1981 - Member of the National Academy of Sciences
His research on Methanococcus often connects related topics like Gene. He connects Gene with Cofactor in his study. He integrates Cofactor with Biochemistry in his research. Many of his studies on Biochemistry apply to Thermophile as well. In his work, Thressa C. Stadtman performs multidisciplinary research in Thermophile and Methanococcus. In his papers, he integrates diverse fields, such as Enzyme and Cysteine. In his works, Thressa C. Stadtman performs multidisciplinary study on Cysteine and Selenocysteine. In his articles, he combines various disciplines, including Selenocysteine and Enzyme. His research on Archaea often connects related areas such as Methanobacterium.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
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 of the United States of America (1996)
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.
Science (1997)
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.
Proceedings of the National Academy of Sciences of the United States of America (1986)
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.
Proceedings of the National Academy of Sciences of the United States of America (1996)
Responsiveness of selenoproteins to dietary selenium.
Christian B. Allan;Gerard M. Lacourciere;Thressa C. Stadtman.
Annual Review of Nutrition (1999)
Selenium Biochemistry Proteins containing selenium are essential components of certain bacterial and mammalian enzyme systems
Thressa C. Stadtman.
Science (1974)
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.
Journal of Biological Chemistry (1989)
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.
Proceedings of the National Academy of Sciences of the United States of America (2000)
Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium
Milton J. Axley;August Bock;Thressa C. Stadtman.
Proceedings of the National Academy of Sciences of the United States of America (1991)
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 (1973)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below:
Brigham and Women's Hospital
National Institutes of Health
Ludwig-Maximilians-Universität München
National Institutes of Health
National Institutes of Health
Kyoto University
Kyoto University
Chinese University of Hong Kong
National Institutes of Health
National Institutes of Health
University of Washington
Singapore Management University
KU Leuven
Nanyang Technological University
Stanford University
Physical Electronics, Inc.
Harvard University
American Museum of Natural History
Foundation for Biomedical Research
University of Paris-Saclay
University of Miami
Columbia University
Translational Genomics Research Institute
Stanford University
Palo Alto Research Center
Ludwig-Maximilians-Universität München