tryptophan has been researched along with bnps-skatole in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (30.00) | 18.7374 |
| 1990's | 5 (50.00) | 18.2507 |
| 2000's | 2 (20.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Deibler, GE; Kramer, AJ; Martenson, RE | 1 |
| Eulitz, M; Zeitler, HJ | 1 |
| Eliopoulos, EE; Findlay, JB; Zagalsky, PF | 1 |
| Crimmins, DL; Macke, K; McCourt, DW; Schwartz, BD; Scott, MG; Thoma, RS | 1 |
| Katzhendler, J; Kowalski, K; Russell, J; Schneider, AB; Sherwood, LM | 1 |
| Fenselau, C; Kelly, MA; Vestling, MM | 1 |
| Altichieri, L; De Antoni, F; De Filippis, V; Fontana, A; Polverino de Laureto, P; Vindigni, A | 1 |
| Carter, CW; Doublié, S; Xue, H; Xue, Y | 1 |
| Haussler, MR; Hsieh, JC; Maalouf, GJ; Mohr, SC; Paz, N; Ray, R; Swamy, N; Xu, W | 1 |
| Eaton, EM; Jameson, MJ; Kibbey, MM; Rosenzweig, SA | 1 |
10 other study(ies) available for tryptophan and bnps-skatole
| Article | Year |
|---|---|
Reaction of peptide 89-169 of bovine myelin basic protein with 2-(2-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine.
Topics: Amino Acids; Animals; Bromine; Cattle; Chemical Phenomena; Chemistry; Electrophoresis, Polyacrylamide Gel; Myelin Basic Protein; Peptides; Skatole; Spectrophotometry, Ultraviolet; Sulfenic Acids; Tryptophan | 1977 |
Improved preparation and structural elucidation of the tryptophan cleavage reagent 2-(2'-nitro-phenylsulfenyl)-3-methyl-3-bromoindolenine (BNPS-skatole).
Topics: Chemical Phenomena; Chemistry; Humans; Immunoglobulin kappa-Chains; Indoles; Peptide Fragments; Proteins; Skatole; Sulfenic Acids; Tryptophan | 1978 |
The lobster carapace carotenoprotein, alpha-crustacyanin. A possible role for tryptophan in the bathochromic spectral shift of protein-bound astaxanthin.
Topics: Animals; Apoproteins; beta Carotene; Binding Sites; Carotenoids; Carrier Proteins; Electrophoresis, Polyacrylamide Gel; Models, Molecular; Nephropidae; Protein Conformation; Proteins; Skatole; Spectrophotometry; Tryptophan; Xanthophylls | 1991 |
In situ chemical cleavage of proteins immobilized to glass-fiber and polyvinylidenedifluoride membranes: cleavage at tryptophan residues with 2-(2'-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine to obtain internal amino acid sequence.
Topics: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Cattle; Chickens; Electrophoresis, Polyacrylamide Gel; Glass; Humans; Immunoblotting; Indoles; Membranes, Artificial; Molecular Sequence Data; Polyvinyls; Protein Binding; Proteins; Skatole; Tryptophan | 1990 |
The single tryptophan residue of human placental lactogen. Effects of modification and cleavage on biologic activity and protein conformation.
Topics: Amino Acids; Animals; Biological Assay; Circular Dichroism; Female; Kinetics; Lactation; Mammary Glands, Animal; Placental Lactogen; Pregnancy; Protein Conformation; Rabbits; Radioimmunoassay; Receptors, Cell Surface; Receptors, Peptide; Skatole; Tryptophan | 1981 |
Optimization by mass spectrometry of a tryptophan-specific protein cleavage reaction.
Topics: Alkylation; Amino Acid Sequence; Angiotensin I; Animals; Horses; Indicators and Reagents; Mass Spectrometry; Melitten; Molecular Sequence Data; Oxidation-Reduction; Proteins; Skatole; Somatostatin; Somatostatin-28; Triose-Phosphate Isomerase; Tryptophan | 1994 |
The core domain of hirudin from the leech Hirudinaria manillensis. Chemical modification of a tryptophan-containing synthetic peptide analog.
Topics: Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Hirudins; Indicators and Reagents; Leeches; Molecular Sequence Data; Nitrobenzenes; Peptide Fragments; Peptides; Protein Structure, Secondary; Skatole; Tryptophan | 1996 |
Chemical modifications of Bacillus subtilis tryptophanyl-tRNA synthetase.
Topics: Bacillus subtilis; Binding Sites; Bromosuccinimide; Cysteine; Enzyme Activation; Iodoacetamide; Protein Conformation; Skatole; Sulfhydryl Compounds; Tryptophan; Tryptophan-tRNA Ligase | 1997 |
Molecular modeling, affinity labeling, and site-directed mutagenesis define the key points of interaction between the ligand-binding domain of the vitamin D nuclear receptor and 1 alpha,25-dihydroxyvitamin D3.
Topics: Affinity Labels; Alkylating Agents; Amino Acid Sequence; Calcifediol; Calcitriol; Carbon Radioisotopes; Cholecalciferol; Cysteine; Humans; Ligands; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Tertiary; Receptors, Calcitriol; Sequence Alignment; Sequence Homology, Amino Acid; Skatole; Tryptophan | 2000 |
Insulin-like growth factor binding protein-2: contributions of the C-terminal domain to insulin-like growth factor-1 binding.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Cells, Cultured; Humans; Insulin-Like Growth Factor Binding Protein 2; Insulin-Like Growth Factor I; Ligands; Molecular Sequence Data; Mutation; Protein Structure, Tertiary; Recombinant Proteins; Sequence Deletion; Skatole; Tryptophan | 2006 |