s-adenosylmethionine has been researched along with protocatechuic acid in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (50.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Nissinen, E; Schultz, E | 1 |
| Nissinen, E | 1 |
| Julkunen, I; Lotta, T; Melén, K; Taskinen, J; Tilgmann, C; Ulmanen, I; Vidgren, J | 1 |
| Dixon, RA; Guo, D; Kota, P; Noel, J; Zubieta, C | 1 |
4 other study(ies) available for s-adenosylmethionine and protocatechuic acid
| Article | Year |
|---|---|
Inhibition of rat liver and duodenum soluble catechol-O-methyltransferase by a tight-binding inhibitor OR-462.
Topics: Animals; Catalysis; Catechol O-Methyltransferase Inhibitors; Catechols; Duodenum; Hydroxybenzoates; Ketones; Kinetics; Liver; Magnesium; Pentanones; Rats; Rats, Inbred Strains; S-Adenosylmethionine | 1989 |
Determination of catechol-O-methyltransferase activity in brain tissue by high-performance liquid chromatography with on-line radiochemical detection.
Topics: Animals; Brain; Catechol O-Methyltransferase; Chromatography, High Pressure Liquid; Hydroxybenzoates; Kinetics; Radiochemistry; Rats; S-Adenosylmethionine | 1985 |
Kinetics of human soluble and membrane-bound catechol O-methyltransferase: a revised mechanism and description of the thermolabile variant of the enzyme.
Topics: Animals; Base Sequence; Catechol O-Methyltransferase; Cell Membrane; Dopamine; Enzyme Stability; Hot Temperature; Humans; Hydroxybenzoates; Kinetics; Levodopa; Magnesium; Methylation; Models, Molecular; Molecular Sequence Data; Norepinephrine; Rats; Recombinant Proteins; S-Adenosylmethionine | 1995 |
O-Methylation of benzaldehyde derivatives by "lignin specific" caffeic acid 3-O-methyltransferase.
Topics: Amino Acid Substitution; Benzaldehydes; Carbon Radioisotopes; Down-Regulation; Hydroxybenzoates; Kinetics; Lignin; Medicago sativa; Methylation; Methyltransferases; Phenols; Plant Stems; Plants, Genetically Modified; Recombinant Proteins; S-Adenosylmethionine; Substrate Specificity | 2004 |