Mini reviewMolecular biology of the cyclic AMP-specific cyclic nucleotide phosphodiesterases: A diverse family of regulatory enzymes
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Cited by (131)
The long and winding road of designing phosphodiesterase inhibitors for the treatment of heart failure
2021, European Journal of Medicinal ChemistryCitation Excerpt :In general, PDEs are found in their dimeric form through the association of two enzymatic subunits [7]. The monomeric structure of all isoforms is composed by 3 distinct domains: a catalytic, an N-terminal, and a C-terminal domains [8–10]. The C-terminal domain is conserved in all PDE families, with the exception of PDE6, which shares 18–46% homology [11].
Phosphodiesterase inhibitors say NO to Alzheimer's disease
2019, Food and Chemical ToxicologySyntheses of PDE3A inhibitor ORG9935 and determination of the absolute stereochemistries of its enantiomers by X-ray crystallography
2018, TetrahedronCitation Excerpt :The cyclic nucleotide phosphodiesterase (PDE) families,1,2 are associated with a variety biological processes such as inflammation, ion channel function, muscle contraction, differentiation, apoptosis, lipogenesis, glycogenolysis, and gluconeogenesis.3
The human area postrema and other nuclei related to the emetic reflex express cAMP phosphodiesterases 4B and 4D
2010, Journal of Chemical Neuroanatomy
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