nandrolone has been researched along with equilenin in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (20.00) | 18.7374 |
1990's | 1 (20.00) | 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 |
---|---|
Ban, F; Cherkasov, A; Fallahi, M; Hammond, GL; Santos-Filho, O; Thorsteinson, N | 1 |
Alfsen, A; Baulieu, EE; Vincent, F; Weintraub, H | 1 |
Choi, G; Choi, KY; Jang, DS; Joo, S; Kim, DH; Kim, JS; Nam, GH; Oh, BH | 1 |
Choi, G; Choi, KY; Ha, NC; Kim, DH; Kim, SW; Oh, BH; Park, S | 1 |
Choi, KY; Kim, YG; Nam, GH; Oh, BH; Yun, YS | 1 |
5 other study(ies) available for nandrolone and equilenin
Article | Year |
---|---|
An updated steroid benchmark set and its application in the discovery of novel nanomolar ligands of sex hormone-binding globulin.
Topics: Binding Sites; Binding, Competitive; Computer Simulation; Databases as Topic; Humans; Ligands; Linear Models; Models, Molecular; Predictive Value of Tests; Protein Binding; Quantitative Structure-Activity Relationship; Reproducibility of Results; Sex Hormone-Binding Globulin; Steroids | 2008 |
'Half-of-the-sites' reactivity of steroid isomerase.
Topics: Binding Sites; Binding, Competitive; Equilenin; Estradiol; Isomerases; Kinetics; Nandrolone; Pseudomonas; Spectrometry, Fluorescence; Steroid Isomerases | 1976 |
Roles of active site aromatic residues in catalysis by ketosteroid isomerase from Pseudomonas putida biotype B.
Topics: Alanine; Amino Acid Substitution; Binding Sites; Catalysis; Equilenin; Kinetics; Mutagenesis, Site-Directed; Nandrolone; Phenylalanine; Pseudomonas putida; Recombinant Proteins; Spectrometry, Fluorescence; Steroid Isomerases; Tryptophan; Tyrosine | 1999 |
Asp-99 donates a hydrogen bond not to Tyr-14 but to the steroid directly in the catalytic mechanism of Delta 5-3-ketosteroid isomerase from Pseudomonas putida biotype B.
Topics: Asparagine; Aspartic Acid; Binding Sites; Catalysis; Equilenin; Glutamic Acid; Hydrogen Bonding; Kinetics; Macromolecular Substances; Mutagenesis, Site-Directed; Nandrolone; Pseudomonas putida; Steroid Isomerases; Tyrosine | 2000 |
Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B.
Topics: Amino Acid Motifs; Catalysis; Enzyme Stability; Equilenin; Hydrophobic and Hydrophilic Interactions; Kinetics; Models, Molecular; Mutation; Nandrolone; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Pseudomonas putida; Steroid Isomerases; Steroids | 2005 |