N-terminal domain of soluble epoxide hydrolase negatively regulates the VEGF-mediated activation of endothelial nitric oxide synthase

AIMS: The mammalian soluble epoxide hydrolase (sEH) has both an epoxide hydrolase and a phosphatase domain. The role of sEH hydrolase activity in the metabolism of epoxyeicosatrienoic acids (EETs) and the activation of endothelial nitric oxide synthase (eNOS) in endothelial cells (ECs) has been well...

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Dettagli Bibliografici
Autori principali: Hou, Hsin-Han, Hammock, Bruce D., Su, Kou-Hui, Morisseau, Christophe, Kou, Yu Ru, Imaoka, Susumu, Oguro, Ami, Shyue, Song-Kun, Zhao, Jin-Feng, Lee, Tzong-Shyuan
Natura: Artigo
Lingua:Inglês
Pubblicazione: Oxford University Press 2012
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Original Articles
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC3243038/
https://ncbi.nlm.nih.gov/pubmed/22072631
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/cvr/cvr267
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