English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Background The cyclic nucleotide second messengers cAMP and cGMP play key roles in mammalian signal transduction. Their intracellular levels are tightly controlled by the rate of synthesis and degradation. Hydrolysis of the cyclic nucleotides is dependent on the activity of phosphodiesterases (PDE) of which to date 11 families have been identified. The cGMP-stimulated cGMP/cAMP phosphodiesterase 2 is encoded by one gene, which has been shown to be spliced into three variants that have been cloned from different species. Besides the ubiquitous soluble PDE2A1, two membrane associated forms, PDE2A2 and PDE2A3, have been described. The PDE2A splice variants only differ in short stretches of amino acids at their very N terminus. This region has previously been suggested to determine the subcellular localization of the enzyme, but data about the mechanism underlying membrane attachment of PDE2A3 are lacking.

The neuronal PDE2A3 splice variant is targeted to membranes via dual acylation