hydrogen carbonate has been researched along with tiglyl-coenzyme a in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (75.00) | 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 |
|---|---|
| Gibson, KM; Kamali, V; Lee, CF; Søvik, O | 1 |
| Diez, TA; Nikolau, BJ; Wurtele, ES | 1 |
| Chen, Y; Nikolau, BJ; Wang, X; Wurtele, ES | 1 |
| Aguilar, JA; Campos-García, J; Díaz-Pérez, AL; Díaz-Pérez, C; Nikolau, BJ; Rodríguez-Zavala, JS | 1 |
4 other study(ies) available for hydrogen carbonate and tiglyl-coenzyme a
| Article | Year |
|---|---|
A coupled assay detecting defects in fibroblast isoleucine degradation distal to enoyl-CoA hydratase: application to 3-oxothiolase deficiency.
Topics: Acetyl-CoA C-Acetyltransferase; Acyl Coenzyme A; Adenosine Triphosphate; Bicarbonates; Carbon Radioisotopes; Cells, Cultured; Enoyl-CoA Hydratase; Fibroblasts; Humans; Isoleucine; Magnesium Chloride; NAD; Sodium; Sodium Bicarbonate | 1992 |
Purification and characterization of 3-methylcrotonyl-coenzyme-A carboxylase from leaves of Zea mays.
Topics: Acyl Coenzyme A; Adenosine Triphosphate; Bicarbonates; Biotin; Carbon-Carbon Ligases; Cations, Divalent; Hydrogen-Ion Concentration; Kinetics; Ligases; Magnesium; Molecular Weight; Protein Conformation; Zea mays | 1994 |
Purification and characterization of 3-methylcrotonyl-CoA carboxylase from somatic embryos of Daucus carota.
Topics: Acyl Coenzyme A; Adenosine Triphosphate; Bicarbonates; Biotin; Carbon-Carbon Ligases; Chemical Fractionation; Chemical Precipitation; Chromatography, Affinity; Chromatography, Ion Exchange; Hydrogen-Ion Concentration; Kinetics; Ligases; Molecular Weight; Polyethylene Glycols; Seeds; Sodium; Sodium Bicarbonate; Substrate Specificity; Vegetables | 1993 |
Substrate specificity of the 3-methylcrotonyl coenzyme A (CoA) and geranyl-CoA carboxylases from Pseudomonas aeruginosa.
Topics: Acyl Coenzyme A; Adenosine Triphosphate; Bacterial Proteins; Bicarbonates; Carbon-Carbon Ligases; Cloning, Molecular; Enzyme Stability; Escherichia coli; Gene Expression; Hydrogen-Ion Concentration; Kinetics; Metabolic Networks and Pathways; Models, Biological; Pseudomonas aeruginosa; Recombinant Proteins; Substrate Specificity; Temperature | 2008 |