Malonyl-CoA Decarboxylase Is Not a Substrate of AMP-Activated Protein Kinase in Rat Fast-Twitch Skeletal Muscle or an Islet Cell Line
- 1 December 2001
- journal article
- Published by Elsevier BV in Archives of Biochemistry and Biophysics
- Vol. 396 (1), 71-79
- https://doi.org/10.1006/abbi.2001.2589
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Reduced Food Intake and Body Weight in Mice Treated with Fatty Acid Synthase InhibitorsScience, 2000
- Dealing with energy demand: the AMP-activated protein kinaseTrends in Biochemical Sciences, 1999
- REGULATION OF MAMMALIAN ACETYL-COENZYME A CARBOXYLASEAnnual Review of Nutrition, 1997
- The AMP‐Activated Protein KinaseEuropean Journal of Biochemistry, 1997
- Contraction-induced Changes in Acetyl-CoA Carboxylase and 5′-AMP-activated Kinase in Skeletal MuscleJournal of Biological Chemistry, 1997
- The Mitochondrial Carnitine Palmitoyltransferase System — From Concept to Molecular AnalysisEuropean Journal of Biochemistry, 1997
- Critical phosphorylation sites for acetyl-CoA carboxylase activity.Journal of Biological Chemistry, 1994
- Acetyl-CoA carboxylase regulation of fatty acid oxidation in the heart.Journal of Biological Chemistry, 1993
- Regulation of mitochondrial carnitine palmitoyl transferases from liver and extrahepatic tissuesAdvances in Enzyme Regulation, 1992
- Observations on the affinity for carnitine, and malonyl-CoA sensitivity, of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the ratBiochemical Journal, 1983