serine and propylthiouracil

serine has been researched along with propylthiouracil in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (66.67)29.6817
2010's1 (33.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chen, M; Ding, L; Lian, G; Liu, L; Ni, J; Zhao, D1
Darras, VM; Demeneix, B; Destree, O; Klootwijk, W; Kuiper, GG; Morvan Dubois, G; Van der Geyten, S; Visser, TJ1
Gereben, B; Goemann, IM; Harney, JW; Larsen, PR; Maia, AL; Zhu, B1

Other Studies

3 other study(ies) available for serine and propylthiouracil

ArticleYear
A selenium-containing catalytic antibody with Type I deiodinase activity.
    Biochemical and biophysical research communications, 2001, May-25, Volume: 283, Issue:5

    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.
    Endocrinology, 2006, Volume: 147, Issue:7

    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.
    Endocrinology, 2010, Volume: 151, Issue:2

    Topics: Amino Acid Substitution; Catalytic Domain; Cell Line; Dithiothreitol; Glutathione; Humans; Iodide Peroxidase; Kidney; Kinetics; Liver; Proline; Propylthiouracil; Serine; Thyroxine; Transfection

2010