tryptophan has been researched along with phenylmercuric acetate in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (66.67) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Dix, JA; Lukacovic, MF; Tinklepaugh, MS; Verkman, AS | 1 |
| Birnbaum, ER; Darnall, DW; Le, HP; McPherson, RA; Shahid, F; Suzukida, M | 1 |
| Itoh, Y; Nagase, H; Stack, MS; Young, TN | 1 |
3 other study(ies) available for tryptophan and phenylmercuric acetate
| Article | Year |
|---|---|
Quenching of red cell tryptophan fluorescence by mercurial compounds.
Topics: Anion Exchange Protein 1, Erythrocyte; Biological Transport; Body Water; Chloromercuribenzoates; Depression, Chemical; Dose-Response Relationship, Drug; Erythrocyte Membrane; Ethylmaleimide; Fluorescence; Humans; Kinetics; p-Chloromercuribenzoic Acid; Phenylmercuric Acetate; Protein Binding; Tryptophan; Urea | 1986 |
Resonance energy transfer between cysteine-34 and tryptophan-214 in human serum albumin. Distance measurements as a function of pH.
Topics: Cysteine; Humans; Hydrogen-Ion Concentration; Kinetics; Phenylmercuric Acetate; Protein Conformation; Serum Albumin; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tryptophan | 1983 |
Fluorescence quenching studies of matrix metalloproteinases (MMPs): evidence for structural rearrangement of the proMMP-2/TIMP-2 complex upon mercurial activation.
Topics: Acrylamide; Acrylamides; Enzyme Activation; Enzyme Precursors; Female; Fluorescence; Gelatinases; Humans; In Vitro Techniques; Macromolecular Substances; Metalloendopeptidases; Molecular Structure; Phenylmercuric Acetate; Protease Inhibitors; Proteins; Spectrometry, Fluorescence; Tissue Inhibitor of Metalloproteinase-2; Tryptophan | 1996 |