pyridoxal phosphate has been researched along with 1,5-i-aedans in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 2 (40.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Churchich, JE; Kim, YT; Kwok, F | 1 |
Bucci, E; Kowalczyk, J; Sassaroli, M | 1 |
Cash, VL; Dean, DR; White, RH; Zheng, L | 1 |
Flint, DH | 1 |
Bittner, F; Heidenreich, T; Mendel, RR; Wollers, S | 1 |
5 other study(ies) available for pyridoxal phosphate and 1,5-i-aedans
Article | Year |
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Interactions of pyridoxal kinase and aspartate aminotransferase emission anisotropy and compartmentation studies.
Topics: Animals; Apoenzymes; Aspartate Aminotransferases; Brain; Chromatography, Affinity; Fluorescence Polarization; Fluorescent Dyes; Isothiocyanates; Kinetics; Naphthalenesulfonates; Phosphotransferases; Pyridoxal Kinase; Pyridoxal Phosphate; Sheep; Spectrophotometry; Thiocyanates | 1988 |
Probe dependence of correlation times in heme-free extrinsically labeled human hemoglobin.
Topics: Anilino Naphthalenesulfonates; Apoproteins; Fluoresceins; Fluorescent Dyes; Hemoglobins; Humans; Hydrogen-Ion Concentration; Naphthalenesulfonates; Pyridoxal Phosphate; Spectrometry, Fluorescence; Viscosity | 1986 |
Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product.
Topics: Allylglycine; Azotobacter vinelandii; Bacterial Proteins; Base Sequence; Catalysis; Cysteine; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Naphthalenesulfonates; Nitrogenase; Pyridoxal Phosphate; Sulfur | 1994 |
Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase.
Topics: Alanine; Amino Acid Sequence; Azotobacter vinelandii; Bacterial Proteins; Chromatography, Gel; Chromatography, Ion Exchange; Cysteine; Disulfides; Escherichia coli; Genes, Bacterial; Haemophilus influenzae; Hydro-Lyases; Iron-Sulfur Proteins; Kinetics; Macromolecular Substances; Molecular Sequence Data; Naphthalenesulfonates; Pantetheine; Peptide Fragments; Pyridoxal Phosphate; Sequence Homology, Amino Acid; Sulfhydryl Reagents | 1996 |
Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration.
Topics: Aldehyde Oxidase; Arabidopsis; Arabidopsis Proteins; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Cysteine; Cytosol; Fluorescent Dyes; Genetic Vectors; Iron-Sulfur Proteins; Kinetics; Lyases; Lysine; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Naphthalenesulfonates; Pichia; Plant Proteins; Protein Binding; Protein Structure, Tertiary; Pteridines; Pyridoxal Phosphate; Selenocysteine; Spectrophotometry; Substrate Specificity; Sulfides; Sulfurtransferases; Xanthine Dehydrogenase | 2005 |