Evidence map›Paper›PMID 37794193›Full record

ArticleNature2023

Sialoglycan binding triggers spike opening in a human coronavirus.

Matti F Pronker, Robert Creutznacher, Ieva Drulyte, Ruben J G Hulswit, Zeshi Li, Frank J M van Kuppeveld, Joost Snijder, Yifei Lang, Berend-Jan Bosch, Geert-Jan Boons and 3 more

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
14.6field-weighted citation impact, top 1% 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

61 citing papers in PubMed, 75 citations in OpenAlex.

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  15. Human coronavirus HKU1 neutralization by glycan receptor mimicry.bioRxiv : the preprint server for biology · 2025
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1 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

13 authors at 4 institutions in 3 countries.

Matti F PronkerBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0001-5268-7690
Robert CreutznacherVirology Section, Infectious Diseases and Immunology Division, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0002-5998-2171
Ieva DrulyteMaterials and Structural Analysis, Thermo Fisher Scientific, Eindhoven, The Netherlands.
Ruben J G HulswitVirology Section, Infectious Diseases and Immunology Division, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Zeshi LiDepartment of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0002-8358-3162
Frank J M van KuppeveldVirology Section, Infectious Diseases and Immunology Division, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0001-5800-749X
Joost SnijderBiomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0002-9310-8226
Yifei LangVirology Section, Infectious Diseases and Immunology Division, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Berend-Jan BoschVirology Section, Infectious Diseases and Immunology Division, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.ORCID 0000-0002-3864-232X
Geert-Jan BoonsDepartment of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands.
Martin FrankBiognos AB, Gothenburg, Sweden.ORCID 0000-0002-1006-6746
Raoul J de GrootVirology Section, Infectious Diseases and Immunology Division, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands. r.j.degroot@uu.nl.ORCID 0000-0002-2207-9472
Daniel L HurdissVirology Section, Infectious Diseases and Immunology Division, Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands. d.l.hurdiss@uu.nl.ORCID 0000-0003-3834-5808
Utrecht University · NLBiognos (Sweden) · SEThermo Fisher Scientific (Netherlands) · NLUniversity of Applied Sciences Utrecht · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coronavirus spike proteins mediate receptor binding and membrane fusion, making them prime targets for neutralizing antibodies. In the cases of severe acute respiratory syndrome coronavirus, severe acute respiratory syndrome coronavirus 2 and Middle East respiratory syndrome coronavirus, spike proteins transition freely between open and closed conformations to balance host cell attachment and immune evasion

Indexed as

BetacoronavirusPolysaccharidesSialic AcidsSpike Glycoprotein, CoronavirusAllosteric RegulationCommon ColdCryoelectron MicroscopyHumansImmune EvasionMolecular Dynamics SimulationProtein BindingProtein ConformationPolysaccharidesSialic AcidsSpike Glycoprotein, Coronavirus

Identifiers

PMID37794193
PMCPMC10700143
OpenAlexW4387332426

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.