Evidence map›Paper›PMID 34516563›Full record

ArticlePLoS computational biology2021

Characterization of the NiRAN domain from RNA-dependent RNA polymerase provides insights into a potential therapeutic target against SARS-CoV-2.

Abhisek Dwivedy, Richard Mariadasse, Mohammed Ahmad, Sayan Chakraborty, Deepsikha Kar, Satish Tiwari, Sankar Bhattacharyya, Sudipta Sonar, Shailendra Mani, Prafullakumar Tailor and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

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  13. Chemical physics letters · 2021
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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

13 authors at 3 institutions in 1 country.

Abhisek DwivedyNational Institute of Immunology, New Delhi, India.ORCID 0000-0001-9745-8138
Richard MariadasseDepartment of Bioinformatics, Alagappa University, Tamil Nadu, India.ORCID 0000-0002-3041-6993
Mohammed AhmadNational Institute of Immunology, New Delhi, India.
Sayan ChakrabortyNational Institute of Immunology, New Delhi, India.
Deepsikha KarNational Institute of Immunology, New Delhi, India.ORCID 0000-0003-4692-4682
Satish TiwariNational Institute of Immunology, New Delhi, India.
Sankar BhattacharyyaTranslational Health Science and Technology Institute, Faridabad, India.ORCID 0000-0002-9087-8460
Sudipta SonarTranslational Health Science and Technology Institute, Faridabad, India.
Shailendra ManiTranslational Health Science and Technology Institute, Faridabad, India.ORCID 0000-0001-8541-8315
Prafullakumar TailorNational Institute of Immunology, New Delhi, India.
Tanmay MajumdarNational Institute of Immunology, New Delhi, India.ORCID 0000-0003-1087-8493
Jeyaraman JeyakanthanDepartment of Bioinformatics, Alagappa University, Tamil Nadu, India.ORCID 0000-0003-2822-7592
Bichitra Kumar BiswalNational Institute of Immunology, New Delhi, India.ORCID 0000-0002-5927-3244
National Institute of Immunology · INTranslational Health Science and Technology Institute · INAlagappa University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apart from the canonical fingers, palm and thumb domains, the RNA dependent RNA polymerases (RdRp) from the viral order Nidovirales possess two additional domains. Of these, the function of the Nidovirus RdRp associated nucleotidyl transferase domain (NiRAN) remains unanswered. The elucidation of the 3D structure of RdRp from the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2), provided the first ever insights into the domain organisation and possible functional characteristics of the NiRAN domain. Using in silico tools, we predict that the NiRAN domain assumes a kinase or phosphotransferase like fold and binds nucleoside triphosphates at its proposed active site. Additionally, using molecular docking we have predicted the binding of three widely used kinase inhibitors and five well characterized anti-microbial compounds at the NiRAN domain active site along with their drug-likeliness. For the first time ever, using basic biochemical tools, this study shows the presence of a kinase like activity exhibited by the SARS-CoV-2 RdRp. Interestingly, a well-known kinase inhibitor- Sorafenib showed a significant inhibition and dampened viral load in SARS-CoV-2 infected cells. In line with the current global COVID-19 pandemic urgency and the emergence of newer strains with significantly higher infectivity, this study provides a new anti-SARS-CoV-2 drug target and potential lead compounds for drug repurposing against SARS-CoV-2.

Indexed as

Protein DomainsAntiviral AgentsCatalytic DomainComputer SimulationCoronavirus RNA-Dependent RNA PolymeraseHumansSARS-CoV-2Antiviral AgentsCoronavirus RNA-Dependent RNA Polymerase

Identifiers

PMID34516563
PMCPMC8478224
OpenAlexW3201399648

What Socratic 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 Socratic graph.