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Relevant bibliographies by topics / Vitamin K epoxide reductase

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Academic literature on the topic 'Vitamin K epoxide reductase'

Author: Grafiati

Published: 28 May 2022

Last updated: 31 July 2025

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Journal articles on the topic "Vitamin K epoxide reductase"

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Thijssen, H. H. W., Y. P. G. Janssen, and L. T. M. Vervoort. "Microsomal lipoamide reductase provides vitamin K epoxide reductase with reducing equivalents." Biochemical Journal 297, no. 2 (1994): 277–80. http://dx.doi.org/10.1042/bj2970277.

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This study was undertaken to search for the endogenous dithiol cofactor of the reductases of the vitamin K cycle. As a starting point, the redox-active lipophilic endogenous compounds lipoic acid and lipoamide were looked at. The study shows that microsomes contain NADH-dependent lipoamide reductase activity. Reduced lipoamide stimulates microsomal vitamin K epoxide reduction with kinetics comparable with those for the synthetic dithiol dithiothreitol (DTT). Reduced lipoic acid shows higher (4-fold) Km values. No reductase activity with lipoic acid was found to be present in microsomes or cyto

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Berg, Marian de Boer-van den, Henk H. W. Thijssen, and Cees Vermeer. "The In Vivo Effects of Oral Anticoagulants in Man: Comparison Between Liver and Non-Hepatic Tissues." Thrombosis and Haemostasis 59, no. 02 (1988): 147–50. http://dx.doi.org/10.1055/s-0038-1642744.

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SummaryThe in vivo effects of oral anticoagulant therapy with 4–hydroxycoumarins on various vitamin K–dependent enzyme systems in man were compared. In hepatic microsomes obtained from donors who has been treated with 4–hydroxycoumarins for more than 6 months, the vitamin K 2,3 epoxide reductase activity and the DTT–dependent vitamin K quinone reductase activity were diminished to 35% and 20% of the corresponding normal values. In the non–hepatic tissues, only a small decrease in vitamin K 2,3 epoxide reductase activity could be demonstrated, while no differences were found in the vitamin K qu

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Van Horn, Wade D. "Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1." Critical Reviews in Biochemistry and Molecular Biology 48, no. 4 (2013): 357–72. http://dx.doi.org/10.3109/10409238.2013.791659.

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Sun, Yan-Mei, Da-Yun Jin, Rodney M. Camire, and Darrel W. Stafford. "Vitamin K epoxide reductase significantly improves carboxylation in a cell line overexpressing factor X." Blood 106, no. 12 (2005): 3811–15. http://dx.doi.org/10.1182/blood-2005-06-2495.

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Previously we reported that we could increase the fraction of carboxylated factor X by reducing the affinity of the propeptide for its binding site on human gamma glutamyl carboxylase. We attributed this to an increased turnover rate. However, even with the reduced affinity propeptide, when sufficient overproduction of factor X is achieved, there is still a significant fraction of uncarboxylated recombinant factor X. We report here that the factor X of such a cell line was only 52% carboxylated but that the fraction of carboxylated factor X could be increased to 92% by coexpressing the recentl

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Liptay-Reuter, I., K. Dose, T. Guenthner, W. Wörner, and F. Oesch. "Vitamin K epoxide reductase activity in the metabolism of epoxides." Biochemical Pharmacology 34, no. 15 (1985): 2617–20. http://dx.doi.org/10.1016/0006-2952(85)90557-x.

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Chu, Pei-hsuan, Teng-yi Huang, Jason Williams, and Darrel W. Stafford. "Purification of a Single Peptide with Vitamin K Epoxide to Vitamin K and Vitamin K to Vitamin KH2 Activity." Blood 108, no. 11 (2006): 331. http://dx.doi.org/10.1182/blood.v108.11.331.331.

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Abstract More than 21 million prescriptions for warfarin are written yearly in the US. Yet, in spite of its importance, vitamin K epoxide reductase (VKOR), the target of warfarin, has resisted purification since its identification in 1972. We report the first successful purification and reconstitution of activity of a recombinant human vitamin K epoxide reductase. A series of detergents were screened to determine that best for solubilization of VKOR from microsomes. Detergents tested that were effective in solubilization of VKOR also led to loss of measurable activity. This loss of activity su

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Begent, L. A., S. T. Chan, and G. B. Steventon. "Kinetics of vitamin K 2,3 epoxide reductase." Biochemical Society Transactions 27, no. 3 (1999): A129. http://dx.doi.org/10.1042/bst027a129b.

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Hill, Anthony, C. Pallister, D. Cowell, and G. Steventon. "Purification of vitamin K 2,3 epoxide reductase." Biochemical Society Transactions 27, no. 3 (1999): A129. http://dx.doi.org/10.1042/bst027a129c.

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Gardill, Sharyn L., and J. W. Suttie. "Vitamin K epoxide and quinone reductase activities." Biochemical Pharmacology 40, no. 5 (1990): 1055–61. http://dx.doi.org/10.1016/0006-2952(90)90493-5.

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Chu, P. H., T. Y. Huang, J. Williams, and D. W. Stafford. "Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2." Proceedings of the National Academy of Sciences 103, no. 51 (2006): 19308–13. http://dx.doi.org/10.1073/pnas.0609401103.

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Dissertations / Theses on the topic "Vitamin K epoxide reductase"

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Hill, Anthony Paul. "Vitamin K 2,3 epoxide reductase : a kinetic, purification and clinical investigation." Thesis, University of the West of England, Bristol, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.311880.

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Дубовик, Євген Іванович, Евгений Иванович Дубовик та Yevhen Ivanovych Dubovyk. "Патогенетичне значення поліморфізму генів циклу вітаміну К для розвитку ішемічного атеротромботичного інсульту". Thesis, Сумський державний університет, 2017. http://essuir.sumdu.edu.ua/handle/123456789/51790.

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Дисертація присвячена вивченню впливу поліморфних варіантів генів циклу вітаміну К (G-1639A і С1173Т гена VKORC1 та Arg406Arg гена GGCX) на розвиток ішемічного атеротромботичного інсульту (ІАТІ). Встановлено, що у представників української популяції існує зв'язок між частотою генотипів за поліморфними сайтами G-1639A (ген VKORC1) і Arg406Arg (ген GGCX) та ризиком розвитку ІАТІ. Носії мінорного А-алеля (G-1639A-поліморфізм) мають у 2,1 раза більшу ймовірність настання ішемічного інсульту, ніж гомозиготи за основним G-алелем. Зазначений ризик зростає в осіб жіночої статі, пацієнтів із надмірною

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Darghouth, Dhouba Dalenda. "Etude d'un multi-deficit congénital en facteur de coagulation vitamine K-dépendant dans une famille tunisienne." Paris 7, 2006. http://www.theses.fr/2006PA077089.

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La gamma-glutamyl carboxylase (gammaGC) et l'époxyde réductase (VKOR) sont des enzymes membranaires du réticulum endoplasmique, qui assurent la gamma-glutamyl carboxylation des facteurs vitamine K-dépendants (FVKD) : II, VII, IX, X, protéines C, S, Z. Une patiente tunisienne présentait un syndrome hémorragique avec multi-déficit en FVKD. L'enquête familiale a montré une transmission récessive, avec les parents et une sœur cliniquement indemnes, et un frère atteint. Nous avons amplifié par PCR et séquence les gènes de gammaGC et VKOR. Aucune mutation n'a été trouvée sur VKOR. Par contre la prop

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Suaréz, Martínez Marcelo Ignacio. "Variabilidad genética en el factor VII de coagulación, Citocromos P450, γ-Glutamil carboxilasa y el complejo vitamina k epoxido-reductasa y su asociación con la dosis de fármacos antivítaminicos k". Tesis, Universidad de Chile, 2019. http://repositorio.uchile.cl/handle/2250/168595.

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Grado de magíster en farmacología<br>INTRODUCCIÓN: En Chile, las enfermedades cardiovasculares son la primera causa de morbimortalidad. Entre los fármacos que se utilizan para su tratamiento se encuentran los antivitamínicos K (AVK), los cuales presentan un estrecho margen terapéutico asociado a una alta variabilidad individual en su respuesta. Estudios farmacogenéticos realizados hasta la fecha indican que los polimorfismos CYP2C9*2, CYP2C9*3 y VKORC1-1639G>A en poblaciones caucásicas explican un 60% la variabilidad de esta respuesta. Por lo tanto, en este trabajo de tesis se evalúa la influe

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Hodroge, Ahmed. "Les mutations spontanées du gène Vkorc1 chez l’homme et le rat : réalité de la résistance." Thesis, Lyon 1, 2011. http://www.theses.fr/2011LYO10281/document.

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Les anticoagulants antivitamines K (AVKs) sont des molécules qui par inhibition de l’activation des PVKDs, empêchent ou retardent la coagulation sanguine. Aujourd’hui, le traitement par AVKs est la première cause d’accidents iatrogènes médicamenteux chez l’homme. Cependant le bénéfice par rapport au risque étant largement supérieur. Elles sont également utilisées dans le contrôle des populations de rongeurs nuisibles. Les AVKs agissent en inhibant l’enzyme VKORC1. Des phénomènes d’hypersensibilité et de résistance aux AVKs sont apparus et plusieurs mutations spontanées ont été découvertes dans

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Hodroge, Ahmed. "Les mutations spontanées du gène Vkorc1 chez l'homme et le rat : réalité de la résistance." Phd thesis, Université Claude Bernard - Lyon I, 2011. http://tel.archives-ouvertes.fr/tel-00866731.

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Les anticoagulants antivitamines K (AVKs) sont des molécules qui par inhibition de l'activation des PVKDs, empêchent ou retardent la coagulation sanguine. Aujourd'hui, le traitement par AVKs est la première cause d'accidents iatrogènes médicamenteux chez l'homme. Cependant le bénéfice par rapport au risque étant largement supérieur. Elles sont également utilisées dans le contrôle des populations de rongeurs nuisibles. Les AVKs agissent en inhibant l'enzyme VKORC1. Des phénomènes d'hypersensibilité et de résistance aux AVKs sont apparus et plusieurs mutations spontanées ont été découvertes dans

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陳定威. "Synthesis of vitamin K 2,3-epoxide reductase inhibitors and SAR studies." Thesis, 2003. http://ndltd.ncl.edu.tw/handle/49974423267304640953.

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Chang, Chengu-Wei, and 張城瑋. "The Association of Genetic Polymorphisms of Vitamin K 2,3-Epoxide Reductase on Risk of Ischemic Stroke." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/92117440923432669821.

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碩士<br>臺北醫學大學<br>公共衛生學研究所<br>98<br>Atherothrombosis which include atherosclerosis and thrombosis is a main cause of ischemic stroke. Among the process, aggregation and adherence of activated platelets and coagulation cascade are related to form thrombus, and then causing thrombosis. The known vitamin K-dependent proteins include coagulation factors VII, IX, X, prothrombin, and Gas 6 (which be able to facilitate the adherence of activated platelets) are modified by γ-carboxylation (a kind of post-translation). Recent study showed that vitamin K 2,3-epoxide reductase (VKOR) is the rate limiting s

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Misenheimer, Tina Marie. "The vitaim K epoxide reductase and its role in warfarin resistance." 1991. http://catalog.hathitrust.org/api/volumes/oclc/24450585.html.

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Thesis (Ph. D.)--University of Wisconsin--Madison, 1991.<br>Typescript. Vita. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 154-166).

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Kuo, Pei-Yu, and 郭佩玉. "Synthesis and Evaluation of 3-Acyl-4-methoxycoumarins as a Selective Protecting Group for Primary Amines and Mechanistic Studies of Vitamin K 2,3-epoxide Reductase." Thesis, 2002. http://ndltd.ncl.edu.tw/handle/42997680561720882914.

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碩士<br>東海大學<br>化學系<br>90<br>Part I、Synthesis and Evaluation of 3-Acyl-4-methoxy coumarins as a Selective Protecting Group for Primary Amines A series of 3-acyl-4-hydroxycoumarins and 3-acyl-4-methoxy coumarins were prepared and evaluated for their potential a priary amine selective protection group. Among the various compounds tested, N-(2-oxo-2H-3-propionyl-chromen-4-yl)-amino esters 5e、5f and 6b display excellent acid (trifluoroacetic acid) /base (piperidine) stability and can be removed with 5﹪hydrazine in DMF at ambient temperature. It has the potential to serve as a useful tool

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Books on the topic "Vitamin K epoxide reductase"

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Dutton, Rachel Janelle. Vitamin K epoxide reductase homologues provide an alternative pathway for bacterial disulfide bond formation. 2010.

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Book chapters on the topic "Vitamin K epoxide reductase"

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Schomburg, Dietmar, and Dörte Stephan. "Vitamin-K-epoxide reductase (warfarin sensitive)." In Enzyme Handbook 10. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-57756-7_128.

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Schomburg, Dietmar, and Dörte Stephan. "Vitamin-K-epoxide reductase (warfarin-insensitive)." In Enzyme Handbook 10. Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-57756-7_129.

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Ledoux, Julie, Maxim Stolyarchuk, and Luba Tchertanov. "Human Vitamin K Epoxide Reductase as a Target of Its Redox Protein." In Bioinformatics and Biomedical Engineering. Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-07802-6_12.

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von Brederlow, B., A. H. E. Fregin, S. Rost, et al. "Congenital Deficiency of Vitamin K Dependent Coagulation Factors in Two Families: Evidence for a Defective Vitamin K-Epoxide-Reductase Complex." In 30th Hemophilia Symposium Hamburg 1999. Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-642-18240-2_32.

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Antonijević, Marko R., Dejan A. Milenković, Edina H. Avdović, and Zoran S. Marković. "Application of Artificial Intelligence for Predicting of New Potential Inhibitors of Vitamin K Epoxide Reductase." In Applied Artificial Intelligence 2: Medicine, Biology, Chemistry, Financial, Games, Engineering. Springer Nature Switzerland, 2024. http://dx.doi.org/10.1007/978-3-031-60840-7_21.

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"Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase." In Vitamin K in Health and Disease. CRC Press, 2009. http://dx.doi.org/10.1201/9780849333927.ch4.

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Suttie, John W. "Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase." In VITAMIN K in Health and Disease. CRC Press, 2009. http://dx.doi.org/10.1201/9781420005110-4.

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"Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase." In Vitamin K in Health and Disease. CRC Press, 2009. http://dx.doi.org/10.1201/9781420005110.ch4.

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Tie, Jian‐Ke, and Darrel W. Stafford. "Structure and Function of Vitamin K Epoxide Reductase." In Vitamins & Hormones. Elsevier, 2008. http://dx.doi.org/10.1016/s0083-6729(07)00006-4.

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Wallin, Reidar, and Thomas M. Guenthner. "[33] Purification of warfarin-sensitive vitamin K epoxide reductase." In Methods in Enzymology. Elsevier, 1997. http://dx.doi.org/10.1016/s0076-6879(97)82123-4.

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Conference papers on the topic "Vitamin K epoxide reductase"

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Shearer, M., K. Andrassy, H. Bechtold, P. McCarthy, J. Koderisch, and H. Koderisch. "CEPHALOSPORIN-INDUCED HYPOPROTHROMBINAEMIA: RELATION TO CEPHALOSPORIN SIDE CHAIN, VITAMIN K METABOLISM AND VITAMIN K STATUS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643076.

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An increased incidence of bleeding episodes due to hypopro-thrombinaemia has been associated with several cephalosporins especially those which contain an N-methyl-thio-tetrazole (NMTT) side chain. To study the etiology of cephalosporin-induced hypo-prothrombinaemia in the clinical situation we have investigated the ability of different cephalosporins to alter the metabolism of vitamin K and the relationship between hypoprothrombinaemia and vitamin K status as assessed from plasma levels of vitamin K. Cephalosporins containing an NMTT side chain (latamoxef, cefmenoxime, cefoperazone, cefotetan

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Suttie, W. J., A. Cheung, and M. G. Wood. "ENZYMOLOGY OF THE VITAMIN K-DEPENDENT CARBOXYLASE: CURRENT STATUS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643991.

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The vitamin K-dependent microsomal carboxylase converts glutamyl residues in precursor proteins to γ-carboxyglutamyl (Gla) residues in completed proteins. The enzyme activity is present in significant activities in most non-skeletal tissues but has been studied most extensively in rat and bovine liver. Early studies of the enzyme utilized bound precursors of vitamin K-dependent clotting factors as substrates for the enzyme and demonstrated that the enzyme requires the reduced form of vitamin K (vitamin KH2), O2, and CO2. Subsequent investigations have taken advantage of the observation that th

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Malia, R. G., H. J. Kennedy, D. R. Triger, and F. E. Preston. "PROTECTIVE EFFECT OF VITAMIN K AGAINST ACETAMINOPHEN (PARACETAMOL) TOXICITY IN THE HAMSTER." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644341.

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We have previously reported that paracetamol may interfere with the metabolism of vitamin K via the vitamin K 2, 3-epoxide cycle. (Thrombosis and Haemostasis, 54,205,1985). In this study we have examined the effects of large doses of vitamin K on experimentally induced paracetamol hepatic necrosis in a hamster model. Paracetamol (1.2g/Kg) when given by gavage to 24 hamsters (Group I) resulted in 10 deaths (42%) at 24 hours. Simultaneous administration of lmg vitamin K intraperitoneally (Group II) reduced mortality to 3/24 (12%); mortality was 2/24 (8%) if vitamin K was given 4 hours after the

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Vermeer, C., BA M. Soute, and MM W. Ulrich. "IN VITRO CARBOXYLATION OF EXOGENOUS PROTEIN SUBSTRATES BY VITAMIN K-DEPENDENT CARBOXYLASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643994.

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In vivo treatment of experimental animals with vitamin K-antagonists induces the accumulation of non-carboxylated coagulation factor precursors in the liver, where they are tightly bound to vitamin K-dependent carboxylase. If hepatic carboxylase is isolated from warfarin-treated animals, it is obtained therefore almost exclusively in the form of an enzyme/substrate complex. If carboxylase is prepared from non-treated animals, on the other hand, the resulting enzyme is predominantly substrate-free. Small substrates like F L E E L or decarboxylated osteocalcinare carboxylated equally well by bot

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