Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Insight into binding of phosphodiesterase-9A selective inhibitors by crystal structures and mutagenesis.

Journal of medicinal chemistry - 25 Feb 2010

Wang Huanchen, Luo Xuan, Ye Mengchun, Hou Jing, Robinson Howard, Ke Hengming

Abstract excerpt

PDE9 inhibitors have been studied as therapeutics for treatment of cardiovascular diseases, diabetes, and neurodegenerative disorders. To illustrate the inhibitor selectivity, the crystal structures of the PDE9A catalytic domain in complex with the enantiomers of PDE9 inhibitor 1-(2-chlorophenyl)-6-(3,3,3-trifluoro-2-methylpropyl)-1H-pyrazolo[3,4-d]pyrimidine-4(5H)-one ((R)-BAY73-6691 or (S)-BAY73-6691, 1r or 1s)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 3',5'-Cyclic-AMP Phosphodiesterases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Mutagenesis, Site-Directed

Share to Protein Conformation

Share to Pyrazoles

Share to Pyrimidines

Share to Stereoisomerism

Source

Open in PubMed Open full text

Identifiers

PMID: 20121115
DOI: 10.1021/jm901519f
PMCID: PMC2831206

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insight into binding of phosphodiesterase-9A selective inhibitors by crystal structures and mutagenesis.PMID 20121115Read ↗

Identification of inhibitor binding sites of the cAMP-specific phosphodiesterase 4.Semantic proximity Read ↗

Critical amino acids in phosphodiesterase-5 catalytic site that provide for high-affinity interaction with cyclic guanosine monophosphate and inhibitors.Semantic proximity Read ↗

Structural asymmetry of phosphodiesterase-9, potential protonation of a glutamic acid, and role of the invariant glutamine.Semantic proximity Read ↗

Chemical Space Exploration and Machine Learningbased Screening of PDE7A InhibitorsSemantic proximity Read ↗

A GIBAC-based selectivity strategy for the design of PDE5 inhibitors to minimize visual disturbancesSemantic proximity Read ↗

Molecular study of mechanisms of action of cilostazol on certain families of phosphodiesterasesSemantic proximity Read ↗

Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity.Semantic proximity Read ↗

Molecular docking of competitive phosphodiesterase inhibitors.Semantic proximity Read ↗

1-(2,6-Dibenzyloxybenzoyl)-3-(9H-fluoren-9-yl)-urea: a novel cyclophilin A allosteric activator.Semantic proximity Read ↗

Molecular modeling of two CYP2C19 SNPs and its implications for personalized drug design.Semantic proximity Read ↗

In Silico Elucidation of C- and N-Domain Selectivity of Dihydropyrimidinone Derivatives as Angiotensin-Converting Enzyme InhibitorsSemantic proximity Read ↗

Structural insight into substrate specificity of phosphodiesterase 10.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.