ArticleNature chemical biology2025
Mechanisms of neutralization of toxSAS from toxin-antitoxin modules.
Article in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genomic profiling ofMicrobiology spectrum · 2026Article
- Nanobody-mediated control of long RSH Rel and RelA catalysis by restriction of their conformational landscape.Nature communications · 2026Article
- Dual regulation of HEPN RNase in fused MNT-HEPN toxin-antitoxin systems via protein OligoAMPylation and oligomerization.Nucleic acids research · 2026Article
- Comparative study of adenosine 3'-pyrophosphokinase domains of MuF polymorphic toxins.FEBS open bio · 2025Article
- Putting bacteria in alarm.Nature chemical biology · 2025Article
- Toxic small alarmone synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAScience advances · 2024Article
- Article
- Toxic Small Alarmone Synthetase FaRel2 inhibits translation by pyrophosphorylating tRNAbioRxiv : the preprint server for biology · 2024Article
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Authors and funding
9 authors.
Funding
Abstract
Toxic small alarmone synthetase (toxSAS) enzymes constitute a family of bacterial effectors present in toxin-antitoxin and secretion systems. toxSASs act through either translation inhibition mediated by pyrophosphorylation of transfer RNA (tRNA) CCA ends or synthesis of the toxic alarmone adenosine pentaphosphate ((pp)pApp) and adenosine triphosphate (ATP) depletion, exemplified by FaRel2 and FaRel, respectively. However, structural bases of toxSAS neutralization are missing. Here we show that the pseudo-Zn
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