Evidence map›Paper›PMID 36376718›Full record

ArticleMolecular diversity2023

Insight into the Hantaan virus RNA-dependent RNA polymerase inhibition using in-silico approaches.

Shah Faisal, Syed Lal Badshah, Mohamed Sharaf, Mohnad Abdalla

Open access · bronzeAbstract read
In one paragraph

Article in Molecular diversity, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 39% 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, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Pharmacophores of Influenza Virus PA Endonuclease Inhibitors.Advances in experimental medicine and biology · 2026
    Review
  4. 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

4 authors at 3 institutions in 3 countries.

Shah FaisalDepartment of Chemistry, Islamia College University Peshawar, Peshawar, 25120, Pakistan.
Syed Lal BadshahDepartment of Chemistry, Islamia College University Peshawar, Peshawar, 25120, Pakistan. shahbiochemist@gmail.com.ORCID http://orcid.org/0000-0002-0229-1425
Mohamed SharafDepartment of Biochemistry, Faculty of Agriculture, AL-Azhar University, Nasr City, Cairo, 11751, Egypt.
Mohnad AbdallaPediatric Research Institute, Children's Hospital Affiliated to Shandong University, Jinan, 250022, China. mohnadabdalla200@gmail.com.
Islamia College University · PKAl-Azhar University · EGShandong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Hantaan virus (HTN) is a member of the hantaviridae family. It is a segmented type, negative-strand virus (sNSVs). It causes hemorrhagic fever with renal syndrome, which includes fever, vascular hemorrhage, and renal failure. This illness is one of the most serious hemorrhagic diseases in the world, and it is a major public health concern due to its high mortality rate. The Hantaan virus RNA-dependent RNA polymerase complex (RdRp) is involved in viral RNA transcription and replication for the survival and transmission of this virus. Therefore, it is a primary target for antiviral drug development. Interference with the endonucleolytic "cap-snatching" reaction by the HTN virus RdRp endonuclease domain is a particularly appealing approach for drug discovery against this virus. This RdRp endonuclease domain of the HTN virus has a metal-dependent catalytic activity. We targeted this metal-dependent enzymatic activity to identify inhibitors that can bind and disrupt this endonuclease enzyme activity using in-silico approaches i.e., molecular docking, molecular dynamics simulation, predicted absorption, distribution, metabolism, excretion, toxicity (ADMET) and drug-likeness studies. The docking studies showed that peramivir, and ingavirin compounds can effectively bind with the manganese ions and engage with other active site residues of this protein. Molecular simulations also showed stable binding of these ligands with the active site of HTN RdRp. Simulation analysis showed that they were in constant contact with the active site manganese ions and amino acid residues of the HTN virus endonuclease domain. This study will help in better understanding the HTN and related viruses.

Indexed as

Hantaan virusRNA-Dependent RNA PolymeraseEndonucleasesIonsManganeseMolecular Docking SimulationRNA, ViralEndonucleasesIonsManganeseRNA-Dependent RNA PolymeraseRNA, ViralEnzyme inhibitionHemorrhagic feverMolecular dockingPeramivirRNA polymerase

Identifiers

PMID36376718
PMCPMC9663193
OpenAlexW4308950134

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.