Compounds > lysine
Page last updated: 2024-08-17

lysine and malonyl coenzyme a

lysine has been researched along with malonyl coenzyme a in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (12.50)18.2507
2000's2 (25.00)29.6817
2010's3 (37.50)24.3611
2020's2 (25.00)2.80

Authors

AuthorsStudies
Katiyar, SS; Mukherjee, S1
Cohen, I; Fève, B; Girard, J; Guillerault, F; Pan, Y; Prip-Buus, C1
Dai, J; Haro, D; Marrero, PF; Napal, L; Treber, M; Woldegiorgis, G1
Cheng, Z; Colak, G; Dai, L; de Boer, VC; Huang, H; Liu, X; Locasale, JW; Lombard, DB; Park, J; Pougovkina, O; Tan, M; Te Brinke, H; Wan, X; Wanders, RJ; Yue, WW; Zhao, Y1
Hirschey, MD; Wagner, GR1
Carpenter, S; Carroll, RG; Covarrubias, S; Galván-Peña, S; Haneklaus, M; Hinchy, EC; James, AM; Kelly, VP; Modis, LK; Murphy, MP; Nadin, A; Newman, C; O'Neill, LA; Palsson-McDermott, E; Robinson, EK1
Bao, X; Hou, J; Hou, Y; Huang, M; Qi, Q; Qiu, C; Shen, Y; Tao, H; Zhao, J1
Benton, HP; Benzing, T; Bleich, M; Cravatt, BF; Demir, F; Dissanayake, LV; Domingo-Almenara, X; El-Meanawy, A; Gliozzi, ML; Golosova, D; Guijas, C; Himmerkus, N; Hoehne, M; Jaegers, J; Kok, BP; Krüger, M; Palermo, A; Palygin, O; Rinschen, MM; Saez, E; Schafroth, MA; Siuzdak, G; Staruschenko, A; Weisz, OA; Xue, J1

Other Studies

8 other study(ies) available for lysine and malonyl coenzyme a

ArticleYear
Inactivation of enoyl-CoA reductase in pigeon liver fatty acid synthetase by pyridoxal 5'-phosphate: evidence for the presence of one lysine residue at the active site.
    Journal of enzyme inhibition, 1998, Volume: 13, Issue:3

    Topics: Acetyl Coenzyme A; Animals; Binding Sites; Columbidae; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); Enzyme Inhibitors; Fatty Acid Synthases; Kinetics; Liver; Lysine; Malonyl Coenzyme A; Oxidoreductases; Pyridoxal Phosphate; Spectrometry, Fluorescence

1998
The extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA sensitivity but in initial protein folding.
    The Journal of biological chemistry, 2002, Dec-06, Volume: 277, Issue:49

    Topics: Amino Acid Sequence; Animals; Blotting, Western; Carnitine O-Palmitoyltransferase; DNA, Complementary; Dose-Response Relationship, Drug; Gene Deletion; Humans; Immunoblotting; Inhibitory Concentration 50; Kinetics; Liver; Lysine; Malonyl Coenzyme A; Mitochondria; Molecular Sequence Data; Mutation; Plasmids; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Rats; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Subcellular Fractions; Trypsin

2002
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.
    The Journal of biological chemistry, 2003, Sep-05, Volume: 278, Issue:36

    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
Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation.
    Molecular & cellular proteomics : MCP, 2015, Volume: 14, Issue:11

    Topics: Animals; Carboxy-Lyases; Cell Line; Fatty Acids; Fibroblasts; Humans; Liver; Lysine; Male; Malonates; Malonyl Coenzyme A; Metabolism, Inborn Errors; Methylmalonic Acid; Mice; Mice, Knockout; Mitochondria; Models, Molecular; Oxidation-Reduction; Sirtuins

2015
A Prob(e)able Route to Lysine Acylation.
    Cell chemical biology, 2017, 02-16, Volume: 24, Issue:2

    Topics: Acyl Coenzyme A; Acylation; Lysine; Malonyl Coenzyme A; Proteins

2017
Malonylation of GAPDH is an inflammatory signal in macrophages.
    Nature communications, 2019, 01-18, Volume: 10, Issue:1

    Topics: Animals; Cytokines; Glyceraldehyde-3-Phosphate Dehydrogenases; HEK293 Cells; Humans; Inflammation; Inflammation Mediators; Lipopolysaccharides; Lysine; Macrophages; Malonyl Coenzyme A; Mice, Inbred C57BL; Mutagenesis; Polyribosomes; RNA-Binding Proteins; RNA, Messenger; RNA, Small Interfering; Tumor Necrosis Factor-alpha

2019
Biosensor-Coupled
    mSystems, 2022, 04-26, Volume: 7, Issue:2

    Topics: Arginine; Biosensing Techniques; Carbohydrates; Lysine; Malonyl Coenzyme A; Mutagenesis; Saccharomyces cerevisiae

2022
Accelerated lysine metabolism conveys kidney protection in salt-sensitive hypertension.
    Nature communications, 2022, 07-14, Volume: 13, Issue:1

    Topics: Albumins; Animals; Carbon; Disease Models, Animal; Hypertension; Kidney; Lysine; Malonyl Coenzyme A; Rats

2022