{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mortel SLR"],"funding":["NHLBI NIH HHS"],"pagination":["26694-26704"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12224098"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(25)"],"pubmed_abstract":["Vitamin K epoxide reductase (VKOR) is an enzyme involved in the activation of several clotting factors, making its inhibition a well-known mechanism of anticoagulant action. Though the VKOR inhibitor warfarin remains essential and popular today, its adverse effects still make it a high-risk drug. This study intends to identify novel compounds with predicted VKOR inhibition and pharmacokinetic stability and explain the mechanistic basis of their action. A combination of pharmacophore modeling, druglikeness prediction, and molecular docking was used to find hits from existing compound libraries. The top hits showed <i>in vitro</i> activity at the micromolar level in a cell-based VKOR inhibition assay using human embryonic kidney 293 cells, led by A114 (IC<sub>50</sub> = 5.51 μM) and A116 (IC"],"journal":["ACS omega"],"pubmed_title":["&lt;i&gt;In Silico&lt;/i&gt; and &lt;i&gt;In Vitro&lt;/i&gt; Studies of Potential Novel Vitamin K Epoxide Reductase (VKOR) Inhibitors Suggest an Updated Structure-Activity Relationship."],"pmcid":["PMC12224098"],"funding_grant_id":["R01 HL131690"],"pubmed_authors":["Wang M","Mortel SLR","Macalino SJY","Tie JK"],"additional_accession":[]},"is_claimable":false,"name":"&lt;i&gt;In Silico&lt;/i&gt; and &lt;i&gt;In Vitro&lt;/i&gt; Studies of Potential Novel Vitamin K Epoxide Reductase (VKOR) Inhibitors Suggest an Updated Structure-Activity Relationship.","description":"Vitamin K epoxide reductase (VKOR) is an enzyme involved in the activation of several clotting factors, making its inhibition a well-known mechanism of anticoagulant action. Though the VKOR inhibitor warfarin remains essential and popular today, its adverse effects still make it a high-risk drug. This study intends to identify novel compounds with predicted VKOR inhibition and pharmacokinetic stability and explain the mechanistic basis of their action. A combination of pharmacophore modeling, druglikeness prediction, and molecular docking was used to find hits from existing compound libraries. The top hits showed <i>in vitro</i> activity at the micromolar level in a cell-based VKOR inhibition assay using human embryonic kidney 293 cells, led by A114 (IC<sub>50</sub> = 5.51 μM) and A116 (IC","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jul","modification":"2026-06-02T08:44:51.162Z","creation":"2026-04-16T03:12:49.797Z"},"accession":"S-EPMC12224098","cross_references":{"pubmed":["40621007"],"doi":["10.1021/acsomega.5c01116"]}}