Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity.

@article{Scapin2004CrystalSO,
  title={Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity.},
  author={Giovanna Scapin and Sangita B Patel and Christine C Chung and Jeffrey P Varnerin and Scott D. Edmondson and Anthony Mastracchio and Emma R. Parmee and Suresh B. Singh and Joseph W. Becker and Lex H. T. van der Ploeg and Michael R Tota},
  journal={Biochemistry},
  year={2004},
  volume={43 20},
  pages={
          6091-100
        }
}
Phosphodiesterases (PDEs) are enzymes that modulate cyclic nucleotide signaling and as such are clinical targets for a range of disorders including congestive heart failure, erectile dysfunction, and inflammation. The PDE3 family comprises two highly homologous subtypes expressed in different tissues, and inhibitors of this family have been shown to increase lipolysis in adipocytes. A specific PDE3B (the lipocyte-localized subtype) inhibitor would be a very useful tool to evaluate the effects… CONTINUE READING
Highly Cited
This paper has 18 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 11 extracted citations

cUMP hydrolysis by PDE3B

Naunyn-Schmiedeberg's Archives of Pharmacology • 2018
View 4 Excerpts
Highly Influenced