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1 lyzes the conversion of reduced vitamin K to vitamin K epoxide and the concomitant conversion of glut
2 ants resulted in wild type VKOR reduction of vitamin K epoxide; however, the C43A and C51A mutants on
3 reductase complex subunit 1 (VKORC1) reduces vitamin K epoxide in the vitamin K cycle for post-transl
8 arfarin and other 4-hydroxycoumarins inhibit vitamin K epoxide reductase (VKOR) by depleting reduced
10 oralis, and revealed the essential role of a vitamin K epoxide reductase (VKOR) gene in pilus assembl
12 isms in the cytochrome P450 2C9 (CYP2C9) and vitamin K epoxide reductase (VKOR) genes have been shown
20 Despite its importance, warfarin's target, vitamin K epoxide reductase (VKOR), has resisted purific
21 agulation in humans requires the activity of vitamin K epoxide reductase (VKOR), the target of the an
22 K is in excess in both the untransfected and vitamin K epoxide reductase (VKOR)-transfected cells, th
27 d of a key pharmacologic target of warfarin, vitamin K epoxide reductase (VKORC1), contribute to diff
28 logous to the catalytic subunit of mammalian vitamin K epoxide reductase (VKORC1, EC 1.1.4.1) that is
29 n dosing is correlated with polymorphisms in vitamin K epoxide reductase complex 1 (VKORC1) and the c
32 on its interaction with a splice variant of vitamin K epoxide reductase complex subunit 1 (VKORC1),
33 mented but uncharacterized splice variant of vitamin K epoxide reductase complex subunit 1 (VKORC1),
34 ctions of vIL-6 with the ER membrane protein vitamin K epoxide reductase complex subunit 1 variant 2
35 eviously uncharacterized ER membrane protein vitamin K epoxide reductase complex subunit 1 variant 2
36 ociates with a novel membrane protein termed vitamin K epoxide reductase complex subunit 1 variant 2
37 largely uncharacterized ER-resident protein vitamin K epoxide reductase complex subunit 1 variant 2
38 ide polymorphisms in cytochrome P450 2C9 and vitamin K epoxide reductase have been shown to make sign
39 on (Ci-Gla1, gamma-glutamyl carboxylase, and vitamin K epoxide reductase) or spatiotemporal regulatio
40 mplicate the bacterial homolog of the enzyme vitamin K epoxide reductase, a protein required for bloo
41 macromolecular interactions by inhibition of vitamin K epoxide reductase, cellular responses includin
46 VKOR) sustains blood coagulation by reducing vitamin K epoxide to the hydroquinone, an essential cofa
47 tif are essential for both the conversion of vitamin K epoxide to vitamin K and the conversion of vit
48 is that VKOR catalyzes both the reduction of vitamin K epoxide to vitamin K and the conversion of vit
49 eptide can accomplish both the conversion of vitamin K epoxide to vitamin K and vitamin K to reduced
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