tryptophan has been researched along with vanadates in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (11.11) | 18.7374 |
| 1990's | 2 (22.22) | 18.2507 |
| 2000's | 4 (44.44) | 29.6817 |
| 2010's | 2 (22.22) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Jona, I; Martonosi, A | 1 |
| Martonosi, A; Papp, S; Pikula, S; Vanderkooi, JM | 1 |
| Csermely, P; Gergely, P; Hollósi, M; Holly, S; Jalsovszky, G; Kahn, CR; Kajtár, J; Mihály, K; Somogyi, J; Söti, C | 1 |
| Ajtai, K; Burghardt, TP; Muhlrad, A; Peyser, YM | 1 |
| Chu, JW; Qu, Q; Sharom, FJ | 1 |
| Daiho, T; Danko, S; Suzuki, H; Yamasaki, K | 1 |
| Benabdelhak, H; Blight, MA; Holland, IB; Horn, C; Jumel, K; Schmitt, L | 1 |
| Chen, J; Ghosh, K; Gibb, B; Gupta, K; Sharp, R; Van Duyne, GD | 1 |
| Alexandrova, AN; Gallup, NM; Hengge, AC; Johnson, SJ; Moise, G | 1 |
9 other study(ies) available for tryptophan and vanadates
| Article | Year |
|---|---|
The effect of high pressure on the conformation, interactions and activity of the Ca(2+)-ATPase of sarcoplasmic reticulum.
Topics: Adenosine Triphosphate; Animals; Calcium; Calcium-Transporting ATPases; Egtazic Acid; Fluorescein-5-isothiocyanate; Fluorescence Polarization; Kinetics; Muscles; Pressure; Protein Conformation; Rabbits; Sarcoplasmic Reticulum; Spectrometry, Fluorescence; Tryptophan; Vanadates | 1991 |
Tryptophan phosphorescence of the Ca2+-ATPase of sarcoplasmic reticulum.
Topics: Adenosine Triphosphate; Animals; Butanones; Calcium; Calcium-Transporting ATPases; Egtazic Acid; In Vitro Techniques; Kinetics; Luminescent Measurements; Rabbits; Sarcoplasmic Reticulum; Sodium Nitrite; Spectrometry, Fluorescence; Trichloroacetic Acid; Tryptophan; Vanadates | 1988 |
ATP induces a conformational change of the 90-kDa heat shock protein (hsp90).
Topics: Adenosine Triphosphate; Animals; Circular Dichroism; Fourier Analysis; Heat-Shock Proteins; Hot Temperature; Liver; Male; Molybdenum; Peptide Fragments; Phosphorylation; Protein Conformation; Protein Structure, Secondary; Rats; Rats, Sprague-Dawley; Spectrophotometry, Infrared; Trypsin; Tryptophan; Vanadates | 1993 |
Effect of ionic strength on the conformation of myosin subfragment 1-nucleotide complexes.
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Alkylation; Animals; Circular Dichroism; Cysteine; Lysine; Muscle, Skeletal; Myosin Subfragments; Nucleotides; Osmolar Concentration; Potassium; Protein Binding; Protein Conformation; Rabbits; Time Factors; Trinitrobenzenes; Tryptophan; Vanadates | 2001 |
Transition state P-glycoprotein binds drugs and modulators with unchanged affinity, suggesting a concerted transport mechanism.
Topics: Adenosine Diphosphate; Anilino Naphthalenesulfonates; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Benzimidazoles; Biological Transport; CHO Cells; Cobalt; Cricetinae; Dihydropyridines; Doxorubicin; Magnesium; Pharmaceutical Preparations; Photoaffinity Labels; Protein Binding; Spectrometry, Fluorescence; Tryptophan; Vanadates; Vinblastine | 2003 |
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 |
Positive co-operative activity and dimerization of the isolated ABC ATPase domain of HlyB from Escherichia coli.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Allosteric Regulation; ATP-Binding Cassette Transporters; Azides; Bacterial Proteins; Carrier Proteins; Chromatography, Gel; Codon; Dimerization; Escherichia coli; Fluorescence; Hemolysin Proteins; Kinetics; Mutation; Peptide Fragments; Potassium Chloride; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Sodium Chloride; Solubility; Temperature; Tryptophan; Ultracentrifugation; Vanadates | 2005 |
Requirements for catalysis in the Cre recombinase active site.
Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Biocatalysis; Catalytic Domain; Glutamic Acid; Histidine; Integrases; Lysine; Models, Molecular; Molecular Sequence Data; Recombination, Genetic; Tryptophan; Tyrosine; Vanadates | 2010 |
Conservative tryptophan mutants of the protein tyrosine phosphatase YopH exhibit impaired WPD-loop function and crystallize with divanadate esters in their active sites.
Topics: Amino Acid Substitution; Bacterial Outer Membrane Proteins; Catalytic Domain; Conserved Sequence; Crystallization; Crystallography, X-Ray; Hydrogen Bonding; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Protein Conformation; Protein Tyrosine Phosphatases; Static Electricity; Tryptophan; Vanadates; Yersinia | 2015 |