Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
about
Human vitamin K 2,3-epoxide reductase complex subunit 1-like 1 (VKORC1L1) mediates vitamin K-dependent intracellular antioxidant functionRecycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulumConserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regenerationStructural Modeling Insights into Human VKORC1 PhenotypesVKORC1 and VKORC1L1: Why do Vertebrates Have Two Vitamin K 2,3-Epoxide Reductases?Oxidative protein folding: selective pressure for prolamin evolution in riceDisulfide bond formation in the mammalian endoplasmic reticulumProtein disulfide isomerase a multifunctional protein with multiple physiological rolesThe dynamic disulphide relay of quiescin sulphydryl oxidaseCellular disulfide bond formation in bioactive peptides and proteinsStructural and functional insights into enzymes of the vitamin K cycleDepletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasisA cellular system for quantitation of vitamin K cycle activity: structure-activity effects on vitamin K antagonism by warfarin metabolites.Disulfide bond formation in prokaryotes: history, diversity and designDifferent interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzymeProcessing and turnover of the Hedgehog protein in the endoplasmic reticulum.A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle.Proinsulin misfolding and endoplasmic reticulum stress during the development and progression of diabetes.Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells.Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells.Human herpesvirus 8 viral interleukin-6 interacts with splice variant 2 of vitamin K epoxide reductase complex subunit 1.Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides.Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanismsAtypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A.Altered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase.Evaluation of warfarin resistance using transcription activator-like effector nucleases-mediated vitamin K epoxide reductase knockout HEK293 cells.Oxidative protein-folding systems in plant cells.Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis.Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding.Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidaseDisulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals.The oxidative protein folding machinery in plant cells.Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1.Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV.Redox regulation of protein damage in plasma.Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.Zebrafish vitamin K epoxide reductases: expression in vivo, along extracellular matrix mineralization and under phylloquinone and warfarin in vitro exposure.Oxidative folding: recent developments.Extracellular Thiol Isomerases and Their Role in Thrombus Formation
P2860
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P2860
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@ast
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@en
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@nl
type
label
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@ast
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@en
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@nl
prefLabel
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@ast
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@en
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@nl
P2860
P356
P1476
Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
@en
P2093
Belinda Wang
P2860
P304
15027-15032
P356
10.1073/PNAS.1009972107
P407
P577
2010-08-09T00:00:00Z