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A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.
  • T. Tamura, T. Stadtman
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 6 February 1996
TLDR
The human lung selenoprotein failed to react with anti-rat liver TR polyclonal antibody in immunoblot assays, suggesting the selenocysteine-containing TR from the adenocarcinoma cells may be a variant form distinct from rat liver TR. Expand
Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe4S4 Cluster
TLDR
Crystal structures of the oxidized and reduced formate dehydrogenase H form have been determined, revealing a four-domain αβ structure with the molybdenum directly coordinated to selenium and both MGD cofactors, which suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the Molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer. Expand
Responsiveness of selenoproteins to dietary selenium.
TLDR
Selenocysteine-containing enzymes that have been identified in mammals include the glutathione peroxidase family, one or more iodothyronine deiodinases and two thioredixin reductases, which are less sensitive to dietary selenium fluctuation than the corresponding selenoprotein levels in other tissues. Expand
Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene.
TLDR
The finding that T-cell TR is a selenoenzyme that contains Se in a conserved C-terminal region provides another example of the role of selenium in a major antioxidant enzyme system (i.e., thioredoxin-thiored toxin reductase), in addition to the well-known glutathione peroxidase enzyme system. Expand
Inhibition of NF-kappaB DNA binding and nitric oxide induction in human T cells and lung adenocarcinoma cells by selenite treatment.
  • I. Kim, T. Stadtman
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 25 November 1997
TLDR
In the present study, activation of NF-kappaB in human T cells and lung adenocarcinoma cells was induced by recombinant human tumor necrosis factor alpha or bacterial lipopolysaccharide, and the effects on DNA-binding activity of this transcription factor were examined. Expand
Selenophosphate synthetase. Enzyme properties and catalytic reaction.
TLDR
Isolation of the enzyme and characterization of some of its physical and catalytic properties are described, and attempts to obtain direct evidence for a postulated enzyme-pyrophosphate intermediate using several experimental approaches are described. Expand
Functional Diversity of the Rhodanese Homology Domain
TLDR
It is shown that ybbB is required in vivo for the specific substitution of selenium for sulfur in 2-thiouridine residues in E. coli tRNA, and that the conserved Cys97 (but not Cys96) in the rhodanese sequence motif Cys 96-Cys97-Xaa-XAA-Gly is required for 2-selenouridine synthase in vivo activity. Expand
Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium.
TLDR
Results indicate that the selenium of formate dehydrogenase H is directly involved in formate oxidation, and may help explain the evolutionary conservation of selenocysteine at the enzyme's active site. Expand
Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component.
TLDR
The formate-hydrogen lyase complex of Escherichia coli decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors and inhibited FDHH activity, which protected the enzyme from inactivation by oxygen. Expand
Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX.
TLDR
Addition of chemically prepared monoselenophosphate caused a dose-dependent decrease in the amount of 75Se incorporated into tRNAs from 75SePX generated in situ by SELD enzyme. Expand
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