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UnknownStructural features determining the vitamin K epoxide reduction activity in the VKOR family of membrane oxidoreductases.
Not available
S-EPMC9346089 | biostudies-literature
UnknownHuman vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1) mediates vitamin K-dependent intracellular antioxidant function.
Not available
S-EPMC3083210 | biostudies-literature
OtherMultiplexed measurement of variant abundance and activity reveals VKOR topology, active site and human variant impact
Vitamin K epoxide reductase (VKOR) drives the vitamin K cycle, activating vitamin K-dependent blood clotting factors. VKOR is also the target of the widely used anticoagulant drug, warfarin. Despite VKOR’s pivotal role in coagulation, its structure and active site remain poorly understood. Here, we ...
ORGANISM(S): Homo sapiens synthetic construct 
2020-08-10 | GSE149922 | GEO
UnknownPhylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family.
Not available
S-EPMC4555120 | biostudies-literature
UnknownStructure of a bacterial homologue of vitamin K epoxide reductase.
Not available
S-EPMC2919313 | biostudies-literature
ProteomicsIn-cell isotope-coded labeling and LC-MS/MS analysis probe warfarin inhibition mechanism
Warfarin targets human vitamin K epoxide reductase (hVKOR), a redox enzyme in the membrane of endoplasmic reticulum (ER), to prevent the formation of blood clots. Although warfarin has been a popular medication since 1954, its mechanism of action is still unclear. A fundamental issue is the controve...
ORGANISM(S): Homo sapiens (Human) 
2017-03-30 | PXD003774 | Pride
Human vitamin k epoxide reuctase N-ethylmeleimide Isotope Bottom-up proteomics Warfarin 
UnknownWarfarin and vitamin K epoxide reductase: a molecular accounting for observed inhibition.
Not available
S-EPMC6085993 | biostudies-literature
UnknownA hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.
Not available
S-EPMC3108363 | biostudies-literature
UnknownVitamin K epoxide reductase and its paralogous enzyme have different structures and functions.
Not available
S-EPMC5732223 | biostudies-literature
UnknownA novel vitamin K derived anticoagulant tolerant to genetic variations of vitamin K epoxide reductase.
Not available
S-EPMC7925372 | biostudies-literature
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