histidine has been researched along with dihydrotestosterone in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (40.00) | 18.2507 |
| 2000's | 3 (60.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Khan, MS; Rosner, W | 1 |
| Liao, M; Wilson, EM; Zhou, Zx | 1 |
| Liao, M; Wilson, EM | 1 |
| Huang, YW; Lin, SX; Lu, ML | 1 |
| Boswell, EL; Pletnev, V; Scaccia, LA; Thomas, JL; Umland, TC | 1 |
1 review(s) available for histidine and dihydrotestosterone
| Article | Year |
|---|---|
Production and purification of histidine-tagged dihydrotestosterone-bound full-length human androgen receptor.
Topics: Animals; Dihydrotestosterone; Histidine; Humans; Receptors, Androgen; Recombinant Fusion Proteins | 2001 |
4 other study(ies) available for histidine and dihydrotestosterone
| Article | Year |
|---|---|
Histidine 235 of human sex hormone-binding globulin is the covalent site of attachment of the nucleophilic steroid derivative, 17 beta-bromoacetoxydihydrotestosterone.
Topics: Affinity Labels; Amino Acid Sequence; Binding Sites; Binding, Competitive; Chromatography, High Pressure Liquid; Dihydrotestosterone; Female; Histidine; Humans; Kinetics; Molecular Sequence Data; Peptide Fragments; Peptide Mapping; Pregnancy; Sex Hormone-Binding Globulin; Trypsin | 1990 |
Redox-dependent DNA binding of the purified androgen receptor: evidence for disulfide-linked androgen receptor dimers.
Topics: Animals; Antibodies, Monoclonal; Baculoviridae; Binding Sites; Dihydrotestosterone; Dimerization; Disulfides; DNA-Binding Proteins; Electrophoresis, Polyacrylamide Gel; Histidine; Humans; Mice; Oxidation-Reduction; Receptors, Androgen; Recombinant Proteins; Solutions; Spodoptera | 1999 |
Purification, reconstitution, and steady-state kinetics of the trans-membrane 17 beta-hydroxysteroid dehydrogenase 2.
Topics: 17-Hydroxysteroid Dehydrogenases; 20-alpha-Dihydroprogesterone; Androstenols; Animals; Catalysis; Cell Line; Cell Membrane; Centrifugation, Density Gradient; Cross-Linking Reagents; Detergents; Dihydrotestosterone; Dimerization; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Estradiol; Estradiol Dehydrogenases; Glycerol; Histidine; Humans; Insecta; Kinetics; Liposomes; NADP; Oxygen; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Substrate Specificity; Testosterone; Time Factors | 2002 |
Identification of key amino acids responsible for the substantially higher affinities of human type 1 3beta-hydroxysteroid dehydrogenase/isomerase (3beta-HSD1) for substrates, coenzymes, and inhibitors relative to human 3beta-HSD2.
Topics: 3-Hydroxysteroid Dehydrogenases; Allosteric Site; Amino Acid Sequence; Androstenols; Animals; Arginine; Baculoviridae; Blotting, Western; Catalysis; Catalytic Domain; Cell Line; Dihydrotestosterone; DNA Primers; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Glutamine; Histidine; Humans; Insecta; Kinetics; Models, Chemical; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NAD; Protein Binding; Protein Conformation; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity; Tissue Distribution | 2005 |