ArticleNucleic acids research2024
Structural basis for difunctional mechanism of m-AMSA against African swine fever virus pP1192R.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Epigallocatechin gallate (EGCG) inhibits African swine fever virus replication by targeting key viral proteins and regulating host lipid metabolism.Emerging microbes & infections · 2026Article
- Identification of new ER-targeted anticancer hits active against MCF-7 breast cancer cells in the marine fungal secondary metabolite library using computative and experimental approaches.Journal of computer-aided molecular design · 2026Article
- Anticancer activity of lichen-derived compounds against triple-negative breast cancer: integrated in vitro evaluation, network pharmacology, molecular docking, and KEGG pathway analysis.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Article
- In Silico Discovery of mTOR Inhibitors as Potential Therapeutics for Feline Hypertrophic Cardiomyopathy.Journal of molecular modeling · 2026Article
- Mechanistic insights and therapeutic advances in antiviral strategies against African swine fever virus.Acta pharmaceutica Sinica. B · 2026Review
- An integrated multiscale computational study of nephrotoxicity mechanism of citrinin and its metabolites (CIMs)：density functional theory, network toxicology, and molecular dynamics simulation.Mycotoxin research · 2025Article
- Molecular modeling studies, in vitro antioxidant and antimicrobial assay and BSA affinity of novel benzyl-amine derived scaffolds as CYP51B inhibitors.Molecular diversity · 2025Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
19 authors.
Funding
Abstract
The African swine fever virus (ASFV) type II topoisomerase (Topo II), pP1192R, is the only known Topo II expressed by mammalian viruses and is essential for ASFV replication in the host cytoplasm. Herein, we report the structures of pP1192R in various enzymatic stages using both X-ray crystallography and single-particle cryo-electron microscopy. Our data structurally define the pP1192R-modulated DNA topology changes. By presenting the A2+-like metal ion at the pre-cleavage site, the pP1192R-DNA-m-AMSA complex structure provides support for the classical two-metal mechanism in Topo II-mediated DNA cleavage and a better explanation for nucleophile formation. The unique inhibitor selectivity of pP1192R and the difunctional mechanism of pP1192R inhibition by m-AMSA highlight the specificity of viral Topo II in the poison binding site. Altogether, this study provides the information applicable to the development of a pP1192R-targeting anti-ASFV strategy.
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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.