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Items: 1 to 20 of 120

1.

Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells.

Tie JK, Jin DY, Stafford DW.

Antioxid Redox Signal. 2012 Feb 15;16(4):329-38. doi: 10.1089/ars.2011.4043. Epub 2011 Nov 22.

2.

Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration.

Tie JK, Jin DY, Stafford DW.

J Biol Chem. 2014 Mar 28;289(13):9396-407. doi: 10.1074/jbc.M113.534446. Epub 2014 Feb 13.

4.

Vitamin K epoxide reductase complex subunit 1 (VKORC1): the key protein of the vitamin K cycle.

Oldenburg J, Bevans CG, Müller CR, Watzka M.

Antioxid Redox Signal. 2006 Mar-Apr;8(3-4):347-53. Review.

PMID:
16677080
5.

[Vitamin K epoxide reductase: Fresh blood for oral anticoagulant therapies].

Loriot MA, Beaune P.

Rev Med Interne. 2006 Dec;27(12):979-82. Epub 2006 Oct 11. Review. French.

PMID:
17070618
6.

The vitamin K oxidoreductase is a multimer that efficiently reduces vitamin K epoxide to hydroquinone to allow vitamin K-dependent protein carboxylation.

Rishavy MA, Hallgren KW, Wilson LA, Usubalieva A, Runge KW, Berkner KL.

J Biol Chem. 2013 Nov 1;288(44):31556-66. doi: 10.1074/jbc.M113.497297. Epub 2013 Aug 5.

7.

Vitamin K epoxide reductase: homology, active site and catalytic mechanism.

Goodstadt L, Ponting CP.

Trends Biochem Sci. 2004 Jun;29(6):289-92.

PMID:
15276181
8.

Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase.

Wang X, Dutton RJ, Beckwith J, Boyd D.

Antioxid Redox Signal. 2011 Apr 15;14(8):1413-20. doi: 10.1089/ars.2010.3558. Epub 2011 Feb 18.

9.

VKORC1 deficiency in mice causes early postnatal lethality due to severe bleeding.

Spohn G, Kleinridders A, Wunderlich FT, Watzka M, Zaucke F, Blumbach K, Geisen C, Seifried E, Müller C, Paulsson M, Brüning JC, Oldenburg J.

Thromb Haemost. 2009 Jun;101(6):1044-50.

PMID:
19492146
10.

VKORC1 and the vitamin K cycle.

Garcia AA, Reitsma PH.

Vitam Horm. 2008;78:23-33. doi: 10.1016/S0083-6729(07)00002-7. Review.

PMID:
18374188
12.

miR-133a regulates vitamin K 2,3-epoxide reductase complex subunit 1 (VKORC1), a key protein in the vitamin K cycle.

Pérez-Andreu V, Teruel R, Corral J, Roldán V, García-Barberá N, Salloum-Asfar S, Gómez-Lechón MJ, Bourgeois S, Deloukas P, Wadelius M, Vicente V, González-Conejero R, Martínez C.

Mol Med. 2013 Jan 22;18:1466-72. doi: 10.2119/molmed.2012.00062.

15.

Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms.

Tie JK, Jin DY, Stafford DW.

J Biol Chem. 2012 Oct 5;287(41):33945-55. doi: 10.1074/jbc.M112.402941. Epub 2012 Aug 24.

16.
17.

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.

Caspers M, Czogalla KJ, Liphardt K, Müller J, Westhofen P, Watzka M, Oldenburg J.

Thromb Res. 2015 May;135(5):977-83. doi: 10.1016/j.thromres.2015.01.025. Epub 2015 Jan 26.

18.

VKORC1L1, an enzyme rescuing the vitamin K 2,3-epoxide reductase activity in some extrahepatic tissues during anticoagulation therapy.

Hammed A, Matagrin B, Spohn G, Prouillac C, Benoit E, Lattard V.

J Biol Chem. 2013 Oct 4;288(40):28733-42. doi: 10.1074/jbc.M113.457119. Epub 2013 Aug 8.

19.
20.

The Arg98Trp mutation in human VKORC1 causing VKCFD2 disrupts a di-arginine-based ER retention motif.

Czogalla KJ, Biswas A, Rost S, Watzka M, Oldenburg J.

Blood. 2014 Aug 21;124(8):1354-62. doi: 10.1182/blood-2013-12-545988. Epub 2014 Jun 24.

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