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cAMP-dependent protein kinase

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cAMP-dependent protein kinase
a tetrameric protein composed of two regulatory subunits that bind cAMP, and two catalytic subunits that catalyze the transfer of a phosphoryl group from ATP to a target enzyme.
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Activation of the GLP-1 receptor results in the stimulation of adenylyl cyclase, leading to an increase in intracellular cyclic adenosine monophosphate (cAMP) and the cAMP-dependent protein kinase A (PKA) activation in the pancreatic tissue [10,11,14,22].
Effects of extracellular matrix proteins on expansion, proliferation ... by Adams, Gary G.; Cui, Yu-Xin / Journal of Biomedical Science and Engineering (JBiSE)
In this study we established cooperative interaction between substrate binding sites of the cAMP-dependent protein kinase catalytic subunit (protein kinase A, EC 2.
Single-subunit allostery in the kinetics of peptide phosphorylation ... by Kuznetsov, Aleksei; Jarv, Jaak / Proceedings of the Estonian Academy of Sciences
But the trio acted synergistically to upregulate a regulatory subunit of cAMP-dependent protein kinase, a ubiquitous protein involved in neurologic pathways and a key regulator of neuronal growth in the clam embryo model.
Triple threat activates neurons by Potera, Carol / Environmental Health Perspectives
 
 
 
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