across variants of concern.

Callum M Ives, Linh Nguyen, Carl A Fogarty, Aoife M Harbison, Yves Durocher, John Klassen, Elisa Fadda

Abstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Glycans Modulate the Adsorption of RBD Glycoproteins on Polarizable Surfaces.Journal of chemical information and modeling · 2026
    Article
  6. Review
  7. Article
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  10. Review
  11. 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

7 authors.

Callum M Ives *Department of Chemistry, Maynooth University, Maynooth, Ireland.
Linh Nguyen *Department of Chemistry, University of Alberta, Edmonton, Canada.
Carl A FogartyDepartment of Chemistry, Maynooth University, Maynooth, Ireland.
Aoife M HarbisonDepartment of Chemistry, Maynooth University, Maynooth, Ireland.
Yves DurocherHuman Health Therapeutics Research Centre, Life Sciences Division, National Research Council Canada, Québec, Canada.
John KlassenDepartment of Chemistry, University of Alberta, Edmonton, Canada.ORCID https://orcid.org/0000-0002-3389-7112
Elisa FaddaSchool of Biological Sciences, University of Southampton, Southampton, United Kingdom.ORCID https://orcid.org/0000-0002-2898-7770

Funding

Irish Research Council GOIPG/201912212Science Foundation Ireland 20/FFP-P/8809
6 · The paper itself

Abstract

Glycosylation of the SARS-CoV-2 spike (S) protein represents a key target for viral evolution because it affects both viral evasion and fitness. Successful variations in the glycan shield are difficult to achieve though, as protein glycosylation is also critical to folding and structural stability. Within this framework, the identification of glycosylation sites that are structurally dispensable can provide insight into the evolutionary mechanisms of the shield and inform immune surveillance. In this work, we show through over 45 μs of cumulative sampling from conventional and enhanced molecular dynamics (MD) simulations, how the structure of the immunodominant S receptor binding domain (RBD) is regulated by

Indexed as

Molecular Dynamics SimulationProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusBinding SitesCOVID-19GlycosylationHumansMutationPolysaccharidesProtein ConformationProtein DomainsPolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2COVID-19glycosylationhumanmolecular biophysicsRBDreceptor binding domainSARS-CoV-2spikestructural biologyvariants

Identifiers

PMID38864493
PMCPMC11168744

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.