Suchergebnisse - "Flavin-Adenine Dinucleotide/metabolism"

Cryo-EM structures of the MnmE–MnmG complex reveal large conformational changes and provide new insights into the mechanism of tRNA modification

Autoren: Laila Maes Israel Mares-Mejía Ella Martin et al.

Weitere Verfasser: Laila Maes Israel Mares-Mejía Ella Martin et al.

Quelle: Nucleic Acids Research. 53

Schlagwörter: Models, Molecular, RNA, Transfer/metabolism, Methyltransferases/chemistry, Protein Conformation, Flavin-Adenine Dinucleotide/metabolism, Escherichia coli Proteins/chemistry, Cryoelectron Microscopy, NAD/metabolism, Protein Binding, GTP Phosphohydrolases

Zugangs-URL: https://biblio.vub.ac.be/vubir/cryoem-structures-of-the-mnmemnmg-complex-reveal-large-conformational-changes-and-provide-new-insights-into-the-mechanism-of-trna-modification(e0a1d23a-e82f-4641-8e99-f03cd8c1729f).html

Essential elements of radical pair magnetosensitivity in Drosophila

Autoren: Adam A. Bradlaugh Giorgio Fedele Anna L. Munro et al.

Quelle: Nature
Bradlaugh, A A, Fedele, G, Munro, A L, Hansen, C N, Hares, J M, Patel, S, Kyriacou, C P, Jones, A R, Rosato, E & Baines, R A 2023, 'Essential elements of radical pair magnetosensitivity in Drosophila', Nature, vol. 615, pp. 111-116. https://doi.org/10.1038/s41586-023-05735-z

Schlagwörter: Neurons, 0301 basic medicine, Behavior, 0303 health sciences, Behavior, Animal, Animal, Flavin-Adenine Dinucleotide/metabolism, Tryptophan/metabolism, Tryptophan, Article, Cryptochromes/chemistry, Cryptochromes, Electrophysiology, Neurons/cytology, 03 medical and health sciences, Drosophila melanogaster, Magnetic Fields, Flavin-Adenine Dinucleotide, Drosophila melanogaster/chemistry, Animals, Drosophila, Single-Cell Analysis

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/36813962
https://research.manchester.ac.uk/en/publications/9a4e6ea6-4a7c-4d96-a800-cb2a11e2ae8b
https://doi.org/10.1038/s41586-023-05735-z
https://hdl.handle.net/20.500.11770/380458
https://doi.org/10.1038/s41586-023-05735-z

A new era for electron bifurcation

Autoren: R. Brian Dyer Peng Zhang David W. Mulder et al.

Weitere Verfasser: R. Brian Dyer Peng Zhang David W. Mulder et al.

Quelle: Current Opinion in Chemical Biology. 47:32-38

Schlagwörter: 0301 basic medicine, Flavin-Adenine Dinucleotide - analogs & derivatives, Flavin-Adenine Dinucleotide - chemistry, Hydroquinones - metabolism, Mitochondria - metabolism, Mitochondria - chemistry, Electron Transport Chain Complex Proteins - chemistry, Flavin-Adenine Dinucleotide - metabolism, Benzoquinones - chemistry, Electron Transport, Medicinal and Biomolecular Chemistry, 03 medical and health sciences, Benzoquinones - metabolism, Medicinal and biomolecular chemistry, Benzoquinones, eredox, NAD - chemistry, 0303 health sciences, Organic Chemistry, Biological Sciences, electron transfer, Electron Transport Chain Complex Proteins - metabolism, NAD, 6. Clean water, Hydroquinones, Mitochondria, Electron Transport Chain Complex Proteins, electron bifurcation, Biochemistry and cell biology, Flavin-Adenine Dinucleotide, NAD - metabolism, Biochemistry and Cell Biology, Hydroquinones - chemistry, Oxidation-Reduction

Dateibeschreibung: application/pdf; pdf

Zugangs-URL: https://www.osti.gov/biblio/1465646
https://pubmed.ncbi.nlm.nih.gov/30077080
https://khepri-node.dev.meta-infra.org/papers/a-new-era-for-electron-bifurcation/30077080
https://europepmc.org/article/MED/30077080
https://www.ncbi.nlm.nih.gov/pubmed/30077080
https://experts.illinois.edu/en/publications/a-new-era-for-electron-bifurcation
https://pubmed.ncbi.nlm.nih.gov/30077080/
https://asu.pure.elsevier.com/en/publications/a-new-era-for-electron-bifurcation
https://escholarship.org/uc/item/0z74p706

Lysine-Specific Histone Demethylase 1A Regulates Macrophage Polarization and Checkpoint Molecules in the Tumor Microenvironment of Triple-Negative Breast Cancer

Autoren: Tan, Abel H Y Tu, WenJuan McCuaig, Robert et al.

Quelle: Frontiers in Immunology

Schlagwörter: Animals, Cell Differentiation, Co-Repressor Proteins/metabolism, Cytokines/metabolism, Disease Models, Animal, Flavin-Adenine Dinucleotide/metabolism, Histone Demethylases/antagonists & inhibitors, Humans, Macrophage Activation, Macrophages/immunology, Mice, Nerve Tissue Proteins/metabolism, Phenelzine/pharmacology, RAW 264.7 Cells, RNA, Small Interfering/genetics, Snail Family Transcription Factors/metabolism, Th1 Cells/immunology, Triple Negative Breast Neoplasms/immunology, Tumor Microenvironment

Dateibeschreibung: application/pdf

Relation: https://eprints.qut.edu.au/210042/1/fimmu_10_01351.pdf; https://eprints.qut.edu.au/210042/

Verfügbarkeit: https://doi.org/10.3389/fimmu.2019.01351
https://eprints.qut.edu.au/210042/

Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase

Autoren: Volkers, G. Palm, G. J. Weiss, M. S. et al.

Quelle: FEBS letters 585, 1061-1066 (2011). doi:10.1016/j.febslet.2011.03.012

Schlagwörter: Models, Molecular, 0301 basic medicine, Antibiotic resistance, TetX, Crystallography, X-Ray, Tigecycline, Mixed Function Oxygenases: metabolism, Mixed Function Oxygenases, 03 medical and health sciences, Oxygen: metabolism, Bacteroides, Tetracycline: metabolism, 0303 health sciences, Bacteroides: drug effects, Binding Sites, Flavin, Tetracycline Resistance, Mixed Function Oxygenases: chemistry, Tetracycline, Bacteroides: enzymology, Tetracycline degradation, Protein Structure, Tertiary, 3. Good health, Oxygen, Flavin-Adenine Dinucleotide: metabolism, Flavin-Adenine Dinucleotide, Tetracycline: pharmacology

Zugangs-URL: https://febs.onlinelibrary.wiley.com/doi/pdfdirect/10.1016/j.febslet.2011.03.012
https://pubmed.ncbi.nlm.nih.gov/21402075
https://febs.onlinelibrary.wiley.com/doi/full/10.1016/j.febslet.2011.03.012
https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2011.03.012
https://europepmc.org/abstract/MED/21402075
https://pubag.nal.usda.gov/catalog/982976
http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2011.03.012/full?scrollTo=references
http://www.sciencedirect.com/science/article/pii/S0014579311001657
https://bib-pubdb1.desy.de/record/94982

Severe X-Linked Mitochondrial Encephalomyopathy Associated with a Mutation in Apoptosis-Inducing Factor

Autoren: Ghezzi D. Sevrioukova I. Invernizzi F. et al.

Weitere Verfasser: Ghezzi D. Sevrioukova I. Invernizzi F. et al.

Quelle: The American Journal of Human Genetics. 86:639-649

Schlagwörter: Male, 0301 basic medicine, DNA Primer, Protein Conformation, Riboflavin, Apoptosis, Mitochondrial Encephalomyopathies: genetic, Gene, MITOCHONDRIAL, Mitochondrial Encephalomyopathie, Apoptosis Inducing Factor, Apoptosis Inducing Factor: genetics, Apoptosis Inducing Factor: metabolism, Caspase 3, Caspase 3: metabolism, Computer Simulation, DNA, DNA Primers, DNA Primers: chemistry, Dietary Supplements, Electron Transport, Electron Transport: physiology, Female, Fibroblasts, Fibroblasts: cytology, Fibroblasts: drug effects, Fibroblasts: metabolism, Flavin-Adenine Dinucleotide, Flavin-Adenine Dinucleotide: metabolism, Genes, Humans, In Situ Nick-End Labeling, Infant, Magnetic Resonance Imaging, Mitochondrial, Mitochondrial Encephalomyopathies, Mitochondrial Encephalomyopathies: genetics, Mitochondrial Encephalomyopathies: metabolism, Mitochondrial Encephalomyopathies: pathology, Mitochondrial: genetics, Mitochondrial: metabolism, Monozygotic, Muscle, Mutation, Mutation: genetics, Nervous System Diseases, Nervous System Diseases: drug therapy, Nervous System Diseases: etiology, Newborn, Pedigree, Poly(ADP-ribose) Polymerases, Poly(ADP-ribose) Polymerases: metabolism, Riboflavin: administration \& dosage, Skeletal, Skeletal: cytology, Skeletal: drug effects, Skeletal: metabolism, Staurosporine, Staurosporine: pharmacology, Twins, X-Linked, ENCEPHALOMYOPATHY, Genes, X-Linked, Genetics(clinical), Mutation: genetic, X-LINKED, Nervous System Disease, Poly(ADP-ribose) Polymerase, 0303 health sciences, Fibroblast, Human, DNA, Mitochondrial, Infant, Newborn, Muscle, Skeletal, Poly (ADP-Ribose) Polymerase-1, Twins, Monozygotic, Fibroblasts: drug effect, 03 medical and health sciences, Genetics, Skeletal: drug effect, Apoptosis Inducing Factor: genetic, Dietary Supplement, Mitochondrial: genetic, Apoptosi, Twin

Dateibeschreibung: STAMPA; application/pdf

Zugangs-URL: http://www.cell.com/article/S000292971000145X/pdf
https://pubmed.ncbi.nlm.nih.gov/20362274
http://hdl.handle.net/11368/2489177
https://www.sciencedirect.com/science/article/abs/pii/S000292971000145X
https://www.cell.com/ajhg/fulltext/S0002-9297(10)00145-X
http://europepmc.org/abstract/MED/20362274
https://pubmed.ncbi.nlm.nih.gov/20362274/
https://www.sciencedirect.com/science/article/pii/S000292971000145X
https://www.pubmedcentral.nih.gov/pmc/articles/PMC2850437/
https://hdl.handle.net/2434/826589
https://doi.org/10.1016/j.ajhg.2010.03.002
https://hdl.handle.net/11577/3354276
https://doi.org/10.1016/j.ajhg.2010.03.002

Sequence–structure–function analysis of the bifunctional enzyme MnmC that catalyses the last two steps in the biosynthesis of hypermodified nucleoside mnm5s2U in tRNA

Autoren: Martine Roovers Joël Caillet Janusz Marek Bujnicki et al.

Weitere Verfasser: Martine Roovers Joël Caillet Janusz Marek Bujnicki et al.

Quelle: Proteins: Structure, Function, and Bioinformatics. 71:2076-2085

Schlagwörter: Models, Molecular, 0301 basic medicine, Secondary, Protein Folding, Sequence Homology, Ligands, Multienzyme Complexes -- analysis, Protein Structure, Secondary, RNA, Transfer, Computational Biology -- methods, Models, Escherichia coli Proteins -- chemistry, Conserved Sequence, Sequence Deletion, 0303 health sciences, Escherichia coli Proteins, Multienzyme Complexes -- genetics, Sciences bio-médicales et agricoles, Bacterial -- biosynthesis, Amino Acid, RNA, Bacterial, Flavin-Adenine Dinucleotide -- metabolism, Thiouridine -- metabolism, Escherichia coli Proteins -- genetics, Flavin-Adenine Dinucleotide, Sequence Analysis, Protein Binding, Protein Structure, Thiouridine -- analogs & derivatives, Static Electricity, Molecular Sequence Data, Methylation, Catalysis, Structure-Activity Relationship, 03 medical and health sciences, Transfer -- biosynthesis, Multienzyme Complexes, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Escherichia coli Proteins -- metabolism, Binding Sites, Genetic Complementation Test, Molecular, Computational Biology, Multienzyme Complexes -- chemistry, Protein Structure, Tertiary, Escherichia coli Proteins -- analysis, Amino Acid Substitution, RNA, Multienzyme Complexes -- metabolism, Tertiary

Dateibeschreibung: 1 full-text file(s): application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/18186482
https://hal.science/hal-00310550v1
https://www.onlinelibrary.wiley.com/doi/abs/10.1002/prot.21918
https://www.ncbi.nlm.nih.gov/pubmed/18186482
https://www.onlinelibrary.wiley.com/doi/10.1002/prot.21918
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/50477/Details
http://europepmc.org/abstract/MED/18186482

Further insights into the tRNA modification process controlled by proteins MnmE and GidA of Escherichia coli.

Autoren: Yim, Lucía Moukadiri, Ismaïl Björk, Glenn et al.

Quelle: Nucleic Acids Res. 34(20):5892-905

Schlagwörter: Antibodies, Bacterial/biosynthesis/immunology, Bacterial Proteins/analysis/chemistry/*metabolism, Escherichia coli/genetics/metabolism, Escherichia coli Proteins/*metabolism, Flavin-Adenine Dinucleotide/metabolism, GTP Phosphohydrolases/*metabolism, Mutation, Phenotype, Protein Structure, Tertiary, RNA Processing, Post-Transcriptional, RNA, Transfer/chemistry/*metabolism, Uridine/*metabolism

Dateibeschreibung: print

Zugangs-URL: https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-16729

FAD Is a Preferred Substrate and an Inhibitor ofEscherichia coli General NAD(P)H:Flavin Oxidoreductase

Autoren: Louie, Tai Man Yang, Haw Karnchanaphanurach, Pallop et al.

Quelle: Journal of Biological Chemistry. 277:39450-39455

Schlagwörter: 0301 basic medicine, Flavin-Adenine Dinucleotide - chemistry, Escherichia coli - metabolism, Time Factors, FMN Reductase, Protein Conformation, Chemical, Electrons, Flavin-Adenine Dinucleotide - metabolism, Fluorescence, Mass Spectrometry, Dose-Response Relationship, 03 medical and health sciences, Models, Escherichia coli, Enzyme Inhibitors, Chromatography, High Pressure Liquid, Chromatography, 0303 health sciences, Binding Sites, Dose-Response Relationship, Drug, Spectrometry, FMN Reductase - metabolism, FMN Reductase - antagonists & inhibitors, 3. Good health, Kinetics, Spectrometry, Fluorescence, Models, Chemical, High Pressure Liquid, Escherichia coli - enzymology, Flavin-Adenine Dinucleotide, Enzyme Inhibitors - pharmacology, Drug, Hydrogen, Protein Binding

Zugangs-URL: http://www.jbc.org/content/277/42/39450.full.pdf
https://pubmed.ncbi.nlm.nih.gov/12177066
https://europepmc.org/article/MED/12177066
https://www.jbc.org/article/S0021-9258(19)72304-7/fulltext
https://www.sciencedirect.com/science/article/pii/S0021925819723047
https://www.ncbi.nlm.nih.gov/pubmed/12177066
https://www.jbc.org/content/277/42/39450.full
https://pubmed.ncbi.nlm.nih.gov/12177066/

Site-Directed Mutations in the FAD-Binding Domain of Glycerophosphate Dehydrogenase: Catalytic Defects with Preserved Mitochondrial Anchoring of the Enzyme in Transfected COS-7 Cells

Autoren: Fabregat, Marta E Gudayol, Monica Rasschaert, Joanne et al.

Quelle: Molecular Genetics and Metabolism. 75:168-173

Schlagwörter: 0301 basic medicine, Glycerolphosphate Dehydrogenase, Binding Sites -- genetics, Transfection, Catalysis, 03 medical and health sciences, Mitochondria -- metabolism, Glycerolphosphate Dehydrogenase -- metabolism, Cricetinae, Site-Directed, Animals, Humans, FAD-linked glycerophosphate dehydrogenase, 0303 health sciences, Binding Sites, Sciences bio-médicales et agricoles, Mitochondria, 3. Good health, Flavin-Adenine Dinucleotide -- metabolism, Catalytic defects in site-directed mutations, Mutagenesis, COS Cells, Flavin-Adenine Dinucleotide, Mutagenesis, Site-Directed, Mitochondrial anchoring, Glycerolphosphate Dehydrogenase -- genetics

Dateibeschreibung: No full-text files

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/11855936
https://core.ac.uk/display/8854942
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/55198/Details
https://www.sciencedirect.com/science/article/pii/S109671920193286X
http://www.sciencedirect.com/science/article/pii/S109671920193286X

Quantification of the Metabolic State in Cell-Model of Parkinson's Disease by Fluorescence Lifetime Imaging Microscopy.

Autoren: Chakraborty, Sandeep Nian, Fang-Shin Tsai, Jin-Wu et al.

Quelle: Scientific Reports, 6 (1), 19145 (2016-01-13)

Schlagwörter: NAD, Flavin-Adenine Dinucleotide, Nerve Growth Factor, Animals, Flavin-Adenine Dinucleotide/metabolism, NAD/metabolism, Nerve Growth Factor/pharmacology, PC12 Cells, Parkinson Disease/metabolism, Rats, Energy Metabolism/drug effects, Metabolomics/methods, Microscopy, Fluorescence/methods, Models, Biological, Energy Metabolism, Metabolomics, Fluorescence, Parkinson Disease, Multidisciplinary, Life sciences, Biotechnology, Sciences du vivant, Biotechnologie

Relation: https://www.nature.com/articles/srep19145.pdf; urn:issn:2045-2322; https://orbi.uliege.be/handle/2268/330649; info:hdl:2268/330649; info:pmid:26758390

Verfügbarkeit: https://orbi.uliege.be/handle/2268/330649
https://orbi.uliege.be/bitstream/2268/330649/1/2016%20Chakraborty-Quantification%20of%20the%20Metabolic%20State%20in%20Cell-Model%20of%20Parkinson%27s%20Disease%20by%20Fluorescence%20Lifetime%20Imaging%20Microscopy.pdf
https://doi.org/10.1038/srep19145

Long term in vitro effects of streptozotocin, interleukin-1, and high glucose concentration on the activity of mitochondrial dehydrogenases and the secretion of insulin in pancreatic islets

Autoren: Rasschaert, Joanne Eizirik, Decio L. Malaisse, Willy

Quelle: Endocrinology. 130:3522-3528

Schlagwörter: Male, 0301 basic medicine, Insulin -- metabolism, Cells, Inbred Strains, Streptozocin -- pharmacology, Glycerolphosphate Dehydrogenase, Mice, Inbred Strains, Ketoglutarate Dehydrogenase Complex -- metabolism, DNA -- metabolism, Recombinant Proteins -- pharmacology, Islets of Langerhans, Mice, 03 medical and health sciences, Glucose -- pharmacology, Glutamate Dehydrogenase -- metabolism, Glycerolphosphate Dehydrogenase -- metabolism, Glutamate Dehydrogenase, Islets of Langerhans -- drug effects, Mitochondria -- enzymology, Insulin Secretion, Insulin -- secretion, Islets of Langerhans -- secretion, Animals, Insulin, Ketoglutarate Dehydrogenase Complex, Interleukin-1 -- pharmacology, Cells, Cultured, 0303 health sciences, Cultured, Proteins, Islets of Langerhans -- enzymology, DNA, Sciences bio-médicales et agricoles, NAD, Mitochondria, Rats, Kinetics, Flavin-Adenine Dinucleotide -- metabolism, Glucose, NAD -- metabolism, Flavin-Adenine Dinucleotide, Proteins -- metabolism, Interleukin-1

Dateibeschreibung: No full-text files

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/1534541
https://core.ac.uk/display/8855695
http://www.ncbi.nlm.nih.gov/pubmed/1534541
http://europepmc.org/abstract/MED/1534541
https://academic.oup.com/endo/article-abstract/130/6/3522/3034399
http://press.endocrine.org/doi/10.1210/endo.130.6.1534541
https://academic.oup.com/endo/article-lookup/doi/10.1210/endo.130.6.1534541

A concerted mechanism for berberine bridge enzyme

Autoren: Peter Macheroux Sabrina Riedl Andreas Winkler et al.

Quelle: Nature Chemical Biology 4, 739-741 (2008). doi:10.1038/nchembio.123

Schlagwörter: 0301 basic medicine, discretamine, 0303 health sciences, Eschscholzia, Berberine Alkaloids, Oxidoreductases, N-Demethylating, Eschscholzia: enzymology, Oxidoreductases, N-Demethylating: metabolism, Catalysis, 3. Good health, Oxygen, reticuline oxidase, Kinetics, 03 medical and health sciences, Alkaloids, Catalytic Domain, Flavin-Adenine Dinucleotide: metabolism, Flavin-Adenine Dinucleotide, Protons, Oxidoreductases, N-Demethylating: chemistry

Zugangs-URL: https://bib-pubdb1.desy.de/record/84445/files/winkler_et_al_final.pdf
https://pubmed.ncbi.nlm.nih.gov/18953357
https://pubmed.ncbi.nlm.nih.gov/18953357/
https://www.nature.com/articles/nchembio.123
https://europepmc.org/abstract/MED/18953357
https://core.ac.uk/display/20503491
https://www.nature.com/articles/nchembio.123.pdf
https://graz.pure.elsevier.com/en/publications/a-concerted-mechanism-for-berberine-bridge-enzyme
https://bib-pubdb1.desy.de/record/84445

A concerted mechanism for berberine bridge enzyme

Autoren: Winkler, A. Łyskowski, A. Riedl, S. et al.

Quelle: Nature Chemical Biology 4, 739-741 (2008). doi:10.1038/nchembio.123

Schlagwörter: Alkaloids, Berberine Alkaloids, Catalysis, Catalytic Domain, Eschscholzia: enzymology, Flavin-Adenine Dinucleotide: metabolism, Kinetics, Oxidoreductases, N-Demethylating: chemistry, N-Demethylating: metabolism, Oxygen, Protons, Flavin-Adenine Dinucleotide, discretamine, reticuline oxidase, N-Demethylating

Geographisches Schlagwort: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/1552-4469; info:eu-repo/semantics/altIdentifier/issn/1552-4450; info:eu-repo/semantics/altIdentifier/wos/WOS:000260955900009; info:eu-repo/semantics/altIdentifier/pmid/pmid:18953357

Verfügbarkeit: https://bib-pubdb1.desy.de/record/84445
https://bib-pubdb1.desy.de/search?p=id:%22PHPPUBDB-8673%22

Structural and Catalytic Differences between Two FADH2-Dependent Monooxygenases: 2,4,5-TCP 4-Monooxygenase (TftD) from Burkholderia cepacia AC1100 and 2,4,6-TCP 4-Monooxygenase (TcpA) from Cupriavidus necator JMP134

Autoren: Robert P. Hayes Brian N. Webb Arun Kumar Subramanian et al.

Quelle: Int J Mol Sci
International Journal of Molecular Sciences; Volume 13; Issue 8; Pages: 9769-9784

Schlagwörter: Models, Molecular, 0301 basic medicine, Flavin-Adenine Dinucleotide - analogs & derivatives, Cupriavidus necator - enzymology, Protein Conformation, Chlorophenols - metabolism, Molecular Sequence Data, Sequence Homology, Burkholderia cepacia, Flavin-Adenine Dinucleotide - metabolism, Crystallography, X-Ray, Article, Catalysis, Mixed Function Oxygenases, Substrate Specificity, 03 medical and health sciences, Models, Amino Acid Sequence, Burkholderia cepacia - enzymology, 0303 health sciences, Crystallography, Sequence Homology, Amino Acid, Molecular, Mixed Function Oxygenases - metabolism, 3. Good health, Amino Acid, X-Ray, Flavin-Adenine Dinucleotide, Cupriavidus necator, Mixed Function Oxygenases - chemistry, TCP, flavin, bioremediation, monooxygenase, TcpA, TftD, crystal structure , Chlorophenols

Dateibeschreibung: application/pdf

Zugangs-URL: https://www.mdpi.com/1422-0067/13/8/9769/pdf
https://pubmed.ncbi.nlm.nih.gov/22949829
https://www.mdpi.com/1422-0067/13/8/9769/pdf
http://europepmc.org/articles/PMC3431827
https://pubmed.ncbi.nlm.nih.gov/22949829/
https://www.ncbi.nlm.nih.gov/pubmed/22949829
https://www.rcsb.org/structure/4G5E
https://www.mdpi.com/1422-0067/13/8/9769

Pathway of Glycine Betaine Biosynthesis in Aspergillus fumigatus

Autoren: Lambou, Karine Pennati, Andrea Valsecchi, Isabel et al.

Weitere Verfasser: Lambou, Karine Pennati, Andrea Valsecchi, Isabel et al.

Quelle: ISSN: 1535-9778.

Schlagwörter: MESH: Alcohol Oxidoreductases/genetics, MESH: Alcohol Oxidoreductases/metabolism, MESH: Flavin-Adenine Dinucleotide/metabolism, MESH: Fungal Proteins/genetics, MESH: Fungal Proteins/metabolism, MESH: Gene Expression Regulation, Fungal, MESH: Kinetics, MESH: Mutation, MESH: Mycelium/genetics, MESH: Mycelium/metabolism, MESH: Species Specificity, MESH: Spores, Fungal/genetics, MESH: Aspergillus fumigatus/genetics, Fungal/metabolism, MESH: Aspergillus fumigatus/metabolism, MESH: Betaine/analogs & derivatives, MESH: Betaine/metabolism, MESH: Betaine-Aldehyde Dehydrogenase/genetics, MESH: Betaine-Aldehyde Dehydrogenase/metabolism, MESH: Choline/metabolism, MESH: Enzyme Assays, [SDV]Life Sciences [q-bio], [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology, [SDV.MP.MYC]Life Sciences [q-bio]/Microbiology and Parasitology/Mycology

Relation: info:eu-repo/semantics/altIdentifier/pmid/23563483; info:eu-repo/grantAgreement//260338/EU/Fungi in the setting of inflammation, allergy and autoimmune diseases:Translating basic science into clinical practices/ALLFUN; PUBMED: 23563483; PUBMEDCENTRAL: PMC3675988

Verfügbarkeit: https://hal.science/hal-02468278
https://doi.org/10.1128/EC.00348-12

Ionic Liquides as Performance Additives for Electroenzymatic Syntheses

Autoren: Kohlmann, C. Greiner, L. Leitner, W. et al.

Quelle: Chemistry 15, 11692 - 11700 (2009). doi:10.1002/chem.200901046

Schlagwörter: info:eu-repo/classification/ddc/540, Amino Acid Oxidoreductases: metabolism, Biocatalysis, Chloride Peroxidase: metabolism, Electrochemical Techniques, Flavin-Adenine Dinucleotide: metabolism, Hydrogen Peroxide: metabolism, Ionic Liquids: chemistry, NADP: metabolism, Solubility, Ionic Liquids, Flavin-Adenine Dinucleotide, NADP, Hydrogen Peroxide, Chloride Peroxidase, Amino Acid Oxidoreductases, biotechnology, electroenzymatic synthesis, sustainable chemistry

Geographisches Schlagwort: DE

Relation: info:eu-repo/semantics/altIdentifier/wos/WOS:000271992100033; info:eu-repo/semantics/altIdentifier/issn/0947-6539; info:eu-repo/semantics/altIdentifier/pmid/pmid:19777513

Verfügbarkeit: https://juser.fz-juelich.de/record/5895
https://juser.fz-juelich.de/search?p=id:%22PreJuSER-5895%22

Sensing cell metabolism by time-resolved autofluorescence

Autoren: Wu, Yicong Zheng, Wei Qu, Jianan Y.

Quelle: Optics Letters. 31:3122

Schlagwörter: L-Lactate Dehydrogenase: metabolism, 0301 basic medicine, Cells, NAD: metabolism, Uterine Cervical Neoplasms, 01 natural sciences, Fluorescence, Cell Line, 03 medical and health sciences, 0103 physical sciences, Humans, Cells, Cultured, Cell Line, Transformed, Microscopy, Cultured, Microscopy, Confocal, L-Lactate Dehydrogenase, Spectrometry, NAD, Uterine Cervical Neoplasms: metabolism, Spectrometry, Fluorescence, Transformed, Confocal, Flavin-Adenine Dinucleotide: metabolism, Flavin-Adenine Dinucleotide, Female

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/17041655
https://www.ncbi.nlm.nih.gov/pubmed/17041655
https://www.osapublishing.org/ol/abstract.cfm?uri=ol-31-21-3122
http://ui.adsabs.harvard.edu/abs/2006OptL...31.3122W/abstract
https://dialnet.unirioja.es/servlet/articulo?codigo=2155204
http://www.ece.ust.hk/~eequ/Dr%20Qu's%20Homepage_files/2006_OL_Cell.pdf
http://repository.ust.hk/ir/Record/1783.1-30633

Sequence-structure-function analysis of the bifunctional enzyme MnmC that catalyses the last two steps in the biosynthesis of hypermodified nucleoside mnm5s2U in tRNA.

Autoren: Roovers, Martine Oudjama, Yamina Kaminska, Katarzyna H et al.

Quelle: Proteins, 71 (4

Schlagwörter: Sciences bio-médicales et agricoles, Amino Acid Sequence, Amino Acid Substitution, Binding Sites, Catalysis, Computational Biology -- methods, Conserved Sequence, Escherichia coli Proteins -- analysis, Escherichia coli Proteins -- chemistry, Escherichia coli Proteins -- genetics, Escherichia coli Proteins -- metabolism, Flavin-Adenine Dinucleotide -- metabolism, Genetic Complementation Test, Ligands, Methylation, Models, Molecular, Molecular Sequence Data, Multienzyme Complexes -- analysis, Multienzyme Complexes -- chemistry, Multienzyme Complexes -- genetics, Multienzyme Complexes -- metabolism, Protein Binding, Protein Folding, Protein Structure, Secondary, Tertiary, RNA, Bacterial -- biosynthesis, Transfer -- biosynthesis

Dateibeschreibung: 1 full-text file(s): application/pdf

Relation: uri/info:doi/10.1002/prot.21918; uri/info:pmid/18186482; uri/info:scp/44349146074; https://dipot.ulb.ac.be/dspace/bitstream/2013/50477/3/50477.pdf

Verfügbarkeit: http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/50477
https://dipot.ulb.ac.be/dspace/bitstream/2013/50477/3/50477.pdf

A Novel Photoreaction Mechanism for the Circadian Blue Light Photoreceptor Drosophila Cryptochrome

Autoren: Berndt, A. Kottke, T. Breitkreuz, H. et al.

Quelle: The journal of biological chemistry 282, 13011 - 13021 (2007). doi:10.1074/jbc.M608872200

Schlagwörter: info:eu-repo/classification/ddc/570, Animals, Cell Line, Circadian Rhythm, Cryptochromes, DNA Repair, Deoxyribodipyrimidine Photo-Lyase: chemistry, Drosophila: chemistry, Drosophila: metabolism, Drosophila Proteins: chemistry, Drosophila Proteins: metabolism, Flavin-Adenine Dinucleotide: chemistry, Flavin-Adenine Dinucleotide: metabolism, Flavoproteins: chemistry, Flavoproteins: metabolism, Oxidation-Reduction, Photochemistry, Photoreceptor Cells, Invertebrate: chemistry, Invertebrate: metabolism, Drosophila Proteins, Flavoproteins, Flavin-Adenine Dinucleotide, Deoxyribodipyrimidine Photo-Lyase

Geographisches Schlagwort: DE

Relation: info:eu-repo/semantics/altIdentifier/issn/0021-9258; info:eu-repo/semantics/altIdentifier/pmid/pmid:17298948; info:eu-repo/semantics/altIdentifier/wos/WOS:000245942800071

Verfügbarkeit: https://juser.fz-juelich.de/record/59166
https://juser.fz-juelich.de/search?p=id:%22PreJuSER-59166%22