Thressa C. Stadtman - Concepedia

Author

Thressa C. Stadtman

Also Known As

T C STADTMAN, T C Stadtman, T C. STADTMAN, T STADTMAN, T. C. STADTMAN, T. C. Stadtman, T.C. Stadtman, THRESSA C. STADTMAN, Thressa C Stadtman, Thressa C. Stadtman

212

Publications

12.8K

Citations

H-Index

110

Concepts

All Affiliations

National Heart Lung and Blood Institute National Institutes of Health

About

Thressa C. Stadtman is an author at National Heart Lung and Blood Institute specializing in biochemistry, medicine, and natural sciences.

Top Concepts

#	Concept	H-Index	Publications	Citations
1	Medicine	40	74	5.6K
2	Natural Sciences	35	65	5.5K
3	Engineering	22	26	1.8K
4	Health Sciences	6	6	340
5	Public Health	1	1	46

Thressa C. Stadtman

135

Publications

10.1K

Citations

H-Index

Page 1

	Year	Citations
Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe <sub>4</sub> S <sub>4</sub> Cluster Jeffrey C. Boyington, Vadim N. Gladyshev, Sergei V. Khangulov, Science	1997	579
Vitamin B <sub>12</sub> Thressa C. Stadtman Science NutritionBioorganic ChemistryAldo-keto ReductaseMolecular WeightsChemical Biology	1971	545
A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Takashi Tamura, Thressa C. Stadtman Proceedings of the National Academy of Sciences BiochemistryNew SelenoproteinHuman Lung SelenoproteinMedicineBioanalysis	1996	542
Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli. F. Zinoni, Alexander Birkmann, Thressa C. Stadtman, Proceedings of the National Academy of Sciences Bioorganic ChemistryEngineeringMolecular BiologyEscherichia ColiSelenocysteine-containing Polypeptide	1986	480
Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety. Joyce E. Cone, J N Davis, Thressa C. Stadtman Proceedings of the National Academy of Sciences Aldo-keto ReductaseSelenoprotein ComponentGlycobiologyOrganoselenium MoietyMolecular Biology	1976	304
Identification of a selenocysteyl-tRNASer in mammalian cells that recognizes the nonsense codon, UGA B. J. Lee, Peter J. Worland, J N Davis, Journal of Biological Chemistry Molecular BiologyMolecular GeneticsChemical BiologyNucleic Acid ChemistryProtein Expression	1989	284
Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity Seung-Rock Lee, Shoshana Barnoy, Jaeyul Kwon, Proceedings of the National Academy of Sciences Aldo-keto ReductaseMammalian Thioredoxin ReductaseMolecular BiologyChemical BiologyRedox Biology	2000	267
Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium. Milton J. Axley, A Böck, Thressa C. Stadtman Proceedings of the National Academy of Sciences Sulfur Replaces SeleniumBiosynthesisCellular EnzymologyBiochemistryNatural Sciences	1991	233
Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoprotein David C. Turner, Thressa C. Stadtman Archives of Biochemistry and Biophysics Protein ComponentsBiochemistryNatural SciencesProtein BiosynthesisProtein A	1973	219
Biosynthesis and function of selenocysteine-containing enzymes. Thressa C. Stadtman Journal of Biological Chemistry Selenocysteine-containing EnzymesBiosynthesisCellular EnzymologyBiochemistryNatural Sciences	1991	207

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