Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis.

Autor: Lothrop AP; Department of Biochemistry, University of Vermont, College of Medicine , 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405, United States., Snider GW, Flemer S Jr, Ruggles EL, Davidson RS, Lamb AL, Hondal RJ

Publikováno v: Biochemistry [Biochemistry] 2014 Feb 04; Vol. 53 (4), pp. 664-74. Date of Electronic Publication: 2014 Jan 23.

Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium?

Autor: Lothrop AP; Department of Biochemistry, University of Vermont , 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405, United States., Snider GW, Ruggles EL, Hondal RJ

Publikováno v: Biochemistry [Biochemistry] 2014 Jan 28; Vol. 53 (3), pp. 554-65. Date of Electronic Publication: 2014 Jan 15.

No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue.

Autor: Lothrop AP; Department of Biochemistry, University of Vermont, 89 Beaumont Avenue, Given Building Room B413, Burlington, Vermont 05405, USA., Ruggles EL, Hondal RJ

Publikováno v: Biochemistry [Biochemistry] 2009 Jul 07; Vol. 48 (26), pp. 6213-23.

A novel murine protein with no effect on iron homoeostasis is homologous with transferrin and is the putative inhibitor of carbonic anhydrase.

Autor: Wang F; Division of Hematology/Oncology, Children's Hospital Boston, and Harvard Medical School, Boston, MA 02115, USA., Lothrop AP, James NG, Griffiths TA, Lambert LA, Leverence R, Kaltashov IA, Andrews NC, MacGillivray RT, Mason AB

Publikováno v: The Biochemical journal [Biochem J] 2007 Aug 15; Vol. 406 (1), pp. 85-95.