decanoyl-coenzyme a has been researched along with carnitine in 4 studies
*Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism. [MeSH]
*Carnitine: A constituent of STRIATED MUSCLE and LIVER. It is an amino acid derivative and an essential cofactor for fatty acid metabolism. [MeSH]
Studies (decanoyl-coenzyme a) | Trials (decanoyl-coenzyme a) | Recent Studies (post-2010) (decanoyl-coenzyme a) | Studies (carnitine) | Trials (carnitine) | Recent Studies (post-2010) (carnitine) |
---|---|---|---|---|---|
14 | 0 | 2 | 9,625 | 750 | 3,016 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (25.00) | 18.7374 |
1990's | 2 (50.00) | 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 |
---|---|
Nagamatsu, A; Shimeno, H; Soeda, S; Yamakawa, N | 1 |
Bieber, LL; Fiol, CJ; Kerner, J | 1 |
Bieber, LL; Wagner, M | 1 |
Ariño, J; Asins, G; Clotet, J; Hegardt, FG; Morillas, M; Rubí, B; Serra, D | 1 |
4 other study(ies) available for decanoyl-coenzyme a and carnitine
Article | Year |
---|---|
Inhibition of proline endopeptidase activity by acyl-coenzyme A esters.
Topics: Acyl Coenzyme A; Animals; Carboxylic Acids; Carnitine; Coenzyme A; Cytosol; Endopeptidases; Esters; Kinetics; Liver; Prolyl Oligopeptidases; Rats; Serine Endopeptidases; Spectrometry, Fluorescence; Structure-Activity Relationship | 1990 |
Effect of malonyl-CoA on the kinetics and substrate cooperativity of membrane-bound carnitine palmitoyltransferase of rat heart mitochondria.
Topics: Acyl Coenzyme A; Acyltransferases; Animals; Carnitine; Carnitine O-Palmitoyltransferase; Fasting; Kinetics; Malonyl Coenzyme A; Membranes; Mitochondria, Heart; Mitochondrial Swelling; Rats; Substrate Specificity | 1987 |
Effect of pH and acyl-CoA chain length on the conversion of heart mitochondrial CPT-I/CPTo to a high affinity, malonyl-CoA-inhibited state.
Topics: Acyl Coenzyme A; Animals; Carnitine; Carnitine O-Palmitoyltransferase; Dose-Response Relationship, Drug; Drug Interactions; Enzyme Inhibitors; Hydrogen-Ion Concentration; Malonyl Coenzyme A; Mitochondria, Heart; Palmitoyl Coenzyme A; Rats | 1996 |
Inhibition by etomoxir of rat liver carnitine octanoyltransferase is produced through the co-ordinate interaction with two histidine residues.
Topics: Acyl Coenzyme A; Amino Acid Sequence; Animals; Binding Sites; Blotting, Western; Carnitine; Carnitine Acyltransferases; DNA, Complementary; Dose-Response Relationship, Drug; Enzyme Inhibitors; Epoxy Compounds; Histidine; Humans; Kinetics; Liver; Molecular Sequence Data; Mutagenesis, Site-Directed; Peroxisomes; Plasmids; Point Mutation; Protein Binding; Rats; Recombinant Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid | 2000 |