Evidence map›Paper›PMID 35403085›Full record

ArticlePhytomedicine plus : international journal of phytotherapy and phytopharmacology2021

Computational screening of phytochemicals from three medicinal plants as inhibitors of transmembrane protease serine 2 implicated in SARS-CoV-2 infection.

Omotayo O Oyedara, Joseph M Agbedahunsi, Folasade M Adeyemi, Alfredo Juárez-Saldivar, Olatomide A Fadare, Charles O Adetunji, Gildardo Rivera

Open access · goldAbstract read
In one paragraph

Article in Phytomedicine plus : international journal of phytotherapy and phytopharmacology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed, 1 pooled it
4.4field-weighted citation impact, top 6% 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

5 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Biological properties ofF1000Research · 2024
    Pooled it
  2. Article
  3. Review
  4. Anti-angiogenic Potential of Trans-chalcone in anCardiovascular & hematological agents in medicinal chemistry · 2024
    Article
  5. 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 4 institutions in 2 countries.

Omotayo O OyedaraDepartment of Microbiology, Osun State University, Osogbo, Nigeria.
Joseph M AgbedahunsiDrug Research and Production Unit, Faculty of Pharmacy, Obafemi Awolowo University, Ile-Ife, Osun State, 220005, Nigeria.
Folasade M AdeyemiDepartment of Microbiology, Osun State University, Osogbo, Nigeria.
Alfredo Juárez-SaldivarLaboratorio de Biotecnología Farmacéutica, Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Reynosa, 88710, México.
Olatomide A FadareDepartment of Chemistry, Obafemi Awolowo University, Ile-Ife.
Charles O AdetunjiApplied Microbiology, Biotechnology and Nanotechnology Laboratory, Department of Microbiology, Edo State University, Uzairue, Edo State, Nigeria.
Gildardo RiveraLaboratorio de Biotecnología Farmacéutica, Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Reynosa, 88710, México.
Instituto Politécnico Nacional · MXObafemi Awolowo University · NGOsun State University · NGAmbrose Alli University · NG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: SARS-CoV-2 infection or COVID-19 is a major global public health issue that requires urgent attention in terms of drug development. Transmembrane Protease Serine 2 (TMPRSS2) is a good drug target against SARS-CoV-2 because of the role it plays during the viral entry into the cell. Virtual screening of phytochemicals as potential inhibitors of TMPRSS2 can lead to the discovery of drug candidates for the treatment of COVID-19. Purpose: The study was designed to screen 132 phytochemicals from three medicinal plants traditionally used as antivirals; Methods: Homology model of TMPRSS2 was built using the ProMod3 3.1.1 program of the SWISS-MODEL. Binding affinities and interaction between compounds and TMPRSS2 model was examined using molecular docking and molecular dynamics simulation. The drug-likeness and ADMET (absorption, distribution, metabolism, excretion, and toxicity) properties of potential inhibitors of TMPRSS2 were also assessed using admetSAR web tool. Results: Three compounds, namely, niazirin, quercetin, and moringyne from Conclusion: This study demonstrated the potentials of niazirin, quercetin, and moringyne from

Indexed as

ADMETADMET, Absorption, distribution, metabolism, excretion and toxicityBBB, Blood brain barrierCASTp, Computed atlas of surface topography of proteinsCOVID-19, Coronavirus Disease 2019GMQE, Global quality estimation scoreHIA, Human intestinal absorptionHOB, Human oral bioavailabilityLD50, Lethal dose 50Molecular dockingM. oleiferaPhytochemicalQMEAN, Qualitative Model Energy AnalysisRMSD, Root-mean-square deviationSARS-CoV-2SARS-CoV-2, Severe Acute Respiratory Syndrome Coronavirus 2TMPRSS2TMPRSS2, Transmembrane Protease Serine 2

Identifiers

PMID35403085
PMCPMC8479425
OpenAlexW3204363607

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.