serine has been researched along with propylthiouracil in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (66.67) | 29.6817 |
2010's | 1 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Chen, M; Ding, L; Lian, G; Liu, L; Ni, J; Zhao, D | 1 |
Darras, VM; Demeneix, B; Destree, O; Klootwijk, W; Kuiper, GG; Morvan Dubois, G; Van der Geyten, S; Visser, TJ | 1 |
Gereben, B; Goemann, IM; Harney, JW; Larsen, PR; Maia, AL; Zhu, B | 1 |
3 other study(ies) available for serine and propylthiouracil
Article | Year |
---|---|
A selenium-containing catalytic antibody with Type I deiodinase activity.
Topics: Amino Acid Substitution; Animals; Antibodies, Catalytic; Antibodies, Monoclonal; Dithiothreitol; Haptens; Iodide Peroxidase; Kinetics; Mice; Mice, Inbred BALB C; Propylthiouracil; Selenocysteine; Serine; Thyroxine | 2001 |
Characterization of recombinant Xenopus laevis type I iodothyronine deiodinase: substitution of a proline residue in the catalytic center by serine (Pro132Ser) restores sensitivity to 6-propyl-2-thiouracil.
Topics: 3' Untranslated Regions; Amino Acid Sequence; Animals; Base Sequence; Catalytic Domain; Iodide Peroxidase; Kinetics; Molecular Sequence Data; Mutation; Proline; Propylthiouracil; Rats; Selenocysteine; Sequence Homology, Amino Acid; Serine; Xenopus laevis | 2006 |
Substitution of serine for proline in the active center of type 2 iodothyronine deiodinase substantially alters its in vitro biochemical properties with dithiothreitol but not its function in intact cells.
Topics: Amino Acid Substitution; Catalytic Domain; Cell Line; Dithiothreitol; Glutathione; Humans; Iodide Peroxidase; Kidney; Kinetics; Liver; Proline; Propylthiouracil; Serine; Thyroxine; Transfection | 2010 |