An Essential Aspartic Acid at Each of Two Allosteric cGMP-binding Sites of a cGMP-specific Phosphodiesterase
Open Access
- 1 December 1995
- journal article
- research article
- Published by Elsevier
- Vol. 270 (51), 30671-30679
- https://doi.org/10.1074/jbc.270.51.30671
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- The structure of a bovine lung cGMP-binding, cGMP-specific phosphodiesterase deduced from a cDNA clone.Published by Elsevier ,1993
- Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase.Proceedings of the National Academy of Sciences, 1992
- Structure and function studies of the cGMP-stimulated phosphodiesterase.Published by Elsevier ,1991
- Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brainBiochemistry, 1991
- Bovine cone photoreceptor cGMP phosphodiesterase structure deduced from a cDNA clone.Proceedings of the National Academy of Sciences, 1990
- 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
- cGMP is tightly bound to bovine retinal rod phosphodiesterase.Proceedings of the National Academy of Sciences, 1989
- Cyclic GMP phosphodiesterase from bovine retina Amino acid sequence of the α‐subunit and nucleotide sequence of the corresponding cDNAFEBS Letters, 1987
- Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species.Proceedings of the National Academy of Sciences, 1986
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977