Search results
Results From The WOW.Com Content Network
Phosphodiesterase enzymes have been shown to be different in different types of cells, including normal and leukemic lymphocytes [11] and are often targets for pharmacological inhibition due to their unique tissue distribution, structural properties, and functional properties.
A phosphodiesterase inhibitor is a drug that blocks one or more of the five subtypes of the enzyme phosphodiesterase (PDE), thereby preventing the inactivation of the intracellular second messengers, cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP) by the respective PDE subtype(s). The ubiquitous presence of this ...
Phosphodiesterase 9 inhibitors or PDE9 inhibitors are a class of drugs that work by inhibiting the activity of PDE9. The first compound with this effect, BAY 73-6691 , was reported in 2004. [ 1 ] PDE9 inhibitors are under investigation for the treatment of obesity, [ 2 ] hepatic fibrosis , [ 3 ] Alzheimer's disease , schizophrenia , other ...
PDE3 is a phosphodiesterase. The PDEs belong to at least eleven related gene families , which are different in their primary structure , substrate affinity , responses to effectors , and regulation mechanism .
Phosphodiesterase 1, PDE1, EC 3.1.4.1, systematic name oligonucleotide 5 ′-nucleotidohydrolase) is a phosphodiesterase enzyme also known as calcium- and calmodulin-dependent phosphodiesterase. It is one of the 11 families of phosphodiesterase (PDE1-PDE11).
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A is an enzyme that in humans is encoded by the PDE10A gene. [ 5 ] [ 6 ] Various cellular responses are regulated by the second messengers cAMP and cGMP .
1.1 cGMP phosphodiesterase inhibitors. 2 See also. 3 Sources. Toggle the table of contents. ... This page was last edited on 9 February 2024, at 00:17 (UTC).
The crystal structure of the active site of the PDE2 enzyme has been reported. [4] Even though amino acid sequences, for members of the PDE family show considerable difference (25-35% identity), the overall folding, functional and structural elements of the active sites are very similar.