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Vincent C. Manganiello

Researcher at National Institutes of Health

Publications -  198
Citations -  12986

Vincent C. Manganiello is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Phosphodiesterase & Phosphodiesterase 3. The author has an hindex of 60, co-authored 198 publications receiving 12328 citations. Previous affiliations of Vincent C. Manganiello include Lund University & Vanderbilt University.

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Foxp3-dependent programme of regulatory T-cell differentiation

TL;DR: Although its function is required for Tr cell suppressor activity, Foxp3 to a large extent amplifies and fixes pre-established molecular features of Tr cells, including anergy and dependence on paracrine IL-2.
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Advances in targeting cyclic nucleotide phosphodiesterases

TL;DR: Pharmaceutical interest in PDEs has been reignited by the increasing understanding of the roles of individual P DEs in regulating the subcellular compartmentalization of specific cyclic nucleotide signalling pathways, by the structure-based design of novel specific inhibitors and by the development of more sophisticated strategies to target individual PDE variants.
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Structure, localization, and regulation of cGMP-inhibited phosphodiesterase (PDE3).

TL;DR: This review emphasizes the PDE3 family, including structure-function information and regulation of the adipocyte PDE2, which plays a key role in the antilipolytic action of insulin, and other aspects of different PDE families will be discussed.
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Tumor Necrosis Factor-α Stimulates Lipolysis in Differentiated Human Adipocytes Through Activation of Extracellular Signal-Related Kinase and Elevation of Intracellular cAMP

TL;DR: It is suggested that in human adipocytes, TNF-alpha stimulates lipolysis through activation of MEK-ERK and subsequent increase in intracellular cAMP and the increase was abrogated by PD98059.
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Cyclic nucleotide phosphodiesterase 3A–deficient mice as a model of female infertility

TL;DR: Findings provide the first genetic evidence indicating that resumption of meiosis in vivo and in vitro requires PDE3A activity, which underscores inhibition of oocyte maturation as a potential strategy for contraception.