ArticleScientific reports2016
Characterization of the Annonaceous acetogenin, annonacinone, a natural product inhibitor of plasminogen activator inhibitor-1.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.
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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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Who cites it
5 citing papers in PubMed, 1 synthesis or guideline pooled it, 12 citations in OpenAlex.
- Risk factors for mild cognitive impairment in Parkinson disease: a systematic review and meta-analysis.Molecular and cellular biochemistry · 2026Pooled it
- Review
- Motor deficit in the mouse ferric chloride-induced distal middle cerebral artery occlusion model of stroke.Behavioural brain research · 2020Article
- Serpins in Hemostasis as Therapeutic Targets for Bleeding or Thrombotic Disorders.Frontiers in cardiovascular medicine · 2020Review
- Dual-reporter high-throughput screen for small-moleculeThe Journal of biological chemistry · 2019Article
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Authors and funding
16 authors at 6 institutions in 2 countries.
Funding
Abstract
Plasminogen activator inhibitor-1 (PAI-1) is the main inhibitor of the tissue type and urokinase type plasminogen activators. High levels of PAI-1 are correlated with an increased risk of thrombotic events and several other pathologies. Despite several compounds with in vitro activity being developed, none of them are currently in clinical use. In this study, we evaluated a novel PAI-1 inhibitor, annonacinone, a natural product from the Annonaceous acetogenins group. Annonacinone was identified in a chromogenic screening assay and was more potent than tiplaxtinin. Annonacinone showed high potency ex vivo on thromboelastography and was able to potentiate the thrombolytic effect of tPA in vivo in a murine model. SDS-PAGE showed that annonacinone inhibited formation of PAI-1/tPA complex via enhancement of the substrate pathway. Mutagenesis and molecular dynamics allowed us to identify annonacinone binding site close to helix D and E and β-sheets 2A.
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Registered trials
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