tyrosine and flavin mononucleotide

tyrosine has been researched along with flavin mononucleotide in 44 studies

Research

Studies (44)

Timeframe	Studies, this research(%)	All Research%
pre-1990	17 (38.64)	18.7374
1990's	9 (20.45)	18.2507
2000's	13 (29.55)	29.6817
2010's	5 (11.36)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Kasper, CB; Porter, TD; Shen, AL; Wilson, TE	1
Eliasson, R; Jörnvall, H; Reichard, P	1
Veeger, C; Visser, J	1
Hopkins, TR; Spikes, JD	1
MacKenzie, RE; McCormick, DB; Wu, FY	1
Draper, RD; Ingraham, LL	1
D'Anna, JA; Tollin, G	1
McCormick, DB; Ying-Hsiueh Wu, F	1
Glad, BW; Kumagai, LF; Spikes, JD	2
Gariépy, J; Hodges, RS; Reid, RE; Sykes, BD	1
Hasegawa, T; Suzuki, T; Yamada, K	1
Li, Z; Meighen, EA	1
Krey, GD; Swenson, RP	1
Covès, J; Eschenbrenner, M; Fontecave, M; Nivière, V	1
Genzor, CG; Perales-Alcón, A; Romero, A; Sancho, J	1
Geoghegan, SM; Mayhew, SG; O'Connell, DP; O'Farrell, PA; Yalloway, GN	1
Swenson, RP; Zhou, Z	1
Gómez-Moreno, C; Lostao, A; Mayhew, SG; Sancho, J	1
Basran, J; Hille, R; Jang, MH; Scrutton, NS; Sutcliffe, MJ	1
Kopecek, J; Kopecková, P; Shen, HR; Spikes, JD	1
Mayer, B; Pfeiffer, S; Schmidt, K	1
Blaesse, M; Huber, R; Kupke, T; Steinbacher, S	1
di Salvo, ML; Ko, TP; Musayev, FN; Raboni, S; Safo, MK; Schirch, V	1
Murray, TA; Swenson, RP	1
Aoyama, H; Da Silva, CC; Ferreira, CV; Granjeiro, JM; Granjeiro, PA; Taga, EM; Volpe, PL	1
ICHIKAWA, Y; YAMANO, T	1
BENABDELJLIL, C; LISSITZKY, S; SIMON, C	1
BJOERK, W	1
BERENHOLC, M; CILENTO, G	1
BENEVENT, MT; LISSITZKY, S; ROQUES, M	1
Orrit, M	1
Cova, S; Karnchanaphanurach, P; Louie, TM; Luo, G; Rech, I; Xie, XS; Xun, L; Yang, H	1
Dertouzos, J; Gafni, A; Jensen, KF; Palfey, BA; Shi, J; Steel, D	1
Kurtz, DM; Lanzilotta, WN; Ljungdahl, LG; Silaghi-Dumitrescu, R	1
Basran, J; Combe, JP; Hothi, P; Leys, D; Munro, AW; Rigby, SE; Scrutton, NS	1
Muralidhara, BK; Rathinakumar, R; Wittung-Stafshede, P	1
Baldwin, TO; Campbell, ZT; Montfort, WR; Weichsel, A	1
Hore, PJ; Kirsch-De Mesmaeker, A; Luhmer, M; Mugeniwabagara, E; Perrier, S	1
Kokpol, S; Lugsanangarm, K; Nueangaudom, A; Nunthaboot, N; Pianwanit, S; Tanaka, F	1
Chang, CW; Guo, L; Guo, X; He, TF; Wang, L; Zhong, D	1
Chuenchor, W; Hu, J; Rokita, SE	1
Bargon, J; Bernarding, J; Bommerich, U; Bruns, C; Euchner, F; Müller, D; Plaumann, M; Ringleb, R; Trantzschel, T	1
Lin, CC; Liu, HY; Nguyen, HD	1

Other Studies

44 other study(ies) available for tyrosine and flavin mononucleotide

Article	Year
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis. The Journal of biological chemistry, 1989, May-05, Volume: 264, Issue:13 Topics: Amino Acid Sequence; Animals; Base Sequence; Catalysis; Cloning, Molecular; Cytochrome P-450 Enzyme System; DNA Mutational Analysis; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Kinetics; Molecular Sequence Data; NADH Dehydrogenase; NADP; NADPH-Ferrihemoprotein Reductase; Oxidoreductases; Rats; Spectrum Analysis; Tyrosine	1989
Superoxide dismutase participates in the enzymatic formation of the tyrosine radical of ribonucleotide reductase from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 1986, Volume: 83, Issue:8 Topics: Enzyme Activation; Escherichia coli; Flavin Mononucleotide; Free Radicals; NADP; Oxygen; Ribonucleotide Reductases; Superoxide Dismutase; Tyrosine	1986
Relation between conformations and activities of lipoamide dehydrogenase. IV. Apoenzyme structure and flavin binding aspects. Biochimica et biophysica acta, 1970, May-13, Volume: 206, Issue:2 Topics: Adenine; Binding Sites; Chemical Phenomena; Chemistry; Chloromercuribenzoates; Cold Temperature; Dihydrolipoamide Dehydrogenase; Diphosphates; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorometry; Halogens; Hot Temperature; Hydrogen-Ion Concentration; Osmolar Concentration; Protein Binding; Protein Denaturation; Time Factors; Tryptophan; Tyrosine; Urea	1970
Conformational changes in ribonuclease during photodynamic inactivation. Radiation research, 1972, Volume: 51, Issue:2 Topics: Animals; Cattle; Chromatography, Gel; Chromatography, Ion Exchange; Coloring Agents; Flavin Mononucleotide; Fluorescence; Hot Temperature; Immunodiffusion; Light; Methylene Blue; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Rabbits; Radiation Effects; Ribonucleases; Time Factors; Tyrosine; Urea	1972
Kinetics and mechanism of oxidation-reduction reactions between pyridine nucleotides and flavins. Biochemistry, 1970, May-26, Volume: 9, Issue:11 Topics: Alanine; Amino Acids; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Hot Temperature; Hydrocarbons; Kinetics; Nucleotides; Oxidation-Reduction; Peptides; Phenylalanine; Pyridines; Tryptophan; Tyrosine	1970
The affinity of flavin semiquinones for certain aromatic compounds and disulfides. Archives of biochemistry and biophysics, 1970, Volume: 139, Issue:2 Topics: Amino Acids; Chemical Phenomena; Chemistry; Flavin Mononucleotide; Glutathione; Methods; Nicotinic Acids; Oxidation-Reduction; Phenylalanine; Picolinic Acids; Pyridines; Quinones; Riboflavin; Serotonin; Sulfides; Tryptophan; Tyrosine	1970
Protein fluorescence and solvent perturbation spectra as probes of flavin--protein interactions in the Shethna flavoprotein. Biochemistry, 1971, Jan-05, Volume: 10, Issue:1 Topics: Azotobacter; Bacterial Proteins; Circular Dichroism; Energy Transfer; Flavin Mononucleotide; Flavins; Fluorescence; Free Radicals; Glycols; Kinetics; Oxidation-Reduction; Quinones; Solvents; Spectrophotometry; Spectrum Analysis; Tryptophan; Tyrosine	1971
Flavin-sensitized photooxidations of tryptophan and tyrosine. Biochimica et biophysica acta, 1971, May-25, Volume: 236, Issue:2 Topics: Acetates; Colorimetry; Dimethyl Sulfoxide; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Hydrogen-Ion Concentration; Kinetics; Light; Oxidation-Reduction; Peptides; Photochemistry; Radiation Effects; Temperature; Tryptophan; Tyrosine	1971
Tyrosine and thyronine analogs and inhibitors of the dye-sensitized photoinactivatioof lysozyme. Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), 1969, Volume: 131, Issue:4 Topics: Bromine; Diiodotyrosine; Flavin Mononucleotide; Fluoresceins; Light; Methylene Blue; Monoiodotyrosine; Muramidase; Potassium Iodide; Radiation Effects; Radiation-Protective Agents; Radiochemistry; Thyronines; Thyroxine; Triiodothyronine; Tyrosine	1969
The effects of tyrosine and thyronine analogues on the dye-sensitized photoinactivation of trypsin. Life sciences, 1967, Jan-15, Volume: 6, Issue:2 Topics: Diiodotyrosine; Flavin Mononucleotide; Light; Methylene Blue; Potassium Iodide; Thyroid Hormones; Thyronines; Thyroxine; Triiodothyronine; Trypsin; Tyrosine	1967
Proton nuclear magnetic resonance investigation of synthetic calcium-binding peptides. Biochemistry, 1982, Mar-30, Volume: 21, Issue:7 Topics: Amino Acid Sequence; Calcium; Flavin Mononucleotide; Lactoperoxidase; Lasers; Magnetic Resonance Spectroscopy; Muscle Proteins; Peptide Fragments; Potassium Iodide; Troponin; Troponin C; Tyrosine	1982
Interaction between rat lactic dehydrogenase M4 isozyme and vitamin B2 derivatives. Journal of nutritional science and vitaminology, 1982, Volume: 28, Issue:4 Topics: Animals; Arginine; Binding Sites; Chemical Phenomena; Chemistry; Flavin Mononucleotide; Histidine; Isoenzymes; L-Lactate Dehydrogenase; Rats; Structure-Activity Relationship; Tryptophan; Tyrosine	1982
Tryptophan 250 on the alpha subunit plays an important role in flavin and aldehyde binding to bacterial luciferase. Effects of W-->Y mutations on catalytic function. Biochemistry, 1995, Nov-21, Volume: 34, Issue:46 Topics: Aldehydes; Binding Sites; Enterobacteriaceae; Fatty Acids; Flavin Mononucleotide; Kinetics; Luciferases; Luminescent Measurements; Mutagenesis; Oxidation-Reduction; Point Mutation; Spectrometry, Fluorescence; Structure-Activity Relationship; Tryptophan; Tyrosine	1995
Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions. Biochemistry, 1994, Jul-19, Volume: 33, Issue:28 Topics: Binding Sites; Chemical Phenomena; Chemistry, Physical; Desulfovibrio vulgaris; Drug Stability; Electrochemistry; Flavin Mononucleotide; Flavodoxin; Molecular Structure; Mutagenesis, Site-Directed; Oxidation-Reduction; Quinones; Solvents; Spectrometry, Fluorescence; Spectrophotometry; Structure-Activity Relationship; Thermodynamics; Tyrosine	1994
NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase. The Journal of biological chemistry, 1993, Sep-05, Volume: 268, Issue:25 Topics: Amino Acid Sequence; Blotting, Western; Catalysis; Electron Transport; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; FMN Reductase; Free Radicals; Hydroxyurea; Molecular Sequence Data; Molecular Weight; Mutation; NADH, NADPH Oxidoreductases; NADP; Oxidoreductases Acting on Sulfur Group Donors; Ribonucleotide Reductases; Sulfite Reductase (NADPH); Tyrosine	1993
Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin. Nature structural biology, 1996, Volume: 3, Issue:4 Topics: Apoproteins; Crystallography, X-Ray; Flavin Mononucleotide; Flavodoxin; Models, Molecular; Protein Folding; Tryptophan; Tyrosine	1996
Regulation of the redox potentials of flavodoxins: modification of the flavin binding. Biochemical Society transactions, 1996, Volume: 24, Issue:1 Topics: Aspartic Acid; Binding Sites; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Hydrogen-Ion Concentration; Hydroquinones; Mutagenesis, Site-Directed; Oxidation-Reduction; Point Mutation; Recombinant Proteins; Thermodynamics; Tryptophan; Tyrosine	1996
The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris [Hi Biochemistry, 1996, Dec-17, Volume: 35, Issue:50 Topics: Binding Sites; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Point Mutation; Protein Structure, Tertiary; Recombinant Proteins; Static Electricity; Tyrosine	1996
Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials. Biochemistry, 1997, Nov-25, Volume: 36, Issue:47 Topics: Anabaena; Computer Simulation; Flavin Mononucleotide; Flavodoxin; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Point Mutation; Protein Conformation; Recombinant Proteins; Spectrometry, Fluorescence; Spectrophotometry; Thermodynamics; Tryptophan; Tyrosine	1997
The role of Tyr-169 of trimethylamine dehydrogenase in substrate oxidation and magnetic interaction between FMN cofactor and the 4Fe/4S center. The Journal of biological chemistry, 1999, May-07, Volume: 274, Issue:19 Topics: Electron Spin Resonance Spectroscopy; Flavin Mononucleotide; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Kinetics; Methylamines; Oxidation-Reduction; Oxidoreductases, N-Demethylating; Spectrophotometry, Ultraviolet; Substrate Specificity; Tyrosine	1999
Photodynamic crosslinking of proteins. III. Kinetics of the FMN- and rose bengal-sensitized photooxidation and intermolecular crosslinking of model tyrosine-containing N-(2-hydroxypropyl)methacrylamide copolymers. Photochemistry and photobiology, 1999, Volume: 70, Issue:2 Topics: Cross-Linking Reagents; Flavin Mononucleotide; Kinetics; Oxidation-Reduction; Photochemistry; Photosensitizing Agents; Polymers; Proteins; Rose Bengal; Tyrosine	1999
Dityrosine formation outcompetes tyrosine nitration at low steady-state concentrations of peroxynitrite. Implications for tyrosine modification by nitric oxide/superoxide in vivo. The Journal of biological chemistry, 2000, Mar-03, Volume: 275, Issue:9 Topics: Dimerization; Flavin Mononucleotide; Free Radicals; Hydrazines; Hypoxanthine; Kinetics; Nitrates; Nitric Oxide; Nitrogen Oxides; Spermine; Tyrosine; Xanthine Oxidase	2000
Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate. The EMBO journal, 2000, Dec-01, Volume: 19, Issue:23 Topics: Amino Acid Sequence; Anti-Bacterial Agents; Binding Sites; Carboxy-Lyases; Crystallography, X-Ray; Cysteine; Flavin Mononucleotide; Flavoproteins; Models, Molecular; Molecular Sequence Data; Oxidoreductases; Oxygen; Peptides; Protein Processing, Post-Translational; Protein Structure, Secondary; Recombinant Proteins; Ribosomes; Sequence Homology, Amino Acid; Staphylococcus epidermidis; Tyrosine	2000
Active site structure and stereospecificity of Escherichia coli pyridoxine-5'-phosphate oxidase. Journal of molecular biology, 2002, Jan-18, Volume: 315, Issue:3 Topics: Arginine; Binding Sites; Crystallization; Crystallography, X-Ray; Electron Transport; Escherichia coli; Flavin Mononucleotide; Hydrogen; Hydrogen Bonding; Kinetics; Models, Molecular; Mutation; Protein Structure, Secondary; Pyridoxal Phosphate; Pyridoxamine; Pyridoxaminephosphate Oxidase; Stereoisomerism; Substrate Specificity; Tyrosine; Water	2002
Mechanism of flavin mononucleotide cofactor binding to the Desulfovibrio vulgaris flavodoxin. 1. Kinetic evidence for cooperative effects associated with the binding of inorganic phosphate and the 5'-phosphate moiety of the cofactor. Biochemistry, 2003, Mar-04, Volume: 42, Issue:8 Topics: Alanine; Apoproteins; Asparagine; Binding Sites; Desulfovibrio vulgaris; Flavin Mononucleotide; Flavodoxin; Histidine; Kinetics; Models, Chemical; Mutagenesis, Site-Directed; Phosphates; Protein Binding; Riboflavin; Spectrometry, Fluorescence; Thermodynamics; Threonine; Tryptophan; Tyrosine	2003
Inhibition of bovine kidney low molecular mass phosphotyrosine protein phosphatase by uric acid. Journal of enzyme inhibition and medicinal chemistry, 2002, Volume: 17, Issue:5 Topics: Animals; Binding Sites; Binding, Competitive; Cattle; Enzyme Inhibitors; Flavin Mononucleotide; Kidney; Kinetics; Naphthalenes; Nitrophenols; Organophosphates; Organophosphorus Compounds; Phosphates; Protein Tyrosine Phosphatases; Substrate Specificity; Sulfhydryl Compounds; Tyrosine; Uric Acid	2002
STUDIES ON THE PHOTOINACTIVATION OF D-AMINOACID OXIDASE. The Tokushima journal of experimental medicine, 1963, Volume: 10 Topics: Chemical Phenomena; Chemistry; Coloring Agents; D-Amino-Acid Oxidase; Diphosphates; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glutathione; Histidine; Hydrogen-Ion Concentration; Light; Methylene Blue; Oxidoreductases; Riboflavin; Sulfhydryl Compounds; Temperature; Tryptophan; Tyrosine	1963
[COMPARATIVE SPECIFIC RADIOACTIVITIES OF IODINE IN THE 2 CYCLES OF IODOTHYRONINES (T-4,T-3) IN THE RAT THYROID]. Biochimica et biophysica acta, 1964, Jun-08, Volume: 86 Topics: Autoradiography; Chromatography; Diiodotyrosine; Flavin Mononucleotide; Iodides; Iodine; Iodine Isotopes; Metabolism; Radioactivity; Rats; Research; Thyroid Gland; Thyroxine; Triiodothyronine; Tyrosine	1964
ACTIVATION AND STABILIZATION OF SNAKE-VENOM 5'-NUCLEOTIDASE. Biochimica et biophysica acta, 1964, Sep-18, Volume: 89 Topics: 5'-Nucleotidase; Adenine; Adenine Nucleotides; Animals; Chemical Phenomena; Chemistry; Cytosine Nucleotides; Flavin Mononucleotide; Glycine; Guanine Nucleotides; Histidine; Leucine; Nucleotidases; Pentosephosphates; Research; Snakes; Tyrosine; Uracil Nucleotides; Venoms	1964
HEAVY-ATOM PERTURBATION, MOLECULAR COMPLEXING AND ACTIVITY OF THYROXINE. Biochimica et biophysica acta, 1965, Jan-25, Volume: 94 Topics: Antifibrinolytic Agents; Benzoates; Chemical Phenomena; Chemistry; Flavin Mononucleotide; NAD; Naphthoquinones; Pyridines; Research; Riboflavin; Spectrophotometry; Thyroxine; Tyrosine; Vitamin K	1965
[Photochemical deiodination of iodine derivatives of thyronine and tyrosine in the presence of flavin mononucleotide]. Biochimica et biophysica acta, 1961, Aug-05, Volume: 51 Topics: Flavin Mononucleotide; Halogenation; Iodides; Iodine; Thyronines; Tyrosine	1961
Chemistry. The motions of an enzyme soloist. Science (New York, N.Y.), 2003, Oct-10, Volume: 302, Issue:5643 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. Science (New York, N.Y.), 2003, Oct-10, Volume: 302, Issue:5643 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
Multiple states of the Tyr318Leu mutant of dihydroorotate dehydrogenase revealed by single-molecule kinetics. Journal of the American Chemical Society, 2004, Jun-09, Volume: 126, Issue:22 Topics: Binding Sites; Catalysis; Dihydroorotate Dehydrogenase; Escherichia coli; Flavin Mononucleotide; Kinetics; Leucine; Models, Molecular; Molecular Structure; Mutation; Oxidoreductases Acting on CH-CH Group Donors; Protein Conformation; Spectrometry, Fluorescence; Tyrosine	2004
X-ray crystal structures of Moorella thermoacetica FprA. Novel diiron site structure and mechanistic insights into a scavenging nitric oxide reductase. Biochemistry, 2005, May-03, Volume: 44, Issue:17 Topics: Binding Sites; Crystallization; Crystallography, X-Ray; Desulfovibrio gigas; Dimerization; Flavin Mononucleotide; Flavoproteins; Free Radical Scavengers; Gram-Positive Asporogenous Rods, Irregular; Histidine; Iron; Models, Molecular; Mutagenesis, Site-Directed; NADH, NADPH Oxidoreductases; Oxidoreductases; Protein Structure, Quaternary; Protein Structure, Tertiary; 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. The Journal of biological chemistry, 2006, Jun-30, Volume: 281, Issue:26 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
Folding of Desulfovibrio desulfuricans flavodoxin is accelerated by cofactor fly-casting. Archives of biochemistry and biophysics, 2006, Jul-01, Volume: 451, Issue:1 Topics: Alanine; Desulfovibrio desulfuricans; Flavin Mononucleotide; Flavodoxin; Guanidine; Kinetics; Ligands; Molecular Structure; Protein Binding; Protein Denaturation; Protein Folding; Tyrosine	2006
Crystal structure of the bacterial luciferase/flavin complex provides insight into the function of the beta subunit. Biochemistry, 2009, Jul-07, Volume: 48, Issue:26 Topics: Amino Acid Substitution; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Flavin Mononucleotide; Hydrogen Bonding; Hydroquinones; Kinetics; Luciferases, Bacterial; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Subunits; Recombinant Proteins; Tyrosine; Vibrio	2009
Exploring photoreactions between polyazaaromatic Ru(II) complexes and biomolecules by chemically induced dynamic nuclear polarization measurements. Journal of the American Chemical Society, 2009, Sep-02, Volume: 131, Issue:34 Topics: Aza Compounds; Buffers; Flavin Mononucleotide; Guanosine Monophosphate; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Organometallic Compounds; Photochemical Processes; Photosensitizing Agents; Polymers; Ruthenium; Solutions; Tyrosine; Water	2009
Photoinduced electron transfer modeling to simulate flavoprotein fluorescence decay. Methods in molecular biology (Clifton, N.J.), 2014, Volume: 1076 Topics: Carrier Proteins; Desulfovibrio vulgaris; Electron-Transferring Flavoproteins; Flavin Mononucleotide; Fluorescence; Molecular Dynamics Simulation; Photochemistry; Solutions; Tryptophan; Tyrosine	2014
Femtosecond dynamics of short-range protein electron transfer in flavodoxin. Biochemistry, 2013, Dec-23, Volume: 52, Issue:51 Topics: Amino Acid Substitution; Bacterial Proteins; Binding Sites; Desulfovibrio vulgaris; Electrons; Flavin Mononucleotide; Flavodoxin; Kinetics; Light; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Oxidation-Reduction; Photochemical Processes; Tryptophan; Tyrosine	2013
A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. The Journal of biological chemistry, 2015, Jan-02, Volume: 290, Issue:1 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
Low-cost LED-based Photo-CIDNP Enables Biocompatible Hyperpolarization of Chemphyschem : a European journal of chemical physics and physical chemistry, 2018, 10-05, Volume: 19, Issue:19 Topics: Flavin Mononucleotide; Flavins; Fluorine; Lasers; Magnetic Resonance Imaging; Magnetic Resonance Spectroscopy; Tyrosine	2018
Dynamic PEG-Peptide Hydrogels via Visible Light and FMN-Induced Tyrosine Dimerization. Advanced healthcare materials, 2018, Volume: 7, Issue:22 Topics: Amino Acid Sequence; Cell Line, Tumor; Dimerization; Flavin Mononucleotide; Humans; Hydrogels; Light; Matrix Metalloproteinase 2; Microscopy, Confocal; Peptides; Polyethylene Glycols; Tyrosine; Up-Regulation	2018