Phosphorylation of Isolated Human Phosphodiesterase-5 Regulatory Domain Induces an Apparent Conformational Change and Increases cGMP Binding Affinity
Open Access
- 1 December 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (49), 47581-47587
- https://doi.org/10.1074/jbc.m206088200
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Specific cGMP binding by the cGMP binding domains of cGMP-binding cGMP specific phosphodiesteraseCellular Signalling, 2001
- Rapid nitric oxide–induced desensitization of the cGMP response is caused by increased activity of phosphodiesterase type 5 paralleled by phosphorylation of the enzymeThe Journal of cell biology, 2001
- Phosphorylation of phosphodiesterase‐5 by cyclic nucleotide‐dependent protein kinase alters its catalytic and allosteric cGMP‐binding activitiesEuropean Journal of Biochemistry, 2000
- Regulation of cAMP and cGMP signaling: new phosphodiesterases and new functionsCurrent Opinion in Cell Biology, 2000
- Binding of cGMP to both allosteric sites of cGMP-binding cGMP-specific phosphodiesterase (PDE5) is required for its phosphorylationBiochemical Journal, 1998
- The GAF domain: an evolutionary link between diverse phototransducing proteinsTrends in Biochemical Sciences, 1997
- An Essential Aspartic Acid at Each of Two Allosteric cGMP-binding Sites of a cGMP-specific PhosphodiesterasePublished by Elsevier ,1995
- The structure of a bovine lung cGMP-binding, cGMP-specific phosphodiesterase deduced from a cDNA clone.Published by Elsevier ,1993
- Structure and function studies of the cGMP-stimulated phosphodiesterase.Published by Elsevier ,1991
- Identification of a noncatalytic cGMP-binding domain conserved in both the cGMP-stimulated and photoreceptor cyclic nucleotide phosphodiesterases.Proceedings of the National Academy of Sciences, 1990