tyrosine has been researched along with isoalloxazine in 12 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (8.33) | 18.2507 |
| 2000's | 7 (58.33) | 29.6817 |
| 2010's | 4 (33.33) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Carey, PR; Dong, J; Palfey, BA; Zheng, Y | 1 |
| Fazal, A; Fisher, D; Greenfield, J; Madura, JD; Moe, OA; Patson, B; Spidel, J; Wigal, C; Zhou, Z | 1 |
| Blay, J; Butler, JJ; Hoskin, DW; Mader, JS; Watson, CL; Zhang, H | 1 |
| Orrit, M | 1 |
| Cova, S; Karnchanaphanurach, P; Louie, TM; Luo, G; Rech, I; Xie, XS; Xun, L; Yang, H | 1 |
| Barber, MJ; Crowley, LJ; Davis, CA; Marohnic, CC; Smith, ET | 1 |
| Basran, J; Combe, JP; Hothi, P; Leys, D; Munro, AW; Rigby, SE; Scrutton, NS | 1 |
| Chosrowjan, H; Mataga, N; Nishina, Y; Sato, K; Shiga, K; Tanaka, F; Taniguchi, S | 1 |
| Chuenchor, W; Hu, J; Rokita, SE | 1 |
| Naito, H; Nishimura, E; Sakurai, T; Seo, D | 1 |
| Bou-Nader, C; Cornu, D; Fontecave, M; Hamdane, D; Hui-Bon-Hoa, G | 1 |
| Bou-Nader, C; Dozova, N; Hamdane, D; Lacombat, F; Plaza, P | 1 |
12 other study(ies) available for tyrosine and isoalloxazine
| Article | Year |
|---|---|
Using Raman spectroscopy to monitor the solvent-exposed and "buried" forms of flavin in p-hydroxybenzoate hydroxylase.
Topics: 4-Hydroxybenzoate-3-Monooxygenase; Amino Acid Substitution; Binding Sites; Flavin-Adenine Dinucleotide; Flavins; Mutagenesis, Site-Directed; Phenylalanine; Protein Conformation; Pseudomonas aeruginosa; Solvents; Spectrum Analysis, Raman; Tyrosine | 1999 |
Kinetic and docking studies of the interaction of quinones with the quinone reductase active site.
Topics: Animals; Anthraquinones; Benzoquinones; Binding Sites; Flavins; Humans; Kinetics; Models, Chemical; Models, Molecular; NAD(P)H Dehydrogenase (Quinone); Naphthoquinones; Rats; Structure-Activity Relationship; Substrate Specificity; Thermodynamics; Tyrosine | 2003 |
Adenosine inhibits activation-induced T cell expression of CD2 and CD28 co-stimulatory molecules: role of interleukin-2 and cyclic AMP signaling pathways.
Topics: Adenosine; Animals; Antibodies, Monoclonal; Caffeine; CD2 Antigens; CD28 Antigens; CD3 Complex; Cell Cycle; Colforsin; Cyclic AMP; Female; Flavins; Interleukin-2; Lymphocyte Activation; Mice; Mice, Inbred C57BL; Phenethylamines; Receptors, Interleukin-2; Receptors, Purinergic P1; Signal Transduction; T-Lymphocytes; Tyrosine | 2003 |
Chemistry. The motions of an enzyme soloist.
Topics: Catalysis; Chemical Phenomena; Chemistry, Physical; Electrons; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorescence; FMN Reductase; Hydrogen Bonding; Lasers; Likelihood Functions; Mathematics; Mutation; Photons; Protein Conformation; Serine; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tyrosine | 2003 |
Protein conformational dynamics probed by single-molecule electron transfer.
Topics: Amino Acid Substitution; Catalysis; Chemical Phenomena; Chemistry, Physical; Computer Simulation; Electrons; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorescence; FMN Reductase; Hydrogen Bonding; Likelihood Functions; Mathematics; Models, Molecular; Mutagenesis, Site-Directed; Photons; Protein Conformation; Serine; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tyrosine | 2003 |
Cytochrome b5 reductase: role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis.
Topics: Amino Acid Motifs; Amino Acid Substitution; Animals; Catalysis; Circular Dichroism; Cytochrome-B(5) Reductase; Enzyme Activation; Flavin-Adenine Dinucleotide; Flavins; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Mutagenesis, Site-Directed; Oxidation-Reduction; Potentiometry; Proline; Rats; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Thermodynamics; Tyrosine | 2005 |
Lys-D48 is required for charge stabilization, rapid flavin reduction, and internal electron transfer in the catalytic cycle of dihydroorotate dehydrogenase B of Lactococcus lactis.
Topics: Catalysis; Dihydroorotate Dehydrogenase; Dimerization; Electrochemistry; Electron Transport; Flavin Mononucleotide; Flavins; Lactococcus lactis; Lysine; Mutagenesis, Site-Directed; NAD; Orotic Acid; Oxidation-Reduction; Oxidoreductases Acting on CH-CH Group Donors; Protein Structure, Tertiary; Tyrosine | 2006 |
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 |
A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate.
Topics: Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Electron Transport; Electrons; Escherichia coli; Flavin Mononucleotide; Flavins; Gene Expression; Humans; Hydrogen-Ion Concentration; Iodide Peroxidase; Iodides; Models, Molecular; Monoiodotyrosine; Oxidation-Reduction; Protein Binding; Recombinant Proteins; Substrate Specificity; Tyrosine | 2015 |
Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP(+) oxidoreductase activity toward NADPH.
Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Ferredoxin-NADP Reductase; Ferredoxins; Flavin-Adenine Dinucleotide; Flavins; Models, Molecular; Molecular Sequence Data; Mutation, Missense; NADP; Sequence Alignment; Tyrosine | 2015 |
Flavin-Protein Complexes: Aromatic Stacking Assisted by a Hydrogen Bond.
Topics: Amino Acid Sequence; Bacillus subtilis; Catalytic Domain; Flavin-Adenine Dinucleotide; Flavins; Hydrogen Bonding; Methylation; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Protein Conformation; tRNA Methyltransferases; Tyrosine | 2015 |
Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO.
Topics: Adenine; Amino Acid Sequence; Bacillus subtilis; Binding Sites; Cysteine; Flavin-Adenine Dinucleotide; Flavins; Kinetics; Models, Molecular; Oxidation-Reduction; Photochemical Processes; Protein Binding; tRNA Methyltransferases; Tyrosine | 2019 |