Evidence map›Paper›PMID 36928389›Full record

ArticleNucleic acids research2023

A hybrid structure determination approach to investigate the druggability of the nucleocapsid protein of SARS-CoV-2.

Giacomo Padroni, Maria Bikaki, Mihajlo Novakovic, Antje C Wolter, Simon H Rüdisser, Alvar D Gossert, Alexander Leitner, Frederic H-T Allain

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  4. How does NMR support SARS-CoV-2 protein-ligand interaction studies?Analytical and bioanalytical chemistry · 2026
    Review
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  17. Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.bioRxiv : the preprint server for biology · 2023
    Article
  18. Article
  19. 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 at 1 institution in 1 country.

Giacomo PadroniInstitute of Biochemistry, Department of Biology, ETH Zurich, Hönggerbergring 64, 8093 Zürich, Switzerland.
Maria BikakiInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland.
Mihajlo NovakovicInstitute of Biochemistry, Department of Biology, ETH Zurich, Hönggerbergring 64, 8093 Zürich, Switzerland.
Antje C WolterInstitute of Biochemistry, Department of Biology, ETH Zurich, Hönggerbergring 64, 8093 Zürich, Switzerland.
Simon H RüdisserBiomolecular NMR Spectroscopy Platform, ETH Zurich, Hönggerbergring 64, 8093 Zürich, Switzerland.
Alvar D GossertBiomolecular NMR Spectroscopy Platform, ETH Zurich, Hönggerbergring 64, 8093 Zürich, Switzerland.
Alexander LeitnerInstitute of Molecular Systems Biology, Department of Biology, ETH Zurich, Otto-Stern-Weg 3, 8093 Zürich, Switzerland.
Frederic H-T AllainInstitute of Biochemistry, Department of Biology, ETH Zurich, Hönggerbergring 64, 8093 Zürich, Switzerland.ORCID 0000-0002-2131-6237
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pandemic caused by SARS-CoV-2 has called for concerted efforts to generate new insights into the biology of betacoronaviruses to inform drug screening and development. Here, we establish a workflow to determine the RNA recognition and druggability of the nucleocapsid N-protein of SARS-CoV-2, a highly abundant protein crucial for the viral life cycle. We use a synergistic method that combines NMR spectroscopy and protein-RNA cross-linking coupled to mass spectrometry to quickly determine the RNA binding of two RNA recognition domains of the N-protein. Finally, we explore the druggability of these domains by performing an NMR fragment screening. This workflow identified small molecule chemotypes that bind to RNA binding interfaces and that have promising properties for further fragment expansion and drug development.

Indexed as

Coronavirus Nucleocapsid ProteinsCOVID-19COVID-19 Drug TreatmentDrug DevelopmentSARS-CoV-2HumansMass SpectrometryNuclear Magnetic Resonance, BiomolecularPhosphoproteinsProtein BindingRNA, ViralWorkflowCoronavirus Nucleocapsid Proteinsnucleocapsid phosphoprotein, SARS-CoV-2PhosphoproteinsRNA, Viral

Identifiers

PMID36928389
PMCPMC10201421
OpenAlexW4327681706

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.