Identification of a Novel AMP-activated Protein Kinase β Subunit Isoform That Is Highly Expressed in Skeletal Muscle
Open Access
- 1 May 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (20) , 12443-12450
- https://doi.org/10.1074/jbc.273.20.12443
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- The α1 and α2 isoforms of the AMP‐activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitroFEBS Letters, 1996
- Isoform-specific Purification and Substrate Specificity of the 5′-AMP-activated Protein KinasePublished by Elsevier ,1996
- Non-catalytic - and -Subunit Isoforms of the 5′-AMP-activated Protein KinaseJournal of Biological Chemistry, 1996
- Mammalian AMP-activated Protein Kinase SubfamilyJournal of Biological Chemistry, 1996
- 5′-AMP Activates the AMP-activated Protein Kinase Cascade, and Ca2+/Calmodulin Activates the Calmodulin-dependent Protein Kinase I Cascade, via Three Independent MechanismsJournal of Biological Chemistry, 1995
- The AMP-activated Protein Kinase Gene is Highly Expressed in Rat Skeletal Muscle. Alternative Splicing and Tissue Distribution of the mRNAEuropean Journal of Biochemistry, 1995
- An emerging role for protein kinases: The responses to nutritional and environmental stressCellular Signalling, 1994
- Role of the AMP-activated protein kinase in the cellular stress responseCurrent Biology, 1994
- Purification and characterization of the AMP‐activated protein kinaseEuropean Journal of Biochemistry, 1989
- Tissue distribution of the AMP‐activated protein kinase, and lack of activation by cyclic‐AMP‐dependent protein kinase, studied using a specific and sensitive peptide assayEuropean Journal of Biochemistry, 1989