glutamic acid has been researched along with palmitoyl coenzyme a in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 4 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bracher, R; Follath, F; Ha, HR; Krähenbühl, S; Spaniol, M | 1 |
| Jackson, VN; Price, NT; Zammit, VA | 1 |
| Crescenzo, R; Dulloo, AG; Iossa, S; Liverini, G; Mainieri, D; Montani, JP; Seydoux, J; Solinas, G | 1 |
| Dai, J; Haro, D; Marrero, PF; Napal, L; Treber, M; Woldegiorgis, G | 1 |
4 other study(ies) available for glutamic acid and palmitoyl coenzyme a
| Article | Year |
|---|---|
Toxicity of amiodarone and amiodarone analogues on isolated rat liver mitochondria.
Topics: Amiodarone; Animals; Electron Transport; Glutamic Acid; Male; Mitochondria, Liver; Oxidative Phosphorylation; Oxygen Consumption; Palmitoyl Coenzyme A; Rats; Rats, Sprague-Dawley | 2001 |
Specificity of the interactions between Glu-3, Ser-24, and Gln-30 within the N-terminal segment of rat liver mitochondrial overt carnitine palmitoyltransferase (L-CPT I) in determining the malonyl-CoA sensitivity of the enzyme.
Topics: Animals; Carnitine; Carnitine O-Palmitoyltransferase; DNA Primers; Glutamic Acid; Glutamine; Malonyl Coenzyme A; Mitochondria, Liver; Palmitoyl Coenzyme A; Peptide Fragments; Pichia; Plasmids; Point Mutation; Protein Structure, Secondary; Rats; Recombinant Proteins; Serine | 2001 |
Skeletal muscle mitochondrial oxidative capacity and uncoupling protein 3 are differently influenced by semistarvation and refeeding.
Topics: Animal Feed; Animals; Blotting, Western; Body Weight; Carrier Proteins; Food Deprivation; Glutamic Acid; Ion Channels; Lipid Metabolism; Male; Mitochondria; Mitochondrial Proteins; Muscle, Skeletal; Oxygen; Oxygen Consumption; Palmitoyl Coenzyme A; Palmitoylcarnitine; Rats; Rats, Sprague-Dawley; Succinic Acid; Uncoupling Protein 3 | 2003 |
A single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzyme.
Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Blotting, Western; Carnitine; Carnitine O-Palmitoyltransferase; Chickens; Dose-Response Relationship, Drug; Glutamic Acid; Glutamine; Humans; Immunoblotting; Kinetics; Liver; Lysine; Malonyl Coenzyme A; Mice; Molecular Sequence Data; Muscles; Mutation; Palmitoyl Coenzyme A; Pichia; Polymerase Chain Reaction; Protein Isoforms; Protein Structure, Tertiary; Rats; Sequence Homology, Amino Acid; Swine | 2003 |