ArticleACS pharmacology & translational science2025
The Discovery of a Novel Anticoagulant Mechanism: Factor XI Activation Inhibitors.
Article in ACS pharmacology & translational science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
20 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite advances in anticoagulant drug discovery to establish a new standard of care, represented by Factor Xa (FXa) inhibitors, additional therapies are needed to address the concomitant bleeding risk posed by these agents. Factor XI (FXI) plays a key role in the intrinsic coagulation cascade contributing to thrombin generation and fibril formation, and there is an increasing weight of evidence supporting a comparable efficacy and superior safety profile of FXI-based oral anticoagulants. A novel allosteric mechanism of action (MoA) for inhibiting FXI activation to Factor XIa (FXIa) was discovered by applying an AS-MS-based screen to the FXI zymogen. Biochemical and biophysical characterization of these structurally diverse small-molecule classes confirmed this mode of inhibition as specific to the FXI zymogen, and a high-resolution FXI-inhibitor cocomplex structure identified the binding pocket that is distal to the FXI cleavage site. These FXI Activation Inhibitors were active in translational functional assays, prolonging activated partial thromboplastin time (aPTT) in human plasma and demonstrating dose-dependent antithrombotic effects in the rabbit arteriovenous-shunt model of thrombosis. The results affirm that FXI Activation Inhibitors are a novel mechanism for the potential treatment of thrombotic disorders.
Indexed as
Identifiers
What OpenQuestion holds
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.