Evidence map›Paper›PMID 33185784›Full record

ArticleThe protein journal2020

Comparison of Binding Site of Remdesivir and Its Metabolites with NSP12-NSP7-NSP8, and NSP3 of SARS CoV-2 Virus and Alternative Potential Drugs for COVID-19 Treatment.

Lindsey S Jung, Tamara M Gund, Mahesh Narayan

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The protein journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.5field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Expression and immunogenicity of non-structural protein 8 of porcine epidemic diarrhea virus.Veterinary research forum : an international quarterly journal · 2024
    Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Therapeutic dilemmas in addressing SARS-CoV-2 infection: Favipiravir versus Remdesivir.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022
    Review
  7. Article
  8. Review
  9. Review
  10. An overview of potential inhibitors targeting non-structural proteins 3 (PLComputational and structural biotechnology journal · 2021
    Review
  11. Review
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

3 authors at 3 institutions in 1 country.

Lindsey S JungTenafly High School, Tenafly, NJ, 07670, USA.
Tamara M GundDepartment of Chemistry and Environmental Science, New Jersey Institute of Technology, University Heights, Newark, NJ, 07102, USA.
Mahesh NarayanDepartment of Chemistry and Biochemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA. mnarayan@utep.edu.ORCID 0000-0002-2194-5228
Childrens Cardiomyopathy Foundation · USNew Jersey Institute of Technology · USThe University of Texas at El Paso · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Remdesivir was approved by the U.S.A. Food and Drug administration for emergency use to interfere with the replication of SARS CoV-2 virus (the agent that causes COVID-19) in adults and children hospitalized with severe disease. The crystal structure of the metabolite of remdesivir (Monophosphate of GS-441524) and NSP12-NSP8-NSP7 of SARS CoV-2 virus was recently reported. The crystal structures of ADP-Ribose or AMP and NSP3 of SARS CoV-2 virus were also released, recently. This study compared their binding sites and suggests the crystal structure of NSP3 of SARS CoV-2 virus as an alternative binding site of AMP or ADP-ribose to treat COVID-19. We virtually screened 682 FDA-approved compounds, and the top 10 compounds were selected by analysis of docking scores, (G-score, D-score, and Chemscore) and visual analysis using a structure-based docking approach of NSP3 of SARS CoV-2 virus. All immunization approaches are based on the SARS-CoV-2 virus spike protein. A recent study reported that the D614G mutation in the SARS-CoV-2 virus spike protein reduces S1 shedding and increases infectivity of SARS COV-2 virus. Therefore, if there is a severe change in the spike protein of a modified Coronavirus, all developed vaccines can lose their efficacy, necessitating the need for an alternative treatment method. The top 10 compounds (FDA-approved) in this study are selected based on NSP 3 binding site, and therefore are a potential viable treatment because they will show potential activity for all mutations in the SARS-CoV-2 virus spike protein.

Indexed as

COVID-19 Drug TreatmentAdenosine MonophosphateAlanineAntiviral AgentsBinding SitesCoronavirus Papain-Like ProteasesCoronavirus RNA-Dependent RNA PolymeraseCOVID-19HumansMolecular Docking SimulationProtein ConformationSARS-CoV-2Viral Nonstructural ProteinsAdenosine MonophosphateAlanineAntiviral AgentsCoronavirus Papain-Like ProteasesCoronavirus RNA-Dependent RNA PolymeraseNS8 protein, SARS-CoV-2NSP12 protein, SARS-CoV-2ORF1ab polyprotein, SARS-CoV-2papain-like protease, SARS-CoV-2remdesivirViral Nonstructural ProteinsNon-structural protein 3 (NSP3) of SARS CoV-2 virusRemdesivirVirtual screening

Identifiers

PMID33185784
PMCPMC7662030
OpenAlexW3102054360

What OpenQuestion holds

Textmetadata
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.