4-hydroxymercuribenzoate has been researched along with tryptophan in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (50.00) | 18.7374 |
| 1990's | 2 (50.00) | 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 |
|---|---|
| Deshpande, V; Hinge, J; Rao, M | 1 |
| Deshpande, VV; Keskar, SS; Srinivasan, MC | 1 |
| Boyaval, P; Desmazeaud, MJ; Moreira, E | 1 |
| Clottes, E; Leydier, C; Marcillat, O; Perraut, C; Vial, C | 1 |
4 other study(ies) available for 4-hydroxymercuribenzoate and tryptophan
| Article | Year |
|---|---|
Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site.
Topics: Bacillus; Binding Sites; Bromosuccinimide; Cysteine; Dithionitrobenzoic Acid; Enzyme Inhibitors; Glycoside Hydrolases; Hot Temperature; Hydroxymercuribenzoates; Kinetics; Streptomyces; Tryptophan; Xylan Endo-1,3-beta-Xylosidase | 1990 |
Chemical modification of a xylanase from a thermotolerant Streptomyces. Evidence for essential tryptophan and cysteine residues at the active site.
Topics: 2-Hydroxy-5-nitrobenzyl Bromide; Binding Sites; Bromosuccinimide; Cysteine; Glycoside Hydrolases; Hot Temperature; Hydroxymercuribenzoates; Streptomyces; Tryptophan; Xylan Endo-1,3-beta-Xylosidase | 1989 |
Transport of aromatic amino acids by Brevibacterium linens.
Topics: 2,4-Dinitrophenol; Biological Transport, Active; Brevibacterium; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Dinitrophenols; Hydrogen-Ion Concentration; Hydroxymercuribenzoates; Kinetics; Phenylalanine; Temperature; Tryptophan; Tyrosine | 1983 |
Role of quaternary structure in muscle creatine kinase stability: tryptophan 210 is important for dimer cohesion.
Topics: Anilino Naphthalenesulfonates; Animals; Chromatography, High Pressure Liquid; Creatine Kinase; Dimerization; Enzyme Stability; Fluorescence; Guanidine; Hydroxymercuribenzoates; Isoenzymes; Mutagenesis, Site-Directed; Myocardium; Protein Conformation; Protein Denaturation; Protein Folding; Rabbits; Spectrometry, Fluorescence; Structure-Activity Relationship; Tryptophan | 1998 |