Warfarin and vitamin K compete for binding to Phe55 in human VKOR

Structural and functional insights into enzymes of the vitamin K cycle

(2016) J.-K. Tie et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Two enzymes catalyze vitamin K 2,3-epoxide reductase activity in mouse: VKORC1 is highly expressed in exocrine tissues while VKORC1L1 is highly expressed in brain

(2015) Michael Caspers et al.   THROMBOSIS RESEARCH

Structural Modeling Insights into Human VKORC1 Phenotypes

(2015) Katrin Czogalla et al.   Nutrients

Phylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family

(2015) Carville Bevans et al.   Nutrients

Synthesis of an arrayed sgRNA library targeting the human genome

(2015) Tobias Schmidt et al.   Scientific Reports

YASARA View—molecular graphics for all devices—from smartphones to workstations

(2014) Elmar Krieger et al.   BIOINFORMATICS

How I treat poisoning with vitamin K antagonists

(2014) S. Schulman et al.   BLOOD

OutKnocker: a web tool for rapid and simple genotyping of designer nuclease edited cell lines

(2014) Jonathan L. Schmid-Burgk et al.   GENOME RESEARCH

Recent trends in the metabolism and cell biology of vitamin K with special reference to vitamin K cycling and MK-4 biosynthesis

(2014) Martin J. Shearer et al.   JOURNAL OF LIPID RESEARCH

Key Amino Acids of Arabidopsis VKOR in the Activity of Phylloquinone Reduction and Disulfide Bond Formation

(2014) Xiao-Jian Yang et al.   PROTEIN AND PEPTIDE LETTERS

Assessment of the contribution of NAD(P)H-dependent quinone oxidoreductase 1 (NQO1) to the reduction of vitamin K in wild-type and NQO1-deficient mice

(2013) Brian O. Ingram et al.   BIOCHEMICAL JOURNAL

Human VKORC1 mutations cause variable degrees of 4-hydroxycoumarin resistance and affect putative warfarin binding interfaces

(2013) K. J. Czogalla et al.   BLOOD

A cellular system for quantitation of vitamin K cycle activity: structure-activity effects on vitamin K antagonism by warfarin metabolites

(2013) J. A. Haque et al.   BLOOD

VKORC1L1, an Enzyme Rescuing the Vitamin K 2,3-Epoxide Reductase Activity in Some Extrahepatic Tissues during Anticoagulation Therapy

(2013) Abdessalem Hammed et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A new cell culture-based assay quantifies vitamin K 2,3-epoxide reductase complex subunit 1 function and reveals warfarin resistance phenotypes not shown by the dithiothreitol-driven VKOR assay

(2013) A. Fregin et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Evaluation of warfarin resistance using transcription activator-like effector nucleases-mediated vitamin K epoxide reductase knockout HEK293 cells

(2013) J.-K. Tie et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS

New insights into the catalytic mechanism of vitamin K epoxide reductase (VKORC1) - The catalytic properties of the major mutations of rVKORC1 explain the biological cost associated to mutations

(2013) Benjamin Matagrin et al.   FEBS Open Bio

VKORC1mutations detected in patients resistant to vitamin K antagonists are not all associated with a resistant VKOR activity

(2012) A. HODROGE et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Vitamin K Nutrition, Metabolism, and Requirements: Current Concepts and Future Research

(2012) Martin J. Shearer et al.   Advances in Nutrition

Biochemical characterization of spontaneous mutants of rat VKORC1 involved in the resistance to antivitamin K anticoagulants

(2011) Ahmed Hodroge et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Novel Insight into the Mechanism of the Vitamin K Oxidoreductase (VKOR)

(2010) Mark A. Rishavy et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Thirteen novel VKORC1 mutations associated with oral anticoagulant resistance: insights into improved patient diagnosis and treatment

(2010) M. WATZKA et al.   JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Structure of a bacterial homologue of vitamin K epoxide reductase

(2010) Weikai Li et al.   NATURE

Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners

(2010) S. Schulman et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA