ArticleFEBS letters2021
Interface-based design of the favipiravir-binding site in SARS-CoV-2 RNA-dependent RNA polymerase reveals mutations conferring resistance to chain termination.
Article in FEBS letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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.
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.
Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- SARS-CoV-2 drug resistance and therapeutic approaches.Heliyon · 2025Review
- Unfurling the Potential of Antiviral Agents Aimed for RNA Virus Ailment.Current drug targets · 2025Review
- SARS-CoV-2 Resistance to Small Molecule Inhibitors.Current clinical microbiology reports · 2024Article
- Review
- Activation of the urotensin-II receptor by remdesivir induces cardiomyocyte dysfunction.Communications biology · 2023Article
- Computational Protein Design for COVID-19 Research and Emerging Therapeutics.ACS central science · 2023Review
- Oral antiviral treatments for COVID-19: opportunities and challenges.Pharmacological reports : PR · 2022Review
- Hotspot residues and resistance mutations in the nirmatrelvir-binding site of SARS-CoV-2 main protease: Design, identification, and correlation with globally circulating viral genomes.Biochemical and biophysical research communications · 2022Article
- An integrated understanding of the evolutionary and structural features of the SARS-CoV-2 spike receptor binding domain (RBD).International journal of biological macromolecules · 2022Article
- African derived phytocompounds may interfere with SARS-CoV-2 RNA capping machinery via inhibition of 2'-O-ribose methyltransferase: AnJournal of molecular structure · 2022Article
- Lethal Mutagenesis of RNA Viruses and Approved Drugs with Antiviral Mutagenic Activity.Viruses · 2022Review
- Identification of broad anti-coronavirus chemical agents for repurposing against SARS-CoV-2 and variants of concern.Current research in virological science · 2022Article
- Emergence of unique SARS-CoV-2 ORF10 variants and their impact on protein structure and function.International journal of biological macromolecules · 2022Article
- Two years into COVID-19 - Lessons in SARS-CoV-2 and a perspective from papers in FEBS Letters.FEBS letters · 2021Review
- Genomic Variations in the Structural Proteins of SARS-CoV-2 and Their Deleterious Impact on Pathogenesis: A Comparative Genomics Approach.Frontiers in cellular and infection microbiology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Favipiravir is a broad-spectrum inhibitor of viral RNA-dependent RNA polymerase (RdRp) currently being used to manage COVID-19. Accumulation of mutations in severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) RdRp may facilitate antigenic drift, generating favipiravir resistance. Focussing on the chain-termination mechanism utilized by favipiravir, we used high-throughput interface-based protein design to generate > 100 000 designs of the favipiravir-binding site of RdRp and identify mutational hotspots. We identified several single-point mutants and designs having a sequence identity of 97%-98% with wild-type RdRp, suggesting that SARS-CoV-2 can develop favipiravir resistance with few mutations. Out of 134 mutations documented in the CoV-GLUE database, 63 specific mutations were already predicted as resistant in our calculations, thus attaining ˜ 47% correlation with the sequencing data. These findings improve our understanding of the potential signatures of adaptation in SARS-CoV-2 against favipiravir.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.