scholarly article | Q13442814 |
P2093 | author name string | P. C. Preusch | |
P2860 | cites work | Stimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomerase | Q42792635 |
Inhibition of thioredoxin reductase (E.C. 1.6.4.5.) by antitumor quinones | Q43939248 | ||
Solubilization and characterization of vitamin K epoxide reductase from normal and warfarin-resistant rat liver microsomes. | Q54479905 | ||
Vitamin K1 2,3-epoxide and quinone reduction: mechanism and inhibition | Q67298046 | ||
Enzymatic reduction-oxidation of protein disulfides by thioredoxin | Q70397478 | ||
Reduced thioredoxin: a possible physiological cofactor for vitamin K epoxide reductase. Further support for an active site disulfide | Q70407705 | ||
Warfarin inhibition of vitamin K 2,3-epoxide reductase in rat liver microsomes | Q71138461 | ||
Indirect inhibition of vitamin K epoxide reduction by salicylate | Q72590969 | ||
Vitamin K dependent carboxylase: subcellular location of the carboxylase and enzymes involved in Vitamin K metabolism in rat liver | Q72848541 | ||
Identification of a warfarin-sensitive protein component in a 200S rat liver microsomal fraction catalyzing vitamin K and vitamin K 2,3-epoxide reduction | Q93669761 | ||
Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase | Q36405226 | ||
Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins | Q38274381 | ||
Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassay | Q39627376 | ||
Vitamin K epoxide and quinone reductase activities. Evidence for reduction by a common enzyme | Q41238980 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | vitamin K | Q182338 |
(E)-phytonadione | Q186093 | ||
P304 | page(s) | 257-259 | |
P577 | publication date | 1992-07-01 | |
1992-07-06 | |||
P1433 | published in | FEBS Letters | Q1388051 |
P1476 | title | Is thioredoxin the physiological vitamin K epoxide reducing agent? | |
P478 | volume | 305 |
Q28568888 | Characterization and purification of the vitamin K1 2,3 epoxide reductases system from rat liver |
Q24337424 | Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration |
Q40204873 | Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction |
Q39074534 | Functional Study of the Vitamin K Cycle Enzymes in Live Cells |
Q36298281 | Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms |
Q52655392 | Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation. |
Q41862955 | Microsomal lipoamide reductase provides vitamin K epoxide reductase with reducing equivalents |
Q33871717 | News and views on thioredoxin reductases |
Q73788000 | Purification of warfarin-sensitive vitamin K epoxide reductase |
Q37122098 | Structure and function of vitamin K epoxide reductase |
Q34274107 | The thioredoxin system—From science to clinic |
Q28274345 | The vitamin K cycle |
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 |
Q41168727 | Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer. |
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