serine and malonyl coenzyme a

serine has been researched along with malonyl coenzyme a in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19901 (16.67)18.7374
1990's0 (0.00)18.2507
2000's4 (66.67)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Højrup, P; Knudsen, J; Mikkelsen, J; Rasmussen, MM; Roepstorff, P1
Jackson, VN; Price, NT; Zammit, VA1
Bowman, ME; Jez, JM; Noel, JP1
Altarejos, JY; Lopaschuk, GD; Onay-Besikci, A1
Dai, J; Liu, H; Treber, M; Woldegiorgis, G; Zheng, G1
Dyck, JR; Kemp, BE; Kienesberger, PC; Masson, G; Nagendran, J; Pulinilkunnil, T; Steinberg, GR; Waller, TJ; Zordoky, BN1

Other Studies

6 other study(ies) available for serine and malonyl coenzyme a

ArticleYear
Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase.
    The Biochemical journal, 1985, Apr-01, Volume: 227, Issue:1

    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.
    Biochemistry, 2001, Dec-04, Volume: 40, Issue:48

    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.
    Proceedings of the National Academy of Sciences of the United States of America, 2002, Apr-16, Volume: 99, Issue:8

    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.
    The Journal of biological chemistry, 2004, Oct-22, Volume: 279, Issue:43

    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.
    The Journal of biological chemistry, 2005, Feb-11, Volume: 280, Issue:6

    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.
    Circulation research, 2014, Aug-15, Volume: 115, Issue:5

    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