Engineering of a recombinant vitamin K-dependent gamma-carboxylation system with enhanced gamma-carboxyglutamic acid forming capacity: evidence for a functional CXXC redox center in the system
about
Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regenerationEffects of the blood coagulation vitamin K as an inhibitor of arterial calcificationStructural Modeling Insights into Human VKORC1 PhenotypesStructural and functional insights into enzymes of the vitamin K cycleThe vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylationA cellular system for quantitation of vitamin K cycle activity: structure-activity effects on vitamin K antagonism by warfarin metabolites.A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.Quantum Chemical Study of the Mechanism of Action of Vitamin K Carboxylase in Solvent.Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells.siRNA silencing of calumenin enhances functional factor IX production.Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanismsGlucuronidation of monohydroxylated warfarin metabolites by human liver microsomes and human recombinant UDP-glucuronosyltransferases.Enhanced functional recombinant factor VII production by HEK 293 cells stably transfected with VKORC1 where the gamma-carboxylase inhibitor calumenin is stably suppressed by shRNA transfectionThe oxidative protein folding machinery in plant cells.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.Increased production of functional recombinant human clotting factor IX by baby hamster kidney cells engineered to overexpress VKORC1, the vitamin K 2,3-epoxide-reducing enzyme of the vitamin K cycle.VKORC1 pharmacogenomics summary.Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum.Vitamin K epoxide reductase and its paralogous enzyme have different structures and functions.Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation.Warfarin and vitamin K epoxide reductase: a molecular accounting for observed inhibition.
P2860
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P2860
Engineering of a recombinant vitamin K-dependent gamma-carboxylation system with enhanced gamma-carboxyglutamic acid forming capacity: evidence for a functional CXXC redox center in the system
description
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2005
@ast
im März 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2005/03/18)
@sk
vědecký článek publikovaný v roce 2005
@cs
wetenschappelijk artikel (gepubliceerd op 2005/03/18)
@nl
наукова стаття, опублікована в березні 2005
@uk
name
Engineering of a recombinant v ...... XXC redox center in the system
@ast
Engineering of a recombinant v ...... XXC redox center in the system
@en
Engineering of a recombinant v ...... XXC redox center in the system
@nl
type
label
Engineering of a recombinant v ...... XXC redox center in the system
@ast
Engineering of a recombinant v ...... XXC redox center in the system
@en
Engineering of a recombinant v ...... XXC redox center in the system
@nl
prefLabel
Engineering of a recombinant v ...... XXC redox center in the system
@ast
Engineering of a recombinant v ...... XXC redox center in the system
@en
Engineering of a recombinant v ...... XXC redox center in the system
@nl
P2093
P2860
P356
P1476
Engineering of a recombinant v ...... XXC redox center in the system
@en
P2093
David C. Sane
Nadeem Wajih
Reidar Wallin
Susan M. Hutson
P2860
P304
10540–10547
P356
10.1074/JBC.M413982200
P407
P577
2005-03-18T00:00:00Z