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Sharron H. Francis
Researcher at Vanderbilt University
Publications - 142
Citations - 10944
Sharron H. Francis is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Phosphodiesterase & CGMP binding. The author has an hindex of 53, co-authored 142 publications receiving 10537 citations. Previous affiliations of Sharron H. Francis include University of Washington.
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Journal ArticleDOI
cGMP-Dependent Protein Kinases and cGMP Phosphodiesterases in Nitric Oxide and cGMP Action
TL;DR: Current therapies that have successfully targeted the NO-signaling pathway include nitrovasodilators, PDE5 inhibitors, and tadalafil for treatment of a number of vascular diseases including angina pectoris, erectile dysfunction, and pulmonary hypertension, and potential for use of these medications in the treatment of other maladies continues to emerge.
Journal ArticleDOI
Mammalian Cyclic Nucleotide Phosphodiesterases: Molecular Mechanisms and Physiological Functions
TL;DR: Recent reported x-ray crystallographic structures have defined features that provide for specificity for cAMP or cGMP in PDE catalytic sites or their GAF domains, as well as mechanisms involved in catalysis, oligomerization, autoinhibition, and interactions with inhibitors.
Book ChapterDOI
Cyclic nucleotide phosphodiesterases: relating structure and function.
TL;DR: The PDE superfamily continues to be a major target for pharmacological intervention in a number of medically important maladies.
Journal ArticleDOI
Cyclic GMP phosphodiesterase-5: target of sildenafil.
TL;DR: The characteristics of PDE5, its relationship to other PDEs, its role in cGMP signaling, and its involvement in the efficacious action of sildenafil on corpus cavernosum and vascular smooth muscle resulting in penile erection are the subjects of this review.
Journal ArticleDOI
Structure and function of cyclic nucleotide-dependent protein kinases
TL;DR: Studies of the heterogeneity, function, and regulation of cAK and cGK have provided insight into the enzymology of diverse protein kinases and into the roles of these kinases in cellular processes.