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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Bibliografski detalji
Glavni autori: 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
Format: Artigo
Jezik:Inglês
Izdano: Oxford University Press 2012
Teme:
Original Articles
Online pristup: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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