Activation by Autophosphorylation or cGMP Binding Produces a Similar Apparent Conformational Change in cGMP-dependent Protein Kinase
Open Access
- 1 June 1998
- journal article
- Published by Elsevier
- Vol. 273 (23) , 14649-14656
- https://doi.org/10.1074/jbc.273.23.14649
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductasesPublished by Elsevier ,2003
- Ligand-Induced Conformational Changes in Cyclic Nucleotide Phosphodiesterases and Cyclic Nucleotide-Dependent Protein KinasesMethods, 1998
- Identification of Critical Determinants for Autoinhibition in the Pseudosubstrate Region of Type Iα cAMP-dependent Protein KinasePublished by Elsevier ,1997
- A Protein Phosphorylation Switch at the Conserved Allosteric Site in GPScience, 1996
- Arginine 75 in the Pseudosubstrate Sequence of Type Iβ cGMPdependent Protein Kinase Is Critical for Autoinhibition, Although Autophosphorylated Serine 63 Is Outside This SequencePublished by Elsevier ,1996
- Autophosphorylation: a salient feature of protein kinasesMolecular and Cellular Biochemistry, 1993
- Autophosphorylation of Mucor rouxii cAMP-dependent protein kinase and its role in holoenzyme activationCellular Signalling, 1992
- Identification of the residues on cyclic GMP-dependent protein kinase that are autophosphorylated in the presence of cyclic AMP and cyclic GMPBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Characterization of Phosphorylated and Native cGMP‐Dependent Protein KinaseEuropean Journal of Biochemistry, 1983
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965