ArticleNature communications2023
Discovery and structural characterization of monkeypox virus methyltransferase VP39 inhibitors reveal similarities to SARS-CoV-2 nsp14 methyltransferase.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- An integrated review of monkeypox: from pathogen and epidemiology to diagnostics, control, and challenges.Emerging microbes & infections · 2026Review
- Exploring drug repurposing for monkeypox virus: A structural and computational approach.Journal of Taibah University Medical Sciences · 2026Article
- Therapeutic Innovations for Monkeypox Inhibition.International journal of molecular sciences · 2026Review
- Article
- Natural compounds of medicinal plants as a source for novel anti-orthopoxvirus medications.Life medicine · 2026Article
- Structural and computational analysis of monkeypox virus methyltransferase: dynamic inhibition mechanisms and their implications for antiviral design.Molecular diversity · 2026Article
- Monkeypox Virus Countermeasures: Vaccines, Antibodies, Drugs and Traditional Chinese Medicine.Drug design, development and therapy · 2026Review
- Stability-Driven Pose Prediction and Ligand Design via Contact Persistence Analysis from Molecular Dynamics Simulations.Computational and structural biotechnology journal · 2026Article
- Design and Synthesis of Pyrazoline Inhibitors of SARS-CoV‑2 NSP14.ACS medicinal chemistry letters · 2025Article
- Inhibition of monkeypox polymerase holoenzyme and methyltransferase using bioactive compounds of black tea: a computational approach.Scientific reports · 2025Article
- Mpox: disease manifestations and therapeutic development.Journal of virology · 2025Review
- Targeting Monkeypox Virus Methyltransferase: Virtual Screening of Natural Compounds from Middle-Eastern Medicinal Plants.Molecular biotechnology · 2025Article
- Sinefungin analogs targeting VP39 methyltransferase as potential anti-monkeypox therapeutics: a multi-step computational approach.Molecular diversity · 2025Article
- Global Trends in MPOX Research (2014-2025): A Bibliometric Analysis and Overview.Veterinary medicine (Auckland, N.Z.) · 2025Review
- From phytomedicine to conventional drug research, to look for new drug molecule against monkey pox virus; a molecular docking, virtual screening and ADME analysis.In silico pharmacology · 2025Article
- Therapeutic potential ofIn silico pharmacology · 2025Article
- Meeting report of the 37th International Conference on Antiviral Research in Gold Coast, Australia, May 20-24, 2024, organized by the International Society for Antiviral Research.Antiviral research · 2024Article
- Structure of SARS-CoV-2 MTase nsp14 with the inhibitor STM957 reveals inhibition mechanism that is shared with a poxviral MTase VP39.Journal of structural biology: X · 2024Article
- Evaluating the Binding Potential and Stability of Drug-like Compounds with the Monkeypox Virus VP39 Protein Using Molecular Dynamics Simulations and Free Energy Analysis.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Computational analysis of pathogen-host interactome for fast and low-risk in-silico drug repurposing in emerging viral threats like Mpox.Scientific reports · 2024Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monkeypox is a disease with pandemic potential. It is caused by the monkeypox virus (MPXV), a double-stranded DNA virus from the Poxviridae family, that replicates in the cytoplasm and must encode for its own RNA processing machinery including the capping machinery. Here, we present crystal structures of its 2'-O-RNA methyltransferase (MTase) VP39 in complex with the pan-MTase inhibitor sinefungin and a series of inhibitors that were discovered based on it. A comparison of this 2'-O-RNA MTase with enzymes from unrelated single-stranded RNA viruses (SARS-CoV-2 and Zika) reveals a conserved sinefungin binding mode, implicating that a single inhibitor could be used against unrelated viral families. Indeed, several of our inhibitors such as TO507 also inhibit the coronaviral nsp14 MTase.
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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.