nad has been researched along with molybdenum cofactor in 10 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (10.00) | 18.7374 |
1990's | 5 (50.00) | 18.2507 |
2000's | 2 (20.00) | 29.6817 |
2010's | 2 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bray, RC; Burke, JF; Chovnick, A; Doyle, WA; Hughes, RK; Whittle, JR | 1 |
Barber, MJ; Kay, CJ; Solomonson, LP | 1 |
Bray, RC; Deistung, J; Ventom, AM | 1 |
Caboche, M; Gonneau, M; Meyer, C; Rouzé, P | 1 |
Bray, RC; Chovnick, A; Doyle, WA; Whittle, JR | 1 |
Bray, RC; Burke, JF; Chovnick, A; Doyle, WA; Dutton, FL; Whittle, JR | 1 |
Rizzi, M; Schindelin, H | 1 |
Morozkina, EV; Zvyagilskaya, RA | 1 |
Chi, JC; Fischer, K; Krizowski, S; Lambeck, I; Mehlmer, N; Mueller, S; Schwarz, G; Teige, M | 1 |
Clement, B; Havemeyer, A; Ott, G | 1 |
3 review(s) available for nad and molybdenum cofactor
Article | Year |
---|---|
Structural biology of enzymes involved in NAD and molybdenum cofactor biosynthesis.
Topics: Amide Synthases; Bacterial Proteins; Coenzymes; Enzymes; Escherichia coli Proteins; Metalloproteins; Models, Molecular; Molecular Structure; Molybdenum Cofactors; NAD; Nicotinamide-Nucleotide Adenylyltransferase; Protein Structure, Tertiary; Pteridines; Sulfurtransferases | 2002 |
Nitrate reductases: structure, functions, and effect of stress factors.
Topics: Bacteria; Bacterial Physiological Phenomena; Binding Sites; Coenzymes; Electrons; Metalloproteins; Models, Chemical; Molybdenum; Molybdenum Cofactors; NAD; Nitrate Reductase; Nitrogen; Oxygen; Protein Conformation; Pteridines; Substrate Specificity; Temperature | 2007 |
The mammalian molybdenum enzymes of mARC.
Topics: Animals; Coenzymes; Cytochromes b5; Electron Transport; Humans; Mammals; Membrane Proteins; Metabolic Detoxication, Phase I; Metalloproteins; Mitochondria; Mitochondrial Proteins; Molybdenum; Molybdenum Cofactors; NAD; Oxidoreductases; Pteridines | 2015 |
7 other study(ies) available for nad and molybdenum cofactor
Article | Year |
---|---|
Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase.
Topics: Amino Acid Sequence; Animals; Binding Sites; Chromatography, Gel; Coenzymes; Drosophila melanogaster; Flavin-Adenine Dinucleotide; Iron-Sulfur Proteins; Metalloproteins; Molecular Sequence Data; Molybdenum; Molybdenum Cofactors; Mutation; NAD; Pteridines; Sequence Alignment; Structure-Activity Relationship; Xanthine Dehydrogenase | 1992 |
Electrochemical and kinetic analysis of electron-transfer reactions of Chlorella nitrate reductase.
Topics: Chlorella; Coenzymes; Electrochemistry; Flavin-Adenine Dinucleotide; Glucosephosphate Dehydrogenase; Heme; Kinetics; Metalloproteins; Molybdenum Cofactors; NAD; Nitrate Reductase; Nitrate Reductases; Oxidation-Reduction; Pteridines; Spectrophotometry | 1991 |
The isolation of demolybdo xanthine oxidase from bovine milk.
Topics: Animals; Chromatography, Affinity; Coenzymes; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Metalloproteins; Milk; Molybdenum; Molybdenum Cofactors; NAD; Pteridines; Spectrophotometry; Xanthine Oxidase | 1988 |
Identification by mutational analysis of four critical residues in the molybdenum cofactor domain of eukaryotic nitrate reductase.
Topics: Amino Acid Sequence; Base Sequence; Chromatography, Gel; Coenzymes; DNA Mutational Analysis; DNA, Complementary; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Mutation; NAD; Nicotiana; Nitrate Reductase; Nitrate Reductases; Plants, Toxic; Protein Conformation; Pteridines | 1995 |
Role and oxidation state of the pterin molybdenum cofactor of molybdenum enzymes: studies of a Drosophila melanogaster xanthine dehydrogenase (rosy) variant, G1011E.
Topics: Animals; Coenzymes; Cytochrome c Group; Drosophila melanogaster; Genetic Variation; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; NAD; Oxidation-Reduction; Pteridines; Xanthine Dehydrogenase | 1996 |
Properties of xanthine dehydrogenase variants from rosy mutant strains of Drosophila melanogaster and their relevance to the enzyme's structure and mechanism.
Topics: Amino Acid Sequence; Animals; Binding Sites; Coenzymes; Conserved Sequence; Cross Reactions; Drosophila melanogaster; Enzyme Activation; Genetic Variation; Kinetics; Metalloproteins; Molecular Sequence Data; Molybdenum Cofactors; Mutagenesis, Site-Directed; Mutation; NAD; Oxidation-Reduction; Pteridines; Sequence Homology, Amino Acid; Structure-Activity Relationship; Xanthine; Xanthine Dehydrogenase; Xanthines | 1996 |
Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase.
Topics: 14-3-3 Proteins; Arabidopsis; Catalysis; Coenzymes; Eukaryota; Heme; Kinetics; Metalloproteins; Molybdenum; Molybdenum Cofactors; NAD; Nitrate Reductase; Nitrate Reductase (NADH); Nitrate Reductases; Oxidation-Reduction; Phosphorylation; Protein Kinases; Pteridines | 2010 |