tryptophan has been researched along with dithionitrobenzoic acid in 19 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 8 (42.11) | 18.7374 |
| 1990's | 6 (31.58) | 18.2507 |
| 2000's | 4 (21.05) | 29.6817 |
| 2010's | 1 (5.26) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brenner-Holzach, O | 1 |
| Paus, E | 1 |
| Carlson, GM; Colombo, G; Lardy, HA | 1 |
| Lee, ML; Lipscomb, MS; Muench, KH | 1 |
| Leskovac, V; Pavkov-Pericin, D; Prodanov, V; Trivić, S | 1 |
| Fujimoto, H; Haneda, M; Nakatsuka, M; Nisimoto, Y; Nomura, S; Ohta, T; Shibata, Y; Takeuchi, F; Tamai, T; Tsubouchi, R | 1 |
| Deshpande, V; Hinge, J; Rao, M | 1 |
| Criscimagna, NL; Horowitz, PM | 1 |
| Gill, GN; Monken, CE | 1 |
| Brand, L; Han, MK; Knutson, JR; Roseman, S; Walbridge, DG | 1 |
| Borovikov, IuS; Levitskiĭ, DI | 1 |
| Brown, PR; Marsh, P; Tata, R | 1 |
| Helmkamp, GM; Tremblay, JM; Voziyan, PA; Yarbrough, LR | 1 |
| Ghoshal, AK | 1 |
| Arnold, FH; Gershenson, A; Giver, L; Schauerte, JA | 1 |
| Feng, Z; Qin, G; Xicheng, W | 1 |
| Chen, HM; Chow, CY; Fang, HJ; Hu, CK; Tsong, TY; Wu, MC | 1 |
| Bhowmick, R; Jagannadham, MV; Kayastha, AM; Kumari, NK | 1 |
| Gadhave, K; Giri, R; Kalita, P; Shukla, H; Tripathi, T | 1 |
19 other study(ies) available for tryptophan and dithionitrobenzoic acid
| Article | Year |
|---|---|
Properties of fructose 1,6-diphosphate aldolase from Drosophila melanogaster.
Topics: Amino Acids; Animals; Chemical Phenomena; Chemistry; Dithionitrobenzoic Acid; Drosophila melanogaster; Fructose-Bisphosphate Aldolase; Rabbits; Species Specificity; Spectrophotometry, Ultraviolet; Tryptophan | 1979 |
The chemical modification of tryptophan residues of alpha-mannosidase from Phaseolus vulgaris.
Topics: 2-Hydroxy-5-nitrobenzyl Bromide; Amino Acids; Bromosuccinimide; Circular Dichroism; Dithionitrobenzoic Acid; Mannosidases; Oxidation-Reduction; Plants; Spectrophotometry, Ultraviolet; Tryptophan | 1978 |
Phosphoenolpyruvate carboxykinase (guanosine triphosphate) from rat liver cytosol. Separation of homogeneous forms of the enzyme with high and low activity by chromatography on agarose-hexane-guanosine triphosphate.
Topics: Adenosine Triphosphate; Animals; Chromatography, Affinity; Cysteine; Cytosol; Dithionitrobenzoic Acid; Guanosine Triphosphate; Kinetics; Ligands; Liver; Phosphoenolpyruvate Carboxykinase (GTP); Rats; Tryptophan; Tyrosine | 1978 |
Human tryptophan transfer ribonucleic acid synthetase. Composition, function of thiol groups, and structure of thiol peptides.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Amino Acids; Amino Acyl-tRNA Synthetases; Binding Sites; Dithionitrobenzoic Acid; Dithiothreitol; Humans; Iodoacetates; Kinetics; Macromolecular Substances; Magnesium; Molecular Weight; Peptide Fragments; Protein Binding; Protein Conformation; Sulfhydryl Compounds; Tryptophan; Tryptophan-tRNA Ligase | 1976 |
External yeast beta-fructosidase. The role of tryptophyl residues in catalysis.
Topics: Binding Sites; Bromosuccinimide; Diazonium Compounds; Dithionitrobenzoic Acid; Fructose; Glycoside Hydrolases; Nitrobenzenes; Oxidation-Reduction; Protein Binding; Protein Conformation; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Sucrase; Tetrazoles; Tryptophan | 1975 |
On kynureninase activity.
Topics: Animals; Apoenzymes; Benzothiazoles; Cysteine; Dithionitrobenzoic Acid; Dithiothreitol; Enzyme Activation; Hydrolases; Kynurenine; Liver; Magnesium; Male; Phenylpyruvic Acids; Pyridoxal Phosphate; Rats; Rats, Inbred Strains; Tryptophan; Tyrosine; Xanthurenates | 1991 |
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 |
Stable intermediates can be trapped during the reversible refolding of urea-denatured rhodanese.
Topics: Dithionitrobenzoic Acid; Enzyme Stability; Kinetics; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Sulfurtransferases; Thiosulfate Sulfurtransferase; Time Factors; Tryptophan; Urea | 1990 |
A comparison of the cyclic nucleotide-dependent protein kinases using chemical cleavage at tryptophan and cysteine.
Topics: Amino Acid Sequence; Animals; Cattle; Chromatography, Gel; Cyclic AMP; Cyclic GMP; Cysteine; Disulfides; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Kinetics; Molecular Weight; Protein Kinases; Tryptophan | 1985 |
Nanosecond time-resolved fluorescence kinetic studies of the 5,5'-dithiobis(2-nitrobenzoic acid) reaction with enzyme I of the phosphoenolpyruvate:glycose phosphotransferase system.
Topics: Dithionitrobenzoic Acid; Energy Transfer; Fluorescence; Kinetics; Phosphoenolpyruvate Sugar Phosphotransferase System; Protein Conformation; Tryptophan | 1987 |
[High sensitivity to Ca2 ions of the conformational changes of F-actin, induced by the myosin 1 subfragment].
Topics: Actins; Animals; Calcium; Dithionitrobenzoic Acid; Fluorescence Polarization; In Vitro Techniques; Muscle Contraction; Muscles; Myosin Subfragments; Myosins; Peptide Fragments; Protein Binding; Protein Conformation; Rabbits; Tryptophan | 1984 |
Arg-188 and Trp-144 are implicated in the binding of urea and acetamide to the active site of the amidase from Pseudomonas aeruginosa.
Topics: Acetamides; Amidohydrolases; Arginine; Base Sequence; Binding Sites; Dithionitrobenzoic Acid; Enzyme Stability; Hot Temperature; Molecular Sequence Data; Mutation; Polymerase Chain Reaction; Pseudomonas aeruginosa; Tryptophan; Urea | 1994 |
Truncations of the C-terminus have different effects on the conformation and activity of phosphatidylinositol transfer protein.
Topics: Acrylamide; Acrylamides; Anilino Naphthalenesulfonates; Animals; Carrier Proteins; Circular Dichroism; Cysteine; Dithionitrobenzoic Acid; Escherichia coli; Kinetics; Membrane Proteins; Mutation; Phosphatidylcholines; Phosphatidylinositols; Phospholipid Transfer Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Rats; Recombinant Proteins; Sequence Deletion; Tryptophan | 1996 |
Minithioredoxin: a folded and functional peptide fragment of thioredoxin.
Topics: Anilino Naphthalenesulfonates; Circular Dichroism; Dithionitrobenzoic Acid; Dithiothreitol; Escherichia coli; Fluorescent Dyes; Hydrogen-Ion Concentration; Models, Molecular; Peptide Fragments; Phenylalanine; Protein Folding; Spectrometry, Fluorescence; Sulfhydryl Reagents; Thioredoxin-Disulfide Reductase; Thioredoxins; Tryptophan | 1999 |
Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases.
Topics: Directed Molecular Evolution; Dithionitrobenzoic Acid; Enzyme Stability; Esterases; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Luminescent Measurements; Models, Molecular; Mutation; Nitrophenols; Pliability; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Temperature; Tryptophan; Vibration | 2000 |
The kinetic study of arginine kinase from the sea cucumber Stichopus japonicus with 5,5'-dithiobis-(2-nitrobenzoic acid).
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Arginine Kinase; Binding Sites; Catalysis; Cysteine; Dimerization; Dithionitrobenzoic Acid; Dithiothreitol; Dose-Response Relationship, Drug; Kinetics; Magnesium; Models, Chemical; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sea Cucumbers; Spectrometry, Fluorescence; Substrate Specificity; Sulfhydryl Compounds; Time Factors; Tryptophan | 2005 |
Compact dimension of denatured states of staphylococcal nuclease.
Topics: Animals; Cysteine; Dithionitrobenzoic Acid; Fluorescence; Guanidine; Hydrogen-Ion Concentration; Kinetics; Micrococcal Nuclease; Mutant Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Salmon; Tryptophan | 2008 |
Purification and characterization of a novel protease from the latex of Pedilanthus tithymaloids.
Topics: Ammonium Sulfate; Chromatography, Ion Exchange; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Enzyme Activators; Euphorbiaceae; Hydrogen-Ion Concentration; Latex; Peptide Hydrolases; Plant Proteins; Protein Stability; Spectrophotometry; Substrate Specificity; Temperature; Tryptophan; Tyrosine | 2008 |
Role of the glutaredoxin domain and FAD in the stabilization of thioredoxin glutathione reductase.
Topics: Animals; Catalysis; Dithionitrobenzoic Acid; Fasciola; Flavin-Adenine Dinucleotide; Glutaredoxins; Helminth Proteins; Multienzyme Complexes; Mutation; NADH, NADPH Oxidoreductases; NADP; Protein Binding; Protein Conformation; Protein Domains; Protein Stability; Protein Unfolding; Thioredoxins; Tryptophan; Urea | 2018 |