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Chemistry

D-Index
69
Citations
16667
World Ranking
6200
National Ranking
1889

Biology and Biochemistry

D-Index
69
Citations
16650
World Ranking
7406
National Ranking
3381

Research.com Recognitions

  • 1981 - Member of the National Academy of Sciences

Overview

Thressa C. Stadtman was a scientist affiliated with the National Institutes of Health in the United States. Their work contributed to the medical and biological research fields during their career.

In recognition of their contributions, they were elected as a Member of the National Academy of Sciences in 1981.

Best Publications

  • Vitamin B 12.

    Thressa C. Stadtman

  • SELENOCYSTEINE

    Unknown

  • A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.

    Takashi Tamura;Thressa C. Stadtman

  • Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe4S4 Cluster

    Jeffrey C. Boyington;Vadim N. Gladyshev;Sergei V. Khangulov;Thressa C. Stadtman

  • Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli

    F Zinoni;A Birkmann;T C Stadtman;A Böck

  • Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene

    Vadim N. Gladyshev;Kuan-Teh Jeang;Thressa C. Stadtman

  • Responsiveness of selenoproteins to dietary selenium.

    Christian B. Allan;Gerard M. Lacourciere;Thressa C. Stadtman

  • Selenium Biochemistry Proteins containing selenium are essential components of certain bacterial and mammalian enzyme systems

    Thressa C. Stadtman

  • Identification of a selenocysteyl-tRNA(Ser) in mammalian cells that recognizes the nonsense codon, UGA.

    B. J. Lee;P. J. W. Worland;J. N. Davis;T. C. Stadtman

  • 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 Bar-Noy;Jaeyul Kwon;Rodney L. Levine

  • Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium

    Milton J. Axley;August Bock;Thressa C. Stadtman

  • Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoprotein

    David C. Turner;Thressa C. Stadtman

  • Selenium-Dependent Enzymes

    Unknown

  • Biosynthesis and function of selenocysteine-containing enzymes.

    T C Stadtman

  • Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component.

    M J Axley;D A Grahame;T C Stadtman

  • Inhibition of NF-κB DNA binding and nitric oxide induction in human T cells and lung adenocarcinoma cells by selenite treatment

    Ick Young Kim;Thressa C. Stadtman

  • Monoselenophosphate: synthesis, characterization, and identity with the prokaryotic biological selenium donor, compound SePX.

    Richard S. Glass;Waheguru P. Singh;Woncheol Jung;Zsuzsa Veres;Zsuzsa Veres

  • [63] Preparation and assay of cholesterol and ergosterol

    Thressa C. Stadtman

  • Synthesis of 5-methylaminomethyl-2-selenouridine in tRNAs: 31P NMR studies show the labile selenium donor synthesized by the selD gene product contains selenium bonded to phosphorus

    Zsuzsa Veres;Lin Tsai;Thomas D. Scholz;Michael Politino

  • Selenophosphate synthetase: Enzyme properties and catalytic reaction

    Zsuzsa Veres;Ick Young Kim;Thomas D. Scholz;Thressa C. Stadtman

  • STUDIES ON THE METHANE FERMENTATION X. A New Formate-Decomposing Bacterium, Methanococcus vannielii

    Thressa C. Stadtman;H. A. Barker

  • Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer.

    Sergei V. Khangulov;Vadim N. Gladyshev;Gerard Dismukes;Thressa C. Stadtman

Frequent Co-Authors

Vadim N. Gladyshev
Vadim N. Gladyshev Brigham and Women's Hospital
August Böck
August Böck Ludwig-Maximilians-Universität München
Earl R. Stadtman
Earl R. Stadtman National Institutes of Health
Peter D. Sun
Peter D. Sun National Institutes of Health
Rodney L. Levine
Rodney L. Levine National Institutes of Health
Nobuyoshi Esaki
Nobuyoshi Esaki Kyoto University
Sue Goo Rhee
Sue Goo Rhee Ewha Womans University
Hsiang-Fu Kung
Hsiang-Fu Kung Chinese University of Hong Kong
Dolph L. Hatfield
Dolph L. Hatfield National Institutes of Health
Tatsuo Kurihara
Tatsuo Kurihara Kyoto University

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