ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structural basis for Lamassu-based antiviral immunity and its evolution from DNA repair machinery.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Gabija restricts phage circularization and DNA replication.Cell host & microbe · 2026Article
- Shuttling, swapping, and mixing: the rapid modular evolution of antiviral repertoires in temperate phages and their satellites.Nucleic acids research · 2026Article
- Review
- Structural insights into type-I and type-II Lamassu antiphage systems.Nature chemical biology · 2026Article
- Structural insights into the assembly and function of Retron Ec78 PtuAB.Communications biology · 2026Article
- Evolution of pandemic cholera at its global source.Nature · 2026Article
- Article
- It's not me, it's you: Anti-phage nuclease specificity inside a bacterium.PLoS pathogens · 2026Article
- Recurrent acquisition of nuclease-protease pairs in antiviral immunity.Science (New York, N.Y.) · 2026Article
- Defence systems encoded by core genomic islands of seventh pandemicPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
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Abstract
Bacterial immune systems exhibit remarkable diversity and modularity, as a consequence of the continuous selective pressures imposed by phage predation. Despite recent mechanistic advances, the evolutionary origins of many antiphage immune systems remain elusive, especially for those that encode homologs of the structural maintenance of chromosomes (SMC) superfamily, which are essential for chromosome maintenance and DNA repair across domains of life. Here, we elucidate the structural basis and evolutionary emergence of Lamassu, a bacterial immune system family featuring diverse effectors but a core conserved SMC-like sensor. Using cryo-EM, we determined structures of the
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