thioctic acid has been researched along with adenosine monophosphate in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (33.33) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (16.67) | 29.6817 |
2010's | 3 (50.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Christow, CP | 1 |
Craig, DW; Wedding, RT | 1 |
Du, M; Ren, J; Shen, QW; Tong, J; Zhu, MJ | 1 |
Fujiwara, K; Hosaka, H; Maita, N; Nakagawa, A; Okamura-Ikeda, K; Taniguchi, H | 1 |
Bagby, S; Crennell, SJ; Danson, MJ; Dorus, S; Posner, MG; Upadhyay, A; Watson, AJ | 1 |
Cao, X; Cronan, JE | 1 |
6 other study(ies) available for thioctic acid and adenosine monophosphate
Article | Year |
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[Experiments on the influence of metabolites and antimetabolites on the model of Trichomonas vaginalis. V. Relationship between vitamin-B-complexes and Trichomonas vaginalis].
Topics: Adenine; Adenosine Monophosphate; Bacteriological Techniques; Biotin; Carnitine; Choline; Hydrogen-Ion Concentration; Inositol; Models, Biological; Orotic Acid; Pyridoxine; Riboflavin; Thiamine; Thioctic Acid; Trichomonas vaginalis; Vitamin B Complex; Xanthopterin | 1971 |
Regulation of the 2-oxoglutarate dehydrogenase lipoate succinyltransferase complex from cauliflower by nucleotide. Steady state kinetic studies.
Topics: Acyltransferases; Adenosine Monophosphate; Coenzyme A; Hydrogen-Ion Concentration; Ketoglutarate Dehydrogenase Complex; Ketone Oxidoreductases; Kinetics; Multienzyme Complexes; Plants; Succinates; Thioctic Acid | 1980 |
Ca2+/calmodulin-dependent protein kinase kinase is involved in AMP-activated protein kinase activation by alpha-lipoic acid in C2C12 myotubes.
Topics: Acetyl-CoA Carboxylase; Adenosine Monophosphate; Adenosine Triphosphate; AMP-Activated Protein Kinases; Animals; Benzimidazoles; Calcium; Calcium-Calmodulin-Dependent Protein Kinase Kinase; Cell Line; Chelating Agents; Egtazic Acid; Fatty Acids; Isoquinolines; Mice; Mice, Inbred C57BL; Multienzyme Complexes; Muscle Fibers, Skeletal; Muscle, Skeletal; Naphthalimides; Oxidation-Reduction; Phosphorylation; Protein Binding; Protein Kinase Inhibitors; Protein Serine-Threonine Kinases; RNA, Small Interfering; Thioctic Acid | 2007 |
Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.
Topics: Adenosine Monophosphate; Animals; Catalysis; Cattle; Crystallography, X-Ray; Escherichia coli; Ligands; Models, Molecular; Molecular Conformation; Peptide Synthases; Protein Conformation; Protein Interaction Mapping; Protein Structure, Tertiary; Static Electricity; Thioctic Acid; Vitamins | 2010 |
Post-translational modification in the archaea: structural characterization of multi-enzyme complex lipoylation.
Topics: Adenosine Monophosphate; Archaeal Proteins; Binding Sites; Crystallography, X-Ray; Dihydrolipoyllysine-Residue Acetyltransferase; Isoenzymes; Lipoylation; Magnetic Resonance Spectroscopy; Models, Molecular; Multiprotein Complexes; Peptide Synthases; Protein Binding; Protein Conformation; Protein Processing, Post-Translational; Protein Structure, Tertiary; Recombinant Proteins; Substrate Specificity; Thermoplasma; Thioctic Acid | 2013 |
The Streptomyces coelicolor lipoate-protein ligase is a circularly permuted version of the Escherichia coli enzyme composed of discrete interacting domains.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Escherichia coli; Evolution, Molecular; Models, Molecular; Molecular Sequence Data; Peptide Synthases; Phylogeny; Protein Structure, Tertiary; Sequence Alignment; Streptomyces coelicolor; Thioctic Acid | 2015 |