scholarly article | Q13442814 |
P356 | DOI | 10.1021/BI00293A031 |
P698 | PubMed publication ID | 6652076 |
P2093 | author name string | M J Fasco | |
P A Friedman | |||
L M Principe | |||
W A Walsh | |||
P433 | issue | 24 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | vitamin K | Q182338 |
(E)-phytonadione | Q186093 | ||
(RS)-warfarin | Q407431 | ||
P1104 | number of pages | 6 | |
P304 | page(s) | 5655-5660 | |
P577 | publication date | 1983-11-01 | |
P1433 | published in | Biochemistry | Q764876 |
P1476 | title | Warfarin inhibition of vitamin K 2,3-epoxide reductase in rat liver microsomes | |
P478 | volume | 22 |
Q73853938 | Assembly of the warfarin-sensitive vitamin K 2,3-epoxide reductase enzyme complex in the endoplasmic reticulum membrane |
Q52477325 | Is thioredoxin the physiological vitamin K epoxide reducing agent? |
Q41862955 | Microsomal lipoamide reductase provides vitamin K epoxide reductase with reducing equivalents |
Q28242581 | Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2 |
Q33364524 | New pieces to an old puzzle: identifying the warfarin-binding site that prevents clotting |
Q24304387 | Novel insight into the mechanism of the vitamin K oxidoreductase (VKOR): electron relay through Cys43 and Cys51 reduces VKOR to allow vitamin K reduction and facilitation of vitamin K-dependent protein carboxylation |
Q73788000 | Purification of warfarin-sensitive vitamin K epoxide reductase |
Q39761459 | Recent advances in hepatic vitamin K metabolism and function |
Q70407705 | Reduced thioredoxin: a possible physiological cofactor for vitamin K epoxide reductase. Further support for an active site disulfide |
Q28572936 | Species comparison of vitamin K1 2,3-epoxide reductase activity in vitro: kinetics and warfarin inhibition |
Q52582864 | Stabilization of warfarin-binding pocket of VKORC1 and VKORL1 by a peripheral region determines their different sensitivity to warfarin inhibition. |
Q26796613 | Structural Modeling Insights into Human VKORC1 Phenotypes |
Q37122098 | Structure and function of vitamin K epoxide reductase |
Q73854557 | The characterization of potent novel warfarin analogs |
Q42125855 | The long-term effects of the rodenticide, brodifacoum, on blood coagulation and vitamin K metabolism in rats |
Q28115117 | The vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylation |
Q37122109 | VKORC1: a warfarin-sensitive enzyme in vitamin K metabolism and biosynthesis of vitamin K-dependent blood coagulation factors |
Q28583201 | Vitamin K 2,3-epoxide reductase and the vitamin K-dependent gamma-carboxylation system |
Q42848521 | Vitamin K 2,3-epoxide reductase: the basis for stereoselectivity of 4-hydroxycoumarin anticoagulant activity |
Q42181768 | Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum |
Q28274354 | Vitamin K-dependent carboxylation |
Q34564856 | Vitamin K-dependent carboxylation and vitamin K metabolism in liver. Effects of warfarin |
Q51273552 | Warfarin and vitamin K compete for binding to Phe55 in human VKOR. |
Q42062867 | Warfarin poisoning and vitamin K antagonism in rat and human liver. Design of a system in vitro that mimics the situation in vivo |
Q37122112 | Warfarin therapy: influence of pharmacogenetic and environmental factors on the anticoagulant response to warfarin |
Q41168727 | Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer. |
Q29644511 | Warfarin: history, tautomerism and activity |
Q69926294 | gamma-Carboxyglutamic acid |
Search more.