| Name | vitamin K epoxide reductase |
|---|---|
| Synonyms | Vitamin K epoxide reductase; IMAGE3455200; MST134; MST576; MSTP134; MSTP576; Phylloquinone epoxide reductase; UNQ308… |
| Name | brodifacoum |
|---|---|
| CAS |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 6487353 | Hart JA, Haynes BP, Park BK: A study of factors which determine the pharmacological response to in anticoagulated rabbits. Biochem Pharmacol. 1984 Oct 1;33(19):3013-9. The pharmacological response to has been determined by measuring prothrombin complex activity (P.C.A.) in male New Zealand White rabbits anticoagulated (P.C.A. less than 20%) with the long acting brodifacoum, at a dose (10 mg/kg) which produces maximum antagonism of vitamin K1. Thus, according to current concepts, this animal model may be used to assess requirements in the absence of a functional vitamin K-epoxide reductase. |
1(0,0,0,1) | Details |
| 17275317 | Gebauer M: Synthesis and structure-activity relationships of novel derivatives. Bioorg Med Chem. 2007 Mar 15;15(6):2414-20. Epub 2007 Jan 17. Yet little detail is known about the molecular interactions between 4-hydroxycoumarins with vitamin K epoxide reductase (VKER), inhibition of which produces a deficiency of vitamin K and consequently a deficiency of vitamin K-dependent proteins involved in thrombus formation. Ferulenol 19 confers approximately 22 times more potent inhibition than and is approximately 1.5 more potent than the rodenticide brodifacoum in this in vitro assay. |
1(0,0,0,1) | Details |
| 3978316 | Breckenridge AM, Cholerton S, Hart JA, Park BK, Scott AK: A study of the relationship between the pharmacokinetics and the pharmacodynamics of the anticoagulants difenacoum and brodifacoum in the rabbit. Br J Pharmacol. 1985 Jan;84(1):81-91. |
0(0,0,0,0) | Details |
| 19569076 | Cort JR, Cho H: (1) H and (13) C NMR chemical shift assignments and conformational analysis for the two diastereomers of the vitamin K epoxide reductase inhibitor brodifacoum. Magn Reson Chem. 2009 Oct;47(10):897-901. These assignments and conformational analyses may be useful in studies of biomolecular interactions of brodifacoum with target proteins such as VKOR and in source determination of brodifacoum. |
143(1,3,3,3) | Details |
| 11898799 | Eason CT, Murphy EC, Wright GR, Spurr EB: Assessment of risks of brodifacoum to non-target birds and mammals in New Zealand. Ecotoxicology. 2002 Feb;11(1):35-48. Like other second-generation anticoagulants brodifacoum is strongly bound to vitamin K epoxide reductase and will persist, apparently for at least 6 months, in organs and tissue containing this enzyme, e.g., liver, kidney, and pancreas. |
81(1,1,1,1) | Details |
| 3395132 | Trivedi LS, Rhee M, Galivan JH, Fasco MJ: Normal and -resistant rat hepatocyte metabolism of evidence for multiple pathways of hydroxyvitamin K formation. Arch Biochem Biophys. 1988 Jul;264(1):67-73. Addition of the vitamin K 2,3-epoxide reductase inhibitors (5 to 100 microM) and brodifacoum (1 to 5 microM) to normal rat hepatocyte cultures produced a slight increase in hydroxyvitamin K formation and a marked inhibition of formation. |
32(0,1,1,2) | Details |