tryptophan has been researched along with beryllium fluoride 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 | 3 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Daiho, T; Danko, S; Suzuki, H; Yamasaki, K | 1 |
| Iizuka, R; Inobe, T; Ishii, N; Kuwajima, K; Maki, K; Takahashi, K; Yohda, M; Yoshida, T; Zako, T | 1 |
| Champeil, P; Picard, M; Toyoshima, C | 1 |
3 other study(ies) available for tryptophan and beryllium fluoride
| Article | Year |
|---|---|
Distinct natures of beryllium fluoride-bound, aluminum fluoride-bound, and magnesium fluoride-bound stable analogues of an ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase: changes in catalytic and transport sites during ph
Topics: Adenosine Diphosphate; Adenosine Monophosphate; Aluminum Compounds; Animals; Beryllium; Biochemical Phenomena; Biochemistry; Calcimycin; Calcium; Calcium-Transporting ATPases; Catalytic Domain; Cell Membrane; Chelating Agents; Crystallography, X-Ray; Cytoplasm; Dose-Response Relationship, Drug; Fluorides; Hydrogen-Ion Concentration; Hydrolysis; Magnesium Compounds; Models, Chemical; Muscle, Skeletal; Phosphorylation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rabbits; Sarcoplasmic Reticulum; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Spectrometry, Fluorescence; Thapsigargin; Time Factors; Tryptophan; Vanadates | 2004 |
Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine".
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Aluminum Compounds; Archaea; Archaeal Proteins; Beryllium; Chaperonin Containing TCP-1; Chaperonins; Cytosol; Fluorides; Green Fluorescent Proteins; Microscopy, Electron; Models, Biological; Nucleotides; Peptide Hydrolases; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Scattering, Radiation; Spectrometry, Fluorescence; Temperature; Thermococcus; Tryptophan; X-Rays | 2005 |
Effects of inhibitors on luminal opening of Ca2+ binding sites in an E2P-like complex of sarcoplasmic reticulum Ca22+-ATPase with Be22+-fluoride.
Topics: Adenosine Triphosphatases; Aluminum; Aluminum Compounds; Animals; Beryllium; Binding Sites; Biochemistry; Biological Transport; Calcium; Calcium-Transporting ATPases; Cell Membrane; Enzyme Inhibitors; Fluorides; Hydrogen-Ion Concentration; Indoles; Ions; Magnesium; Microscopy, Fluorescence; Phosphorylation; Protein Binding; Protein Conformation; Rabbits; Sarcoplasmic Reticulum; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Thapsigargin; Time Factors; Tryptophan | 2006 |