tryptophan has been researched along with isoalloxazine in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 4 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bellows, DS; Clarke, ID; Diamandis, P; Dirks, PB; Graham, J; Jamieson, LG; Ling, EK; Sacher, AG; Tyers, M; Ward, RJ; Wildenhain, J | 1 |
Foster, MP; Murray, TA; Swenson, RP | 1 |
Antalík, M; Sedlák, E; Sprinzl, M; Sut'ák, R; Zoldák, G | 1 |
Chosrowjan, H; Mataga, N; Nishina, Y; Sato, K; Shiga, K; Tanaka, F; Taniguchi, S | 1 |
4 other study(ies) available for tryptophan and isoalloxazine
Article | Year |
---|---|
Chemical genetics reveals a complex functional ground state of neural stem cells.
Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells | 2007 |
Mechanism of flavin mononucleotide cofactor binding to the Desulfovibrio vulgaris flavodoxin. 2. Evidence for cooperative conformational changes involving tryptophan 60 in the interaction between the phosphate- and ring-binding subsites.
Topics: Apoproteins; Binding, Competitive; Circular Dichroism; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavins; Flavodoxin; Macromolecular Substances; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Phosphates; Protein Binding; Protein Conformation; Recombinant Proteins; Riboflavin; Spectrometry, Fluorescence; Structure-Activity Relationship; Tryptophan | 2003 |
Role of conformational flexibility for enzymatic activity in NADH oxidase from Thermus thermophilus.
Topics: Binding Sites; Catalysis; Circular Dichroism; Crystallography, X-Ray; Dimerization; Flavins; Kinetics; Models, Molecular; Multienzyme Complexes; NADH, NADPH Oxidoreductases; Protein Conformation; Spectrometry, Fluorescence; Temperature; Thermodynamics; Thermus thermophilus; Time Factors; Tryptophan; Urea | 2003 |
Donor-acceptor distance-dependence of photoinduced electron-transfer rate in flavoproteins.
Topics: Acyl-CoA Dehydrogenase; Electron Transport; Flavins; Flavodoxin; Glucose Oxidase; Membrane Transport Proteins; Models, Molecular; Photochemistry; Protein Conformation; Tryptophan; Tyrosine | 2007 |