Evidence map›Paper›PMID 34208755›Full record

ArticleInternational journal of molecular sciences2021

More Is Always Better Than One: The N-Terminal Domain of the Spike Protein as Another Emerging Target for Hampering the SARS-CoV-2 Attachment to Host Cells.

Sonia Di Gaetano, Domenica Capasso, Pietro Delre, Luciano Pirone, Michele Saviano, Emilia Pedone, Giuseppe Felice Mangiatordi

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  8. Molecular Virology of SARS-CoV-2 and Related Coronaviruses.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  9. Article
  10. Review
  11. Structural and energetic analyses of SARS-CoV-2Computational and structural biotechnology journal · 2022
    Article
  12. Review
  13. Article
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 at 3 institutions in 1 country.

Sonia Di GaetanoInstitute of Biostructures and Bioimaging, CNR, 80134 Naples, Italy.ORCID 0000-0001-5523-3619
Domenica CapassoCIRPEB, University of Naples "Federico II", 80134 Naples, Italy.ORCID 0000-0001-7201-3431
Pietro DelreInstitute of Crystallography, CNR, 70126 Bari, Italy.
Luciano PironeInstitute of Biostructures and Bioimaging, CNR, 80134 Naples, Italy.ORCID 0000-0002-7014-4689
Michele SavianoCIRPEB, University of Naples "Federico II", 80134 Naples, Italy.
Emilia PedoneInstitute of Biostructures and Bioimaging, CNR, 80134 Naples, Italy.ORCID 0000-0003-0203-8611
Giuseppe Felice MangiatordiInstitute of Crystallography, CNR, 70126 Bari, Italy.ORCID 0000-0003-4042-2841
Federico II University Hospital · ITInstitute of Crystallography · ITInstitute of Biostructure and Bioimaging · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although the approved vaccines are proving to be of utmost importance in containing the Coronavirus disease 2019 (COVID-19) threat, they will hardly be resolutive as new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2, a single-stranded RNA virus) variants might be insensitive to the immune response they induce. In this scenario, developing an effective therapy is still a dire need. Different targets for therapeutic antibodies and diagnostics have been identified, among which the SARS-CoV-2 spike (S) glycoprotein, particularly its receptor-binding domain, has been defined as crucial. In this context, we aim to focus attention also on the role played by the S N-terminal domain (S1-NTD) in the virus attachment, already recognized as a valuable target for neutralizing antibodies, in particular, building on a cavity mapping indicating the presence of two druggable pockets and on the recent literature hypothesizing the presence of a ganglioside-binding domain. In this perspective, we aim at proposing S1-NTD as a putative target for designing small molecules hopefully able to hamper the SARS-CoV-2 attachment to host cells.

Indexed as

Binding SitesCOVID-19Drug RepositioningHumansMolecular Dynamics SimulationN-Acetylneuraminic AcidProtein BindingProtein DomainsSARS-CoV-2Small Molecule LibrariesSpike Glycoprotein, CoronavirusVirus AttachmentN-Acetylneuraminic AcidSmall Molecule LibrariesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2cavity mappinggalectin inhibitorsspike Protein

Identifiers

PMID34208755
PMCPMC8235207
OpenAlexW3172464066

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.