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BMC psychiatry, ISSN 1471-244X, 07/2019, Volume 19, Issue 1, pp. 221 - 221
Following publication of the original article [1], we have been notified that some important information was omitted by the authors from the Competing... 
Oxidoreductases
Journal Article
1985, ISBN 9780849358692, 285
Book
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2017, Volume 114, Issue 48, pp. 12737 - 12742
Respiratory complex I (NADH: ubiquinone oxidoreductase), one of the largest membrane-bound enzymes in mammalian cells, powers ATP synthesis by using the energy... 
Electron transport chain | NADH:ubiquinone oxidoreductase | Mitochondria | Bioenergetics | Coenzyme Q10 | SUBMITOCHONDRIAL PARTICLES | coenzyme Q10 | electron transport chain | ALTERNATIVE OXIDASE | mitochondria | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | CHAIN | NADH | bioenergetics | ESCHERICHIA-COLI NDH-1 | BEEF-HEART | COENZYME-Q | HEART-MITOCHONDRIA | LIPID-BILAYER | Proteolipids - metabolism | Substrate Specificity | Ubiquinone - metabolism | Electron Transport Complex I - metabolism | Oxidoreductases - chemistry | Terpenes - chemistry | Thermodynamics | Terpenes - metabolism | Cattle | Electron Transport Complex I - genetics | Swine | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Thermus thermophilus - enzymology | Gene Expression | Mitochondria, Heart - chemistry | Thermus thermophilus - chemistry | Biocatalysis | Oxidoreductases - metabolism | Protein Structure, Secondary | Oxidoreductases - genetics | Ubiquinone - analogs & derivatives | Mitochondria, Heart - enzymology | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Static Electricity | Amino Acid Motifs | Electron Transport Complex I - chemistry | Animals | Hydrophobic and Hydrophilic Interactions | Protein Binding | Kinetics | Ubiquinone - chemistry | Proteolipids - chemistry | Physiological aspects | Ubiquinones | Genetic aspects | Oxidoreductases | Research | Protons | Energy use | Oxidoreductase | Electron transfer | Quinol oxidase | Hydrophobicity | Mammalian cells | Quinones | Ubiquinol | Ubiquinone | Energy | Energy conversion | Reaction kinetics | Ubiquinone oxidoreductase | Catalysis | Quinol | Adenosine triphosphate | Translocation | NADH-ubiquinone oxidoreductase | Travel time | Quinone | Cells | Correlation analysis | Nicotinamide adenine dinucleotide | Ubiquinone-10 | Energy of dissociation | Terpenes | Binding sites | Index Medicus | Biological Sciences
Journal Article
PLoS genetics, ISSN 1553-7404, 01/2019, Volume 15, Issue 1, pp. e1007972 - e1007972
[This corrects the article DOI: 10.1371/journal.pgen.1007743.]. 
Pancreas | Oxidoreductase
Journal Article
2004, Methods in Enzymology, ISBN 0121827860, Volume 382, xxxviii, 572
Quinones are members of a class of aromatic compounds with two oxygen atoms bonded to the ring as carbonyl groups. This volume covers more clinical aspects of... 
Book
Cancer Research, ISSN 0008-5472, 07/2010, Volume 70, Issue 13, pp. 5213 - 5219
Journal Article
Phytochemistry, ISSN 0031-9422, 01/2010, Volume 71, Issue 1
Merosesquiterpenids, craterellins A-C (1-3), were isolated from cultures of the basidiomycete Craterellus odoratus together with the previously known... 
Oxidoreductases
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 06/2019, Volume 1860, Issue 6, pp. 478 - 487
Journal Article
2013, 2nd ed., Springer handbook of enzymes, ISBN 3642362648, Volume v. Suppl. 8
Web Resource
Biochemistry, ISSN 0006-2960, 02/2018, Volume 57, Issue 6, pp. 963 - 977
Journal Article
Malaria Journal, ISSN 1475-2875, 06/2017, Volume 16, Issue 1, pp. 247 - 247
Background: Aspartate, which is converted from oxaloacetate (OAA) by aspartate aminotransferase, is considered an important precursor for purine salvage and... 
Fumarate hydratase (FH) | Plasmodium berghei | Luciferase-luciferin system | Malate:quinone oxidoreductase (MQO) | HIGH-EFFICIENCY TRANSFECTION | INFECTIOUS DISEASES | RODENT MALARIA | FUMARASE | BLOOD STAGES | BERGHEI | Malate: quinone oxidoreductase (MQO) | ATOVAQUONE | TROPICAL MEDICINE | METABOLISM | YOELII-YOELII | PARASITE PLASMODIUM-FALCIPARUM | SELECTION | PARASITOLOGY | Oxidoreductases - antagonists & inhibitors | Mitochondria - enzymology | Specific Pathogen-Free Organisms | Fumarate Hydratase - physiology | Mice, Inbred C57BL | Oxaloacetic Acid - metabolism | Plasmodium berghei - genetics | Male | Oxidoreductases - physiology | Fumarate Hydratase - deficiency | Malaria, Cerebral - prevention & control | Blood-Brain Barrier - metabolism | Animals | Plasmodium berghei - enzymology | Malates - metabolism | Membrane Potential, Mitochondrial | Fumarates - metabolism | Plasmodium berghei - growth & development | Female | Fumarate Hydratase - antagonists & inhibitors | Mice | Erythrocytes - parasitology | Mitochondria - physiology | Oxidoreductases - deficiency | Physiological aspects | Plasmodium falciparum | Research | Virulence (Microbiology) | Malaria | Risk factors | Quinone oxidoreductase | Salvaging | Growth | Oxidoreductase | Virulence | Genes | Erythrocytes | Genomes | Biosynthesis | Parasites | Cytosol | Blood | Purines | Mitochondria | Pyrimidines | Dynamics | Extracellular matrix | Dihydrofolate reductase | Public health | Phosphoenolpyruvate carboxylase | Vector-borne diseases | Pathogens | Enzymes | Phenotypes | Human diseases | Quinone | Metabolism | Strain | Pathogenicity | Fumarate hydratase | Mosquitoes | Aspartate aminotransferase | Oxidoreductases | Index Medicus | Luciferase–luciferin system
Journal Article
Journal Article
FEBS Letters, ISSN 0014-5793, 2004, Volume 563, Issue 1, pp. 207 - 212
Properties of Klebsiella pneumoniae respiratory chain enzymes catalyzing NADH oxidation have been studied. Using constructed K. pneumoniae mutant strains, it... 
NADH dehydrogenase | Sodium translocation | Complex I | Klebsiella pneumoniae | Vibrio | NDH-1, bacterial NADH:quinone oxidoreductase similar to mitochondrial complex I | NQR, bacterial NADH:quinone oxidoreductase similar to the sodium-motive NADH dehydrogenase of | CCCP, carbonyl cyanide | NDH-2, non-coupled bacterial NADH:quinone oxidoreductase | dNADH, reduced nicotinamide hypoxanthine dinucleotide | chlorophenylhydrazone | PCR, polymerase chain reaction | CCCP, carbonyl cyanide m-chlorophenylhydrazone | DNADH, reduced nicotinamide hypoxanthine dinucleotide | UBIQUINONE OXIDOREDUCTASE | NDH-I | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | HARVEYI | CELL BIOLOGY | BIOPHYSICS | QUINONE OXIDOREDUCTASE | OXIDOREDUCTASE COMPLEX-I | NA+-TRANSLOCATING NADH | complex I | AZOTOBACTER-VINELANDII | REDUCTASE | sodium translocation | MARINE VIBRIO-ALGINOLYTICUS | Protons | Quinone Reductases - metabolism | Electron Transport | Electron Transport Complex I | Oxidation-Reduction | Oxidoreductases - metabolism | Oxidoreductases - classification | Sodium - metabolism | NADH Dehydrogenase - metabolism | Oxidoreductases - chemistry | Proton Pumps | Vibrio - enzymology | Klebsiella pneumoniae - enzymology | Klebsiella pneumoniae - genetics | Klebsiella pneumoniae - growth & development | Bacterial Proteins - metabolism | NADH, NADPH Oxidoreductases - chemistry | Kinetics | Klebsiella pneumoniae - metabolism | Mutation | NADH, NADPH Oxidoreductases - metabolism | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2018, Volume 115, Issue 15, pp. 3846 - 3851
Pyruvate:ferredoxin oxidoreductase (PFOR) is a microbial enzyme that uses thiamine pyrophosphate (TPP), three [4Fe-4S] clusters, and coenzyme A (CoA) in the... 
Thiamine pyrophosphate | Coenzyme A | Carbon dioxide fixation | Gated electron transfer | Pyruvate:ferredoxin oxidoreductase | WOOD-LJUNGDAHL PATHWAY | HALOBACTERIUM-HALOBIUM | MULTIDISCIPLINARY SCIENCES | pyruvate:ferredoxin oxidoreductase | FREE-RADICAL INTERMEDIATE | thiamine pyrophosphate | OXALATE OXIDOREDUCTASE | PYRUVATE-FERREDOXIN OXIDOREDUCTASE | PEPTIDE FERMENTATION | coenzyme A | carbon dioxide fixation | gated electron transfer | 2-OXOACID OXIDOREDUCTASES | DESULFOVIBRIO-AFRICANUS | CATALYTIC CYCLE | CLOSTRIDIUM-THERMOACETICUM | Moorella - enzymology | Pyruvate Synthase - chemistry | Carbon Dioxide - chemistry | Pyruvic Acid - chemistry | Carbon Dioxide - metabolism | Ferredoxins - metabolism | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Ferredoxins - chemistry | Moorella - genetics | Coenzyme A - chemistry | Crystallography, X-Ray | Coenzyme A - metabolism | Moorella - chemistry | Pyruvate Synthase - genetics | Pyruvate Synthase - metabolism | Pyruvic Acid - metabolism | Bacterial Proteins - metabolism | Kinetics | Binding Sites | Pyruvates | Microbiological research | Coenzymes | Physiological aspects | Bacteria | Oxidoreductases | Research | Structure | Binding sites (Biochemistry) | Wood | Oxidoreductase | Carbon dioxide | Pyruvic acid | Metabolism | Greenhouse gases | Crystallography | Intermediates | Proteins | Microorganisms | Redox reactions | Vitamin B | Decarboxylation | Oxidation | Catalysis | Ferredoxin | Binding sites | Thiamine | Index Medicus | Biological Sciences
Journal Article
Photosynthesis Research, ISSN 0166-8595, 12/2017, Volume 134, Issue 3, pp. 291 - 306
Journal Article