Catalytic subunits of the porcine and rat 5′-AMP-activated protein kinase are members of the SNF1 protein kinase family
- 1 April 1995
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Vol. 1266 (1) , 73-82
- https://doi.org/10.1016/0167-4889(94)00222-z
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinasePublished by Elsevier ,2003
- A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesisPublished by Wiley ,2001
- Structure and expression of a gene from Arabidopsis thaliana encoding a protein related to SNF1 protein kinaseGene, 1992
- Molecular analyses of a barley multigene family homologous to the yeast protein kinase gene SNF1The Plant Journal, 1992
- Phosphorylation and inactivation of HMG‐CoA reductase at the AMP‐activated protein kinase site in response to fructose treatment of isolated rat hepatocytesFEBS Letters, 1992
- Regulation of intracellular acetyl-CoA carboxylase by ATP depletors mimics the action of the 5′-AMP-activated protein kinaseBiochemical and Biophysical Research Communications, 1991
- Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP‐activated protein kinaseEuropean Journal of Biochemistry, 1991
- Basic local alignment search toolJournal of Molecular Biology, 1990
- Regulation of fatty acid synthesis via phosphorylation of acetyl-CoA carboxylaseProgress in Lipid Research, 1989
- A Method for Isolation of Intact, Translationally Active Ribonucleic AcidDNA, 1983