ArticleStructure (London, England : 1993)2024
Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin.
Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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7 citing papers in PubMed, 10 citations in OpenAlex.
- Molecular strategies ofFrontiers in cellular and infection microbiology · 2026Review
- Salmonella enterica persister cells exhibit distinct susceptibility profiles following exposure to human serum and macrophages.PloS one · 2026Article
- Actin isoform-specific interactions revealed byProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Effects of Bile on PathogenicBiomolecules · 2025Article
- The interplay betweenCell insight · 2025Review
- Antagonistic Effects of Actin-Specific Toxins onBiomolecules · 2024Article
- Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024Article
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5 authors at 2 institutions in 1 country.
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Abstract
Entry of Salmonella into host enterocytes relies on its pathogenicity island 1 effector SipA. We found that SipA binds to F-actin in a 1:2 stoichiometry with sub-nanomolar affinity. A cryo-EM reconstruction revealed that SipA's globular core binds at the groove between actin strands, whereas the extended C-terminal arm penetrates deeply into the inter-strand space, stabilizing F-actin from within. The unusually strong binding of SipA is achieved by a combination of fast association via the core and very slow dissociation dictated by the arm. Similar to P
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