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1. Full Text Exceptionally high glucose current on a hierarchically structured porous carbon electrode with "wired" flavin adenine dinucleotide-dependent glucose dehydrogenase
by Tsujimura, Seiya and Murata, Kazuki and Akatsuka, Wataru
Journal of the American Chemical Society, ISSN 0002-7863, 10/2014, Volume 136, Issue 41, pp. 14432 - 14437
This article introduces a carbon electrode designed to achieve efficient enzymatic electrolysis by exploiting a hierarchical pore structure based on macropores... 
REDOX POLYMER-FILMS | BIOELECTROCATALYSIS | OXIDASE | BIOFUEL CELLS | NANOTUBES | DIFFUSION | BIOSENSOR | CHEMISTRY, MULTIDISCIPLINARY | ENZYME ELECTRODES | ELECTROPHORETIC DEPOSITION | HYDROGEL | Electrodes | Flavin-Adenine Dinucleotide - chemistry | Carbon - metabolism | Flavin-Adenine Dinucleotide - metabolism | Glucose 1-Dehydrogenase - chemistry | Glucose 1-Dehydrogenase - metabolism | Surface Properties | Glucose - chemistry | Glucose - metabolism | Molecular Structure | Porosity | Carbon - chemistry | Structure | Carbon compounds | Analysis | Magnesium oxide | Mass transfer | Electric properties | Index Medicus
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2. Full Text Regulation of hypoxia responses by flavin adenine dinucleotide‐dependent modulation of HIF‐1α protein stability
by Yang, Suk‐Jin and Park, Young Soo and Cho, Jung Hee and Moon, Byul and An, Hyun‐Jung and Lee, Ju Yeon and Xie, Zhi and Wang, Yuli and Pocalyko, David and Lee, Dong Chul and Sohn, Hyun Ahm and Kang, Minho and Kim, Jin Young and Kim, Eunhee and Park, Kyung Chan and Kim, Jung‐Ae and Yeom, Young Il
The EMBO Journal, ISSN 0261-4189, 04/2017, Volume 36, Issue 8, pp. 1011 - 1028
Oxygen deprivation induces a range of cellular adaptive responses that enable to drive cancer progression. Here, we report that lysine‐specific demethylase 1 (... 
FAD | hypoxia | cancer | HIF | LSD | biosynthesis | HIF-1 | FAD biosynthesis | LSD1 | INDUCIBLE FACTOR | STEM-CELLS | METHYLATION | LYSINE DEMETHYLASE LSD1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION | HIF1-ALPHA | CELL BIOLOGY | BREAST-CANCER | PATHWAY | DEGRADATION | BINDING | Human Umbilical Vein Endothelial Cells - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - genetics | Humans | Gene Expression Regulation | Histone Demethylases - genetics | Cell Hypoxia | Flavin-Adenine Dinucleotide - metabolism | Histone Demethylases - metabolism | Ubiquitination | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | Human Umbilical Vein Endothelial Cells - pathology | Flavin-Adenine Dinucleotide - genetics | Protein Stability | Index Medicus | Post-translational Modifications, Proteolysis & Proteomics | HIF‐1 | Metabolism
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3. Full Text Nicotinamide Adenine Dinucleotides Arrest Photoreduction of Class II DNA Photolyases in FADH˙ State
by Ignatz, Elisabeth and Geisselbrecht, Yann and Kiontke, Stephan and Essen, Lars‐Oliver
Photochemistry and Photobiology, ISSN 0031-8655, 01/2018, Volume 94, Issue 1, pp. 81 - 87
All light‐sensitive members of the photolyase/cryptochrome family rely on FAD as catalytic cofactor. Its activity is regulated by photoreduction, a... 
SITE | ELECTRON-TRANSFER | ARABIDOPSIS CRYPTOCHROME | BIOPHYSICS | PHOTORECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | Archaeal Proteins - metabolism | Deoxyribodipyrimidine Photo-Lyase - chemistry | Methanosarcina - enzymology | Deoxyribodipyrimidine Photo-Lyase - genetics | Electron Transport | Oxidation-Reduction | Molecular Conformation | Archaeal Proteins - chemistry | Deoxyribodipyrimidine Photo-Lyase - metabolism | Tryptophan - metabolism | Flavin-Adenine Dinucleotide - metabolism | Light | Archaeal Proteins - genetics | Kinetics | Mutation | NADP - metabolism | NAD - metabolism | NADPH | Tryptophan | Electron transfer | Cofactors | Flavin-adenine dinucleotide | Flavin | NADH | Photoreduction | Nicotinamide adenine dinucleotide | Nicotinamide | NADP | Catalysis | Photolyase | Deoxyribonucleic acid--DNA | Crystal structure | Photochemistry | Index Medicus
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4. Full Text Biocomposite Based on Reduced Graphene Oxide Film Modified with Phenothiazone and Flavin Adenine Dinucleotide-Dependent Glucose Dehydrogenase for Glucose Sensing and Biofuel Cell Applications
by Ravenna, Yehonatan and Xia, Lin and Gun, Jenny and Mikhaylov, Alexey A and Medvedev, Alexander G and Lev, Ovadia and Alfonta, Lital
Analytical Chemistry, ISSN 0003-2700, 09/2015, Volume 87, Issue 19, pp. 9567 - 9571
A novel composite material for the encapsulation of redox enzymes was prepared. Reduced graphene oxide film with adsorbed phenothiazone was used as a highly... 
PLATFORM | BURKHOLDERIA-CEPACIA | CATALYTIC SUBUNIT | CHEMISTRY, ANALYTICAL | BIOSENSORS | GLASSY-CARBON ELECTRODE | ESCHERICHIA-COLI | DIRECT ELECTROCHEMISTRY | HYDROGEN-PEROXIDE | HORSERADISH-PEROXIDASE | EXPRESSION | Biocompatible Materials - metabolism | Oxidation-Reduction | Biocompatible Materials - chemistry | Bioelectric Energy Sources | Glucose 1-Dehydrogenase - metabolism | Oxides - chemistry | Electrodes | Flavin-Adenine Dinucleotide - metabolism | Phenothiazines - chemistry | Phenothiazines - metabolism | Biosensing Techniques | Graphite - metabolism | Glucose - metabolism | Graphite - chemistry | Glucose - analysis | Oxides - metabolism | Usage | Chemical properties | Biosensors | Flavin adenine dinucleotide | Graphene | Enzymes | Composite materials | Fuel cells | Electron transfer | Oxidation | Glucose | Index Medicus | Analytical chemistry | Oxide coatings | Adenines
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5. Full Text Influence of surface adsorption on the interfacial electron transfer of flavin adenine dinucleotide and glucose oxidase at carbon nanotube and nitrogen-doped carbon nanotube electrodes
by Goran, Jacob M and Mantilla, Sandra M and Stevenson, Keith J
Analytical Chemistry, ISSN 0003-2700, 02/2013, Volume 85, Issue 3, pp. 1571 - 1581
The adsorption of flavin adenine dinucleotide (FAD) and glucose oxidase (GOx) onto carbon nanotube (CNT) and nitrogen-doped CNT (N-CNT) electrodes was... 
CONNECTION | CHEMISTRY, ANALYTICAL | ELECTROCHEMICAL PROPERTIES | BEHAVIOR | DISPERSION | FAD | GLASSY-CARBON | REDOX ENZYMES | CYCLIC VOLTAMMETRY | AMPEROMETRIC BIOSENSORS | POTENTIAL SWEEP VOLTAMMETRY | Electrodes | Flavin-Adenine Dinucleotide - chemistry | Glucose Oxidase - chemistry | Flavin-Adenine Dinucleotide - metabolism | Glucose Oxidase - metabolism | Nitrogen - metabolism | Adsorption - physiology | Nitrogen - chemistry | Nanotubes, Carbon - chemistry | Surface Properties | Electron Transport - physiology | Research | Adsorption | Electron transport | Flavin adenine dinucleotide | Structure | Nanotubes | Electron transfer | Glucose | Nitrogen | Index Medicus
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6. Full Text Rate enhancement of bacterial extracellular electron transport involves bound flavin semiquinones
by Akihiro Okamoto and Kazuhito Hashimoto and Kenneth H. Nealson and Ryuhei Nakamura
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2013, Volume 110, Issue 19, pp. 7856 - 7861
Extracellular redox-active compounds, flavins and other quinones, have been hypothesized to play a major role in the delivery of electrons from cellular... 
Electrodes | Lactates | Protein metabolism | Biofilms | Cellular metabolism | Voltammetry | Cytochromes | Shewanella | Electric current | Electrons | Microbial fuel cell | Flavin mononucleotide | Electromicrobiology | Iron-reducing bacteria | Whole-cell voltammetry | FLAVODOXIN | MULTIDISCIPLINARY SCIENCES | electromicrobiology | C-TYPE CYTOCHROME | microbial fuel cell | IRON | whole-cell voltammetry | OUTER-MEMBRANE CYTOCHROMES | flavin mononucleotide | THERMODYNAMICS | REDUCTION | iron-reducing bacteria | SHEWANELLA-ONEIDENSIS MR-1 | DESULFOVIBRIO-VULGARIS HILDENBOROUGH | MICROBIAL FUEL-CELLS | PUTREFACIENS MR-1 | Electron Transport | Heme - metabolism | Electron Spin Resonance Spectroscopy | Oxidation-Reduction | Cytochromes c - metabolism | Nucleotides - genetics | Flavin-Adenine Dinucleotide - analogs & derivatives | Shewanella - physiology | Shewanella - metabolism | Cytochrome c Group - metabolism | Flavin-Adenine Dinucleotide - metabolism | Microscopy, Confocal | Flavin Mononucleotide - secretion | Electrochemistry | Quinone | Physiological aspects | Extracellular matrix | Research | Electron transport | Health aspects | Proteins | Bacteria | Diffusion | Cells | Index Medicus | Biological Sciences
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7. Full Text Enzyme-Mediated Conversion of Flavin Adenine Dinucleotide (FAD) to 8-Formyl FAD in Formate Oxidase Results in a Modified Cofactor with Enhanced Catalytic Properties
by Robbins, John M and Souffrant, Michael G and Hamelberg, Donald and Gadda, Giovanni and Bommarius, Andreas S
Biochemistry, ISSN 0006-2960, 07/2017, Volume 56, Issue 29, pp. 3800 - 3807
Flavins, including flavin adenine dinucleotide (FAD), are fundamental catalytic cofactors that are responsible for the redox functionality of a diverse set of... 
RIBOFLAVIN | SITE | SUCCINATE-DEHYDROGENASE | COVALENTLY-BOUND FLAVIN | BIOSYNTHESIS | FMN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FORCE-FIELD | VERSATILITY | CHOLINE OXIDOREDUCTASE FAMILY | Flavin-Adenine Dinucleotide - chemistry | Fungal Proteins - chemistry | Oxidoreductases Acting on Aldehyde or Oxo Group Donors - chemistry | Mutagenesis, Site-Directed | Oxidoreductases Acting on Aldehyde or Oxo Group Donors - metabolism | Fungal Proteins - genetics | Mutation, Missense | Flavin Mononucleotide - chemistry | Coenzymes - metabolism | Flavin-Adenine Dinucleotide - metabolism | Aspergillus oryzae - genetics | Aspergillus oryzae - enzymology | Kinetics | Oxidoreductases Acting on Aldehyde or Oxo Group Donors - genetics | Coenzymes - chemistry | Circular Dichroism | Amino Acid Substitution | Flavin Mononucleotide - metabolism | Fungal Proteins - metabolism | Chemical mutagenesis | Usage | Research | Flavin adenine dinucleotide | Mass spectrometry | Index Medicus
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8. Full Text Genetic dissection of Flaviviridae host factors through genome-scale CRISPR screens
by Marceau, Caleb D and Puschnik, Andreas S and Majzoub, Karim and Ooi, Yaw Shin and Brewer, Susan M and Fuchs, Gabriele and Swaminathan, Kavya and Mata, Miguel A and Elias, Joshua E and Sarnow, Peter and Carette, Jan E
Nature, ISSN 0028-0836, 07/2016, Volume 535, Issue 7610, pp. 159 - 163
The Flaviviridae are a family of viruses that cause severe human diseases. For example, dengue virus (DENV) is a rapidly emerging pathogen causing an estimated... 
REPLICATION | PROTEIN | HEPATITIS-C VIRUS | HUR | HUMAN-CELLS | MEMBRANE | MULTIDISCIPLINARY SCIENCES | INFECTION | N-GLYCOSYLATION | OLIGOSACCHARYLTRANSFERASE | DENGUE VIRUS | Endoplasmic Reticulum-Associated Degradation | Hexosyltransferases - deficiency | RNA-Binding Proteins - genetics | Humans | Endoplasmic Reticulum - metabolism | Flavivirus Infections - genetics | Hexosyltransferases - metabolism | Receptors, Virus - genetics | Molecular Targeted Therapy | Flavin-Adenine Dinucleotide - metabolism | Membrane Proteins - deficiency | Hepacivirus - physiology | Membrane Proteins - metabolism | Zika Virus - metabolism | Membrane Proteins - genetics | Hexosyltransferases - genetics | Flavin-Adenine Dinucleotide - biosynthesis | Glycosylation | CRISPR-Cas Systems - genetics | Drug Discovery | Genome, Human - genetics | Protein Sorting Signals | Dengue Virus - growth & development | Host-Derived Cellular Factors - genetics | Dengue Virus - genetics | Host-Pathogen Interactions - genetics | Virus Replication | Protein Binding | Dengue Virus - physiology | Flavivirus Infections - virology | Viral Nonstructural Proteins - metabolism | Genetic aspects | Host-virus relationships | Nucleotide sequencing | Methods | DNA sequencing | Proteins | Enzymes | MicroRNAs | Genes | Viruses | Genomes | Mutation | Index Medicus
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9. Full Text Sirtuin 3 (SIRT3) protein regulates long-chain acyl-CoA dehydrogenase by deacetylating conserved lysines near the active site
by Bharathi, Sivakama S and Zhang, Yuxun and Mohsen, Al-Walid and Uppala, Radha and Balasubramani, Manimalha and Schreiber, Emanuel and Uechi, Guy and Beck, Megan E and Vockley, Jerry and Rardin, Matthew J and Verdin, Eric and Gibson, Bradford W and Hirschey, Matthew D and Goetzman, Eric S
Journal of Biological Chemistry, ISSN 0021-9258, 11/2013, Volume 288, Issue 47, pp. 33837 - 33847
Long-chain acyl-CoA dehydrogenase (LCAD) is a key mitochondrial fatty acid oxidation enzyme. We previously demonstrated increased LCAD lysine acetylation in... 
Sirtuins | OXIDATION | MECHANISM | ACETYLATION | ACYLATION | Enzyme Catalysis | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAD | Acyl-CoA Dehydrogenase | Mitochondria | METABOLISM | Electron Transfer | PLAYS | ENZYMES | Lysine Acetylation | Fatty Acid Oxidation | Posttranslational Modification | ACETYLOME | CALORIE RESTRICTION | PROTEOMICS | Flavin-Adenine Dinucleotide - chemistry | Mitochondria, Liver - genetics | Recombinant Proteins - metabolism | Sirtuin 3 - genetics | Fatty Acids - chemistry | Sirtuin 3 - metabolism | Oxidation-Reduction | Humans | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Catalytic Domain - physiology | Mitochondria, Liver - enzymology | Mice, Knockout | Flavin-Adenine Dinucleotide - metabolism | Animals | Fatty Acids - genetics | Acyl-CoA Dehydrogenase, Long-Chain | Sirtuin 3 - chemistry | Mice | Acetylation | Flavin-Adenine Dinucleotide - genetics | Fatty Acids - metabolism | Index Medicus | Metabolism
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10. Full Text A bacterial multidomain NAD-independent D-lactate dehydrogenase utilizes flavin adenine dinucleotide and Fe-S clusters as cofactors and quinone as an electron acceptor for D-lactate oxidization
by Jiang, Tianyi and Guo, Xiaoting and Yan, Jinxin and Zhang, Yingxin and Wang, Yujiao and Zhang, Manman and Sheng, Binbin and Ma, Cuiqing and Xu, Ping and Gao, Chao
Journal of Bacteriology, ISSN 0021-9193, 2017, Volume 199, Issue 22
Bacterial membrane-associated NAD-independent D-lactate dehydrogenase (Fe-S D-iLDH) oxidizes D-lactate into pyruvate. A sequence analysis of the enzyme reveals... 
Electron transfer | Lactate utilization | NAD-independent D-lactate dehydrogenase | Iron-sulfur protein | Flavoprotein | Pseudomonas putida | RESPIRATORY ENZYME | ESCHERICHIA-COLI | MICROBIOLOGY | lactate utilization | REFINED STRUCTURE | 4FE-4S CLUSTER | GLUCONOBACTER-OXYDANS | GLYCOLATE OXIDASE | DEPENDENT MONOOXYGENASE | electron transfer | flavoprotein | FLAVOCYTOCHROME B | iron-sulfur protein | PSEUDOMONAS-STUTZERI STRAIN | BOUND L-LACTATE | Lactate Dehydrogenases - metabolism | Coenzymes | Lactate Dehydrogenases - isolation & purification | Mutagenesis, Site-Directed | Oxidation-Reduction | Cytochromes c - metabolism | Lactic Acid - metabolism | Ubiquinone - analogs & derivatives | Bacterial Proteins - genetics | Ubiquinone - metabolism | Pseudomonas putida - enzymology | Lactate Dehydrogenases - genetics | Flavin-Adenine Dinucleotide - metabolism | Bacterial Proteins - metabolism | Iron-Sulfur Proteins - metabolism | NAD - metabolism | Electrons | Quinones - metabolism | Cytochrome c | Quinone | Reports | Oxidoreductases | Research | Nucleotides | Iron-sulfur proteins | Cytochrome | Dehydrogenases | Oxidoreductase | Pyruvic acid | Iron | Dehydrogenase | Cofactors | Flavin | Coenzyme Q10 | Bacteria | Oxidation | Catalysis | Carbon sources | Nucleotide sequence | Adenine | Lactate dehydrogenase | L-Lactate dehydrogenase | Flavin-adenine dinucleotide | NAD | D-Lactate dehydrogenase | Utilization | Mutagenesis | Site-directed mutagenesis | Lactic acid | Index Medicus
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11. Full Text Flavin Adenine Dinucleotide and N-5,N-10-Methenyltetrahydrofolate are the in planta Cofactors of Arabidopsis thaliana Cryptochrome 3
by Gobel, T and Reisbacher, S and Batschauer, A and Pokorny, R
PHOTOCHEMISTRY AND PHOTOBIOLOGY, ISSN 0031-8655, 01/2017, Volume 93, Issue 1, pp. 355 - 362
Members of the cryptochrome/photolyase family (CPF) of proteins utilize noncovalently bound light-absorbing cofactors for their biological function. Usually,... 
PHOTOREACTIVATING ENZYME | ELECTRON-TRANSFER | BIOPHYSICS | BLUE-LIGHT PHOTORECEPTOR | THYMINE-DIMER | CRYSTAL-STRUCTURE | SPECTROSCOPIC PROPERTIES | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | COLI DNA PHOTOLYASE | FLUORESCENT MODIFICATION | CYCLOBUTANE PYRIMIDINE DIMER | Green Fluorescent Proteins - metabolism | Arabidopsis - enzymology | Immunoprecipitation | Cryptochromes - genetics | Spectrometry, Fluorescence | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Tetrahydrofolates - metabolism | Chromatography, Reverse-Phase | Flavin-Adenine Dinucleotide - metabolism | Escherichia coli - genetics | Plants, Genetically Modified | Recombinant Fusion Proteins - genetics | Cryptochromes - metabolism
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12. Full Text Enantioselective Hydrogen Atom Transfer: Discovery of Catalytic Promiscuity in Flavin-Dependent 'Ene'-Reductases
by Sandoval, Braddock A and Meichan, Andrew J and Hyster, Todd K
Journal of the American Chemical Society, ISSN 0002-7863, 08/2017, Volume 139, Issue 33, pp. 11313 - 11316
Flavin has long been known to function as a single electron reductant in biological settings, but this reactivity has rarely been observed with flavoproteins... 
ORGANIC-CHEMISTRY | ELECTRON-TRANSFER | CHEMISTRY, MULTIDISCIPLINARY | OLD YELLOW ENZYME | BIOCATALYSIS | HYDRIDE | Electron Transport | Gluconobacter oxydans - enzymology | Oxidation-Reduction | Oxidoreductases - metabolism | Stereoisomerism | Models, Molecular | Esters - metabolism | Flavin-Adenine Dinucleotide - analogs & derivatives | Flavin-Adenine Dinucleotide - metabolism | Gluconobacter oxydans - metabolism | Halogenation | NADP - metabolism | Hydrogen - metabolism | Flavins - metabolism | Index Medicus
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13. Full Text An algal photoenzyme converts fatty acids to hydrocarbons
by Sorigué, Damien and Légeret, Bertrand and Cuiné, Stéphan and Blangy, Stéphanie and Moulin, Solène and Billon, Emmanuelle and Richaud, Pierre and Brugière, Sabine and Couté, Yohann and Nurizzo, Didier and Müller, Pavel and Brettel, Klaus and Pignol, David and Arnoux, Pascal and Li-Beisson, Yonghua and Peltier, Gilles and Beisson, Fred
Science, ISSN 0036-8075, 09/2017, Volume 357, Issue 6354, pp. 903 - 907
Although many organisms capture or respond to sunlight, few enzymes are known to be driven by light. Among these are DNA photolyases and the photosynthetic... 
MICROBIAL BIOSYNTHESIS | PATHWAY | PHOTOLYASE | ENZYMES | MULTIDISCIPLINARY SCIENCES | LIGHT | OXIDOREDUCTASE | MECHANISMS | DNA-REPAIR | PROTEINS | PHOTORECEPTORS | Carboxy-Lyases - classification | Chlorella - enzymology | Biocatalysis | Oxidoreductases - metabolism | Oxidoreductases - radiation effects | Oxidoreductases - classification | Lipid Metabolism | Carboxy-Lyases - chemistry | Phylogeny | Oxidoreductases - chemistry | Photochemical Processes | Flavin-Adenine Dinucleotide - metabolism | Alkanes - metabolism | Plant Proteins - classification | Plant Proteins - chemistry | Light | Carboxy-Lyases - radiation effects | Plant Proteins - radiation effects | Carboxy-Lyases - metabolism | Plant Proteins - metabolism | Fatty Acids - metabolism | Alkenes - metabolism | Hydrocarbons | Chemical properties | Enzyme kinetics | Observations | Fatty acids | Algae | Alkenes | Oxidoreductase | Escherichia coli | Alkanes | Glucose | Hydrophobicity | Flavin | Lipid metabolism | Catalysis | N-Alkanes | Deoxyribonucleic acid--DNA | Crystal structure | Enzymes | Adenine | Photons | Metabolism | Substrates | Flavin-adenine dinucleotide | Reaction centers | Decarboxylation | Choline | Photosynthesis | Protein structure | Binding sites | Index Medicus | Life Sciences | Cellular Biology
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14. Full Text Electron mediators accelerate the microbiologically influenced corrosion of 304 stainless steel by the Desulfovibrio vulgaris biofilm
by Zhang, Peiyu and Xu, Dake and Li, Yingchao and Yang, Ke and Gu, Tingyue
Bioelectrochemistry, ISSN 1567-5394, 02/2015, Volume 101, pp. 14 - 21
In the microbiologically influenced corrosion (MIC) caused by sulfate reducing bacteria (SRB), iron oxidation happens outside sessile cells while the... 
Biofilm | Electron transfer | Electron mediator | SRB | Biocorrosion | ELECTROCHEMISTRY | BIOCHEMISTRY & MOLECULAR BIOLOGY | IRON | CARBON-STEEL | FLAVINS | BIOPHYSICS | BIOLOGY | MICROBIAL FUEL-CELLS | SULFATE-REDUCING BACTERIA | Biofilms - drug effects | Microscopy, Electron, Scanning | Sulfates - metabolism | Oxidation-Reduction | Stainless Steel - chemistry | Flavin-Adenine Dinucleotide - pharmacology | Riboflavin - pharmacology | Flavin-Adenine Dinucleotide - metabolism | Desulfovibrio vulgaris - physiology | Corrosion | Riboflavin - metabolism | Plankton - microbiology | Desulfovibrio vulgaris - drug effects | Electrons | Steel | Sulfates | Steel, Stainless | Index Medicus
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15. Full Text Generalized langevin equation with fractional gaussian noise: Subdiffusion within a single protein molecule
by Kou, S.C and Xie, X. Sunney
Physical Review Letters, ISSN 0031-9007, 10/2004, Volume 93, Issue 18, pp. 1 - 180603
By introducing fractional Gaussian noise into the generalized Langevin equation, the subdiffusion of a particle can be described as a stationary Gaussian... 
BROWNIAN-MOTION | ANOMALOUS DIFFUSION | ELECTRON-TRANSFER | MODELS | PHYSICS, MULTIDISCIPLINARY | KINETICS | EQUILIBRIUM | DYNAMICS | Flavin-Adenine Dinucleotide - chemistry | Flavin-Adenine Dinucleotide - metabolism | Tyrosine - metabolism | FMN Reductase - metabolism | Models, Chemical | FMN Reductase - chemistry | Fluorescence | Models, Molecular | Protein Conformation | Tyrosine - chemistry | Index Medicus
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