Results 1 to 10 of about 757 (112)

Association Between VKORC1 Gene Polymorphisms and Osteopenia and Osteoporosis: A Systematic Review and Meta-Analysis [PDF]

Medicina
Background and Objectives: The vitamin K epoxide reductase complex subunit 1 (VKORC1) plays a central role in the vitamin K cycle, which is essential for γ-carboxylation of multiple bone-related proteins.
Ştefan Cristian Vesa, Vlad-Mihai Ichim, Silvina Iluț, Stefano Miglietta, Mihai Lupu, Camelia Alexandra Coada, Antonia Eugenia Macarie, Ovidiu Chiroban, Anca Dana Buzoianu, Octavia Sabin   +9 more
doaj   +2 more sources

Characterization of Warfarin Inhibition Kinetics Requires Stabilization of Intramembrane Vitamin K Epoxide Reductases [PDF]

Journal of Molecular Biology, 2020
Weikai Li, , Shixuan Liu
exaly   +2 more sources

Structural features determining the vitamin K epoxide reduction activity in the VKOR family of membrane oxidoreductases [PDF]

FEBS Journal, 2022
San-Qiang Li, Hongli Liu, Guomin Shen
exaly   +2 more sources

Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH ₂ [PDF]

Proceedings of the National Academy of Sciences, 2006
More than 21 million prescriptions for warfarin are written yearly in the U.S. Despite its importance, warfarin's target, vitamin K epoxide reductase (VKOR), has resisted purification since its identification in 1972. Here, we report its purification and reconstitution.
Pei-Hsuan, Chu, Teng-Yi, Huang, Jason, Williams, D W, Stafford   +3 more
openaire   +2 more sources

Structure of a bacterial homologue of vitamin K epoxide reductase [PDF]

Nature, 2010
Vitamin K epoxide reductase (VKOR) generates vitamin K hydroquinone to sustain gamma-carboxylation of many blood coagulation factors. Here, we report the 3.6 A crystal structure of a bacterial homologue of VKOR from Synechococcus sp. The structure shows VKOR in complex with its naturally fused redox partner, a thioredoxin-like domain, and corresponds ...
Li, Weikai, Schulman, Sol, Dutton, Rachel J., Boyd, Dana, Beckwith, Jon, Rapoport, Tom A.   +5 more
openaire   +2 more sources

A novel vitamin K derived anticoagulant tolerant to genetic variations of vitamin K epoxide reductase [PDF]

Journal of Thrombosis and Haemostasis, 2021
Vitamin K antagonists (VKAs), such as warfarin, have remained the cornerstone of oral anticoagulation therapy in the prevention and treatment of thromboembolism for more than half a century. They function by impairing the biosynthesis of vitamin K-dependent (VKD) clotting factors through the inhibition of vitamin K epoxide reductase (VKOR).
Xuejie Chen, Yizhou Liu, Natsuko Furukawa, Da‐Yun Jin, G. Paul Savage, Darrel W. Stafford, Yoshitomo Suhara, Craig M. Williams, Jian‐Ke Tie   +8 more
openaire   +4 more sources

Vitamin K Epoxide Reductase: A Protein Involved in Angiogenesis [PDF]

Molecular Cancer Research, 2005
Abstract Vitamin K epoxide reductase (VKOR) is a newly identified protein which has been reported to convert the epoxide of vitamin K back to vitamin K, a cofactor essential for the posttranslational γ-carboxylation of several blood coagulation factors. We found that the gene is expressed ubiquitously including vascular endothelial cells,
Yibo, Wang, Yisong, Zhen, Yi, Shi, Jingzhou, Chen, Channa, Zhang, Xiaojian, Wang, Xu, Yang, Yi, Zheng, Yuqing, Liu, Rutai, Hui   +9 more
openaire   +2 more sources

Warfarin Resistance: A Case Report

Eurasian Journal of Emergency Medicine, 2019
Warfarin is the most widely prescribed anticoagulant in the world. Patients who need more than 15 mg per day should be considered warfarin-resistant.
Uğur Gönlügür, Tanseli Gönlügür, Öztürk Özdemir, Fatma Sılan   +3 more
doaj   +1 more source

Human Vitamin K Epoxide Reductase as a Target of Its Redox Protein

International Journal of Molecular Sciences, 2022
Human Vitamin K epoxide reductase (hVKORC1) is a key enzyme to reduce vitamin K. Such function requires activation of the enzyme by a redox partner delivering reducing equivalents through thioldisulphide exchange reactions. The activation process represents a first and less studied step in hVKORC1 vital cycle, involving the oxidised luminal loop (L ...
Ledoux, Julie, Stolyarchuck, Maxim, Tchertanov, Luba   +2 more
openaire   +5 more sources

Stereospecificity of vitamin K-epoxide reductase.

Journal of Biological Chemistry, 1983
Vitamin K epoxide can occur as a pair of optical isomers due to the asymmetry of the oxirane ring substituents. The stereoselectivity of vitamin K-epoxide reductase for the oxirane ring configuration was determined by recovery of the partially resolved unreacted substrate following incubations of racemic vitamin K epoxide with rat liver microsomes. The
P C, Preusch, J W, Suttie
openaire   +2 more sources