selenocysteine and propylthiouracil

selenocysteine has been researched along with propylthiouracil in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

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

Other Studies

2 other study(ies) available for selenocysteine and propylthiouracil

Article	Year
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

Article

Year

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