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1. 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
hypoxia | cancer | HIF‐1 | FAD biosynthesis | LSD1 | HIF-1 | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | 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 | Metabolism
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2. 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 (Easton), ISSN 0006-2960, 07/2017, Volume 56, Issue 29, pp. 3800 - 3807
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | 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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3. 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 (Washington), ISSN 0003-2700, 10/2015, Volume 87, Issue 19, pp. 9567 - 9571
Physical Sciences | Chemistry | Chemistry, Analytical | Science & Technology | 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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4. Full Text Metabolic engineering of cofactor flavin adenine dinucleotide (FAD) synthesis and regeneration in Escherichia coli for production of α‐keto acids
by Hou, Ying and Hossain, Gazi S and Li, Jianghua and Shin, Hyun‐Dong and Du, Guocheng and Chen, Jian and Liu, Long
Biotechnology and bioengineering, ISSN 0006-3592, 09/2017, Volume 114, Issue 9, pp. 1928 - 1936
α‐keto acid | formate dehydrogenase | l‐amino acid deaminase | cofactor regeneration | NADH oxidase | α-keto acid | l-amino acid deaminase | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Science & Technology | Keto Acids - isolation & purification | Metabolic Engineering - methods | Escherichia coli Proteins - metabolism | Flavin-Adenine Dinucleotide - biosynthesis | Gene Expression Regulation, Enzymologic - physiology | Keto Acids - metabolism | Gene Expression Regulation, Bacterial - physiology | Multienzyme Complexes - physiology | Escherichia coli Proteins - genetics | Flavin-Adenine Dinucleotide - genetics | Genetic Enhancement - methods | Escherichia coli - physiology | Biosynthetic Pathways - physiology | Phenylpyruvic acid | Oxidase | Adenine | Amino acids | Acid production | Metabolism | Dehydrogenase | Cofactors | Flavin-adenine dinucleotide | Engineering | Regeneration | E coli | Nicotinamide adenine dinucleotide | Ketoglutaric acid | Metabolic engineering | Formate dehydrogenase | Catalysis | Chemical synthesis | Index Medicus
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5. 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
Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | 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 | NADH | Photoreduction | Nicotinamide adenine dinucleotide | Nicotinamide | NADP | Catalysis | Photolyase | Deoxyribonucleic acid--DNA | Crystal structure | Photochemistry | Index Medicus
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6. Full Text Flavine adenine dinucleotide inhibits pathological cardiac hypertrophy and fibrosis through activating short chain acyl-CoA dehydrogenase
by Ma, Zhichao and Qin, Xue and Zhong, Xiaoyi and Liao, Yingqing and Su, Yongshao and Liu, Xi and Liu, Peiqing and Lu, Jing and Zhou, Sigui
Biochemical pharmacology, ISSN 0006-2952, 08/2020, Volume 178, pp. 114100 - 114100
Cardiac hypertrophy | Cardiac fibrosis | Flavin adenine dinucleotide | Short-chain acyl-CoA dehydrogenase | Myocardial energy metabolism | Life Sciences & Biomedicine | Pharmacology & Pharmacy | Science & Technology | Reactive Oxygen Species - metabolism | Rats, Wistar | Flavin-Adenine Dinucleotide - pharmacology | Protein Multimerization | Cardiomegaly - pathology | Male | Adenosine Triphosphate - biosynthesis | Butyryl-CoA Dehydrogenase - metabolism | Heart Failure - prevention & control | Fatty Acids, Nonesterified - metabolism | Protein Interaction Domains and Motifs | Energy Metabolism - genetics | Binding Sites | Fibroblasts - metabolism | Rats, Inbred SHR | Protein Conformation, alpha-Helical | Butyryl-CoA Dehydrogenase - genetics | Enzyme Stability | Rats | Myocardium - pathology | Cardiomegaly - enzymology | Cardiotonic Agents - pharmacology | Fibroblasts - pathology | Molecular Dynamics Simulation | Gene Expression Regulation - drug effects | Myocardium - enzymology | Reactive Oxygen Species - antagonists & inhibitors | Animals | Cardiomegaly - prevention & control | Protein Conformation, beta-Strand | Fibroblasts - drug effects | Fibrosis | Fatty Acids, Nonesterified - antagonists & inhibitors | Protein Binding | Cell Proliferation - drug effects | Cardiomegaly - genetics | Energy Metabolism - drug effects | Index Medicus
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7. Full Text Flavin Adenine Dinucleotide-Dependent Halogenase XanH and Engineering of Multifunctional Fusion Halogenases
by Kong, Lingxin and Wang, Qing and Deng, Zixin and You, Delin
Applied and environmental microbiology, ISSN 0099-2240, 09/2020, Volume 86, Issue 18
Life Sciences & Biomedicine | Microbiology | Biotechnology & Applied Microbiology | Science & Technology | Metabolic Engineering | Streptomyces - metabolism | Flavin-Adenine Dinucleotide - metabolism | Animals | Streptomyces - genetics | Escherichia coli - genetics | Bacterial Proteins - genetics | Escherichia coli - metabolism | Halogenation | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Escherichia coli Proteins - metabolism | Reductases | Protein engineering | Toxicity | Adenine | Cytotoxicity | Biosynthesis | Reducing agents | Biocatalysts | Substrates | Flavin-adenine dinucleotide | Proteins | Engineering | Flavin | NADH | Antibiotics | Substrate specificity | Nicotinamide adenine dinucleotide | Fusion protein | Flavin reductase | Index Medicus
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8. Full Text ETFDH Mutations and Flavin Adenine Dinucleotide Homeostasis Disturbance Are Essential for Developing Riboflavin‐Responsive Multiple Acyl–Coenzyme A Dehydrogenation Deficiency
by Xu, Jingwen and Li, Duoling and Lv, Jingwei and Xu, Xuebi and Wen, Bing and Lin, Pengfei and Liu, Fuchen and Ji, Kunqian and Shan, Jingli and Li, Honghao and Li, Wei and Zhao, Yuying and Zhao, Dandan and Pok, Joo Y and Yan, Chuanzhu
Annals of neurology, ISSN 0364-5134, 11/2018, Volume 84, Issue 5, pp. 659 - 673
Neurosciences | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Cell culture | Oxidoreductase | Liver | Riboflavin | Homeostasis | Electron transfer | Lipids | mRNA | High fat diet | Defects | Proteins | Ubiquinone | Protein folding | Vitamin B | Animal tissues | Fibroblasts | Coenzyme A | Ubiquinone oxidoreductase | Supplementation | Nutrient deficiency | Dietary supplements | Weight loss | Muscles | Adenine | Protein deficiency | Metabolism | Patients | Fatty acids | Carnitine | Flavin-adenine dinucleotide | Dehydrogenation | Mice | In vivo methods and tests | Mutation
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9. 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 (Washington), ISSN 0003-2700, 02/2013, Volume 85, Issue 3, pp. 1571 - 1581
Physical Sciences | Chemistry | Chemistry, Analytical | Science & Technology | 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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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
Electron transfer | Lactate utilization | NAD-independent D-lactate dehydrogenase | Iron-sulfur protein | Flavoprotein | Pseudomonas putida | Life Sciences & Biomedicine | Microbiology | Science & Technology | 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 | 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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