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March 1, 2002Journal of Biological ChemistryOpen Access

Methylseleninate Is a Substrate Rather Than an Inhibitor of Mammalian Thioredoxin Reductase

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Authors

SGStephan GromerCentre National de la Recherche ScientifiqueJGJürgen H. GrossJulius Kühn-Institut

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Gromer et al. (2002) studied this question.

synapsesocial.com/papers/6a9fa18940bc1a697f1dddc7https://doi.org/10.1074/jbc.m109234200
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1The Formation of Diselenide Bridges in Proteins by Incorporation of Selenocysteine Residues: Biosynthesis and Characterization of (Se)2-Thioredoxin1994 · 177 citations
  2. 2Human Thioredoxin Reductase Directly Reduces Lipid Hydroperoxides by NADPH and Selenocystine Strongly Stimulates the Reaction via Catalytically Generated Selenols1995 · 314 citations
  3. 3A hypothesis on the catalytic mechanism of the selenoenzyme thioredoxin reductase1998 · 103 citations
  4. 4Purification of human thioredoxin reductase: Properties and characterization by absorption and circular dichroism spectroscopy1993 · 98 citations