Autophosphorylation of cGMP-dependent protein kinase is stimulated only by occupancy of one the two cGMP binding sites
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(83)80315-9/fullpdf
Reference7 articles.
1. Characterization of Phosphorylated and Native cGMP-Dependent Protein Kinase
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1. Catalytic Activity of cGMP-Dependent Protein Kinase Type I in Intact Cells Is Independent of N-Terminal Autophosphorylation;PLoS ONE;2014-06-04
2. Nitration of Tyrosine 247 Inhibits Protein Kinase G-1α Activity by Attenuating Cyclic Guanosine Monophosphate Binding;Journal of Biological Chemistry;2014-03
3. Aromatic l-amino acid decarboxylase phosphorylation and activation by PKGIαin vitro;Journal of Neurochemistry;2010-04-29
4. Molecular mechanisms that could contribute to prolonged effectiveness of PDE5 inhibitors to improve erectile function;International Journal of Impotence Research;2008-04-17
5. Distinguishing the Roles of the Two Different cGMP-binding Sites for Modulating Phosphorylation of Exogenous Substrate (Heterophosphorylation) and Autophosphorylation of cGMP-dependent Protein Kinase;Journal of Biological Chemistry;2000-01
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