Insulin action rapidly decreases multifunctional protein kinase activity in rat adipose tissue.
Open Access
- 1 September 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (25) , 12677-12681
- https://doi.org/10.1016/s0021-9258(18)37806-2
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Characterization of GSK-M, a glycogen synthase kinase from rat skeletal muscleArchives of Biochemistry and Biophysics, 1987
- After Insulin BindsScience, 1987
- Insulin stimulates the dephosphorylation of phosphothreonine from FAT-PAD ATP-citrate lyaseBiochemical and Biophysical Research Communications, 1984
- Phosphorylation of different sites of acetyl CoA carboxylase by ATP-citrate lyase kinase and cyclic AMP-dependent protein kinaseBiochemical and Biophysical Research Communications, 1983
- Insulin stimulates phosphorylation of a heat-stable protein in rat adipose tissueBiochemical and Biophysical Research Communications, 1983
- Glycogen Synthase from Rabbit Skeletal Muscle; Effect of Insulin on the State of phosphorylation of the Seven Phosphoserine Residues in vivoEuropean Journal of Biochemistry, 1983
- Glycogen Synthase from Rabbit Skeletal MuscleEuropean Journal of Biochemistry, 1982
- The role of protein phosphorylation in neural and hormonal control of cellular activityNature, 1982
- Phosphorylation of ATP‐citrate lyase by a cyclic AMP‐independent protein kinase from a rat liverFEBS Letters, 1981
- Actions of insulin, epinephrine, and dibutyryl adenosine cyclic 5'-monophosphate on fat cell protein phosphorylations. Adenosine cyclic 5'-monophosphate dependent and independent mechanismsBiochemistry, 1975