serine has been researched along with malonyl coenzyme a in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (16.67) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 4 (66.67) | 29.6817 |
2010's | 1 (16.67) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Højrup, P; Knudsen, J; Mikkelsen, J; Rasmussen, MM; Roepstorff, P | 1 |
Jackson, VN; Price, NT; Zammit, VA | 1 |
Bowman, ME; Jez, JM; Noel, JP | 1 |
Altarejos, JY; Lopaschuk, GD; Onay-Besikci, A | 1 |
Dai, J; Liu, H; Treber, M; Woldegiorgis, G; Zheng, G | 1 |
Dyck, JR; Kemp, BE; Kienesberger, PC; Masson, G; Nagendran, J; Pulinilkunnil, T; Steinberg, GR; Waller, TJ; Zordoky, BN | 1 |
6 other study(ies) available for serine and malonyl coenzyme a
Article | Year |
---|---|
Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase.
Topics: Acetyl Coenzyme A; Acyltransferases; Amino Acid Sequence; Animals; Binding Sites; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Fatty Acid Synthases; Female; Goats; Malonyl Coenzyme A; Mammary Glands, Animal; Peptide Fragments; Serine | 1985 |
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 |
Expanding the biosynthetic repertoire of plant type III polyketide synthases by altering starter molecule specificity.
Topics: Acetic Acid; Acyltransferases; Alkaloids; Aniline Compounds; Binding Sites; Chromatography, Thin Layer; Crystallography, X-Ray; Gas Chromatography-Mass Spectrometry; Kinetics; Malonyl Coenzyme A; Models, Chemical; Models, Molecular; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutation; Phenylalanine; Protein Binding; Protein Conformation; Pyrones; Serine | 2002 |
gAd-globular head domain of adiponectin increases fatty acid oxidation in newborn rabbit hearts.
Topics: Acetyl-CoA Carboxylase; Acyl Coenzyme A; Adiponectin; AMP-Activated Protein Kinases; Animals; Animals, Newborn; Blotting, Western; Centrifugation, Density Gradient; Fatty Acids; Glucose; Heart; Insulin; Intercellular Signaling Peptides and Proteins; Malonyl Coenzyme A; Models, Biological; Multienzyme Complexes; Muscle, Skeletal; Myocardium; Oxygen; Palmitic Acid; Phosphorylation; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Rabbits; Recombinant Proteins; Serine; Sucrose; Time Factors | 2004 |
Cysteine-scanning mutagenesis of muscle carnitine palmitoyltransferase I reveals a single cysteine residue (Cys-305) is important for catalysis.
Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Blotting, Western; Carnitine; Carnitine O-Palmitoyltransferase; Catalysis; Cysteine; DNA Primers; Humans; Kinetics; Malonyl Coenzyme A; Models, Chemical; Molecular Sequence Data; Mutagenesis; Mutation; Myocardium; Palmitic Acid; Palmitoylcarnitine; Pichia; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Serine | 2005 |
AMPK-dependent inhibitory phosphorylation of ACC is not essential for maintaining myocardial fatty acid oxidation.
Topics: Acetyl-CoA Carboxylase; AMP-Activated Protein Kinases; Animals; Energy Metabolism; Fatty Acids; Female; Gene Knock-In Techniques; Male; Malonyl Coenzyme A; Mice, Mutant Strains; Mice, Transgenic; Mutation; Myocardial Contraction; Myocardium; Oxidation-Reduction; Phosphorylation; Serine; Time Factors; Ventricular Function, Left | 2014 |