adenosine monophosphate has been researched along with sto 609 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 |
|---|---|
| Carling, D; Carlson, M; Dickerson, K; Heath, R; Hong, SP; Johnstone, SR; Momcilovic, M; Woods, A | 1 |
| Du, M; Ren, J; Shen, QW; Tong, J; Zhu, MJ | 1 |
| Cao, PR; Gu, M; Li, J; Li, JY; Nan, FJ; Pang, T; Qiu, BY; Shao, W; Su, MB; Yu, LF; Zhang, ZS | 1 |
| Hanley-Bowdoin, L; Reyes, MI; Shen, W | 1 |
4 other study(ies) available for adenosine monophosphate and sto 609
| Article | Year |
|---|---|
Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells.
Topics: 3T3 Cells; Adenosine Monophosphate; AMP-Activated Protein Kinases; Animals; Benzimidazoles; Calcium; Calcium-Calmodulin-Dependent Protein Kinase Kinase; Enzyme Activation; Fibroblasts; HeLa Cells; Humans; Hydrogen Peroxide; Ionomycin; Isoenzymes; Isoquinolines; Mice; Multienzyme Complexes; Naphthalimides; Phosphorylation; Protein Serine-Threonine Kinases; Rats; Saccharomyces cerevisiae; Signal Transduction; Sorbitol | 2005 |
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 |
Small molecule antagonizes autoinhibition and activates AMP-activated protein kinase in cells.
Topics: Acetyl-CoA Carboxylase; Adenosine Monophosphate; Adenosine Triphosphate; AMP-Activated Protein Kinase Kinases; AMP-Activated Protein Kinases; Benzimidazoles; Diabetes Mellitus, Type 2; Energy Metabolism; Enzyme Activation; Enzyme Activators; HeLa Cells; Humans; Multienzyme Complexes; Myoblasts; Naphthalimides; Obesity; Phosphorylation; Protein Serine-Threonine Kinases; Protein Structure, Quaternary; Pyrazoles; Pyrimidines; Time Factors | 2008 |
Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate SnRK1 by phosphorylating its activation loop.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Arabidopsis; Arabidopsis Proteins; Benzimidazoles; Cations; Conserved Sequence; Enzyme Activation; Molecular Sequence Data; Naphthalimides; Phosphorylation; Phosphothreonine; Protein Binding; Protein Serine-Threonine Kinases; Substrate Specificity | 2009 |