Evidence map›Paper›PMID 40977902›Full record

ArticleComputational and structural biotechnology journal2025

Repurposing of the nucleoside analogs for influenza.

Pitchayathida Mee-Udorn, Jaraspim Narkpuk, Peera Jaru-Ampornpan, Suradej Hongeng, Tanaporn Uengwetwanit, Nitipol Srimongkolpithak

Abstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. The Redesign of the Molecular Scaffold of Viral Ion Channel Blockers.Computational and structural biotechnology journal · 2026
    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

6 authors.

Pitchayathida Mee-UdornNational Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 111 Thailand Science Park, Phahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani 12120, Thailand.
Jaraspim NarkpukNational Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 111 Thailand Science Park, Phahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani 12120, Thailand.
Peera Jaru-AmpornpanNational Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 111 Thailand Science Park, Phahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani 12120, Thailand.
Suradej HongengExcellence Center for Drug Discovery (ECDD), Faculty of Science, Mahidol University, 272 Rama 6 Road, Phayathai, Rachathewi, Bangkok 10400, Thailand.
Tanaporn UengwetwanitNational Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 111 Thailand Science Park, Phahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani 12120, Thailand.
Nitipol SrimongkolpithakNational Center for Genetic Engineering and Biotechnology (BIOTEC), National Science and Technology Development Agency (NSTDA), 111 Thailand Science Park, Phahonyothin Road, Khlong Nueng, Khlong Luang, Pathum Thani 12120, Thailand.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Influenza viruses remain a global health concern prompting the search for new antivirals. Drug repurposing offers an efficient approach to identify potential therapeutics. This study repurposed 35 FDA-approved nucleoside analogs, screening them against influenza H1N1. Seven compounds exhibited significant antiviral activity, with cytidine analogs Gemcitabine (IC₅₀ = 0.64 ± 0.21 µM) and 5-Azacytidine (IC₅₀ = 3.42 ± 0.38 µM) showing the strongest inhibition. Molecular dynamics simulations showed that key binding site residues (Arg45, Lys229, Arg239, Lys308, Lys480) and a magnesium ion are crucial for drug binding. Stable hydrogen bonds between active analogs and specific residues (Arg239, Thr307, Asn310), along with significant interactions with RNA complementary bases, are associated with antiviral activity. These findings offer structural insights into polymerase inhibition and provide a foundation for future drug design and monitoring of resistance development.

Indexed as

Antiviral assayFDA-approved drugInfluenza virusMolecular dynamics simulationsNucleosideRNA-dependent RNA polymerase

Identifiers

PMID40977902
PMCPMC12447893

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Registered trials

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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.