ArticleACS omega2024
New Triazole-Based Potent Inhibitors of Human Factor XIIa as Anticoagulants.
Article in ACS omega, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed.
- Development of an Interpretable QSAR Model for Predicting Coagulation Factor XIIa Inhibitors Using Ensemble Machine Learning.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Developing Safer Anticoagulant Candidates: Structure-Activity Relationship Studies of 5-Amino-Triazole-Based FXIIa Inhibitors.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2026Article
- Advancements in research on the thrombo-inflammation mechanisms mediated by factor XII in ischemic stroke.Journal of thrombosis and thrombolysis · 2025Review
- BIOCHEMICAL INVESTIGATION OF THE ANTICOAGULANT ACTIVITY OF SULFONATED POLYMERS.Journal of undergraduate chemistry research · 2025Article
- Discovery of a new lead molecule to develop a novel class of human factor XIIa inhibitors.Journal of thrombosis and thrombolysis · 2024Article
- Discovery of Heparin Mimetic, Potent, and Selective Inhibitors of Human Clotting Factor XIIIa.ACS omega · 2024Article
- Discovery of New Inhibitors of Human Activated Protein C to Treat Hemophilia.Letters in drug design & discovery · 2024Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Factor XIIa (FXIIa) functions as a plasma serine protease within the contact activation pathway. Various animal models have indicated a substantial role for FXIIa in thromboembolic diseases. Interestingly, individuals and animals with FXII deficiency seem to maintain normal hemostasis. Consequently, inhibiting FXIIa could potentially offer a viable therapeutic approach for achieving effective and safer anticoagulation without the bleeding risks associated with the existing anticoagulants. Despite the potential, only a limited number of small molecule inhibitors targeting human FXIIa have been documented. Thus, we combined a small library of 32 triazole and triazole-like molecules to be evaluated for FXIIa inhibition by using a chromogenic substrate hydrolysis assay under physiological conditions. Initial screening at 200 μM involved 18 small molecules, revealing that 4 molecules inhibited FXIIa more than 20%. In addition to being the most potent inhibitor identified in the first round, inhibitor
Identifiers
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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.