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Natsuo Ueda

Researcher at Kagawa University

Publications -  171
Citations -  10059

Natsuo Ueda is an academic researcher from Kagawa University. The author has contributed to research in topics: Anandamide & Cannabinoid receptor. The author has an hindex of 51, co-authored 163 publications receiving 9377 citations. Previous affiliations of Natsuo Ueda include University of Tokushima & Osaka City University.

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Molecular characterization of a phospholipase D generating anandamide and its congeners.

TL;DR: It is confirmed that a specific phospholipase D is responsible for the generation of N-acylethanolamines including anandamide, strongly suggesting the physiological importance of lipid molecules of this class.
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Transcriptional Roles of Nuclear Factor κB and Nuclear Factor-Interleukin-6 in the Tumor Necrosis Factor α-Dependent Induction of Cyclooxygenase-2 in MC3T3-E1 Cells (∗)

TL;DR: Data suggested a potential role of both NF-IL6 and NFκB in the induction of cyclooxygenase-2 by TNFα, as judged by the inhibitory effect of NS398, Western blotting, and Northern blotting.
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Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand

TL;DR: The results suggest that anandamide and 2‐arachidonoylglycerol can be inactivated by the same enzyme.
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The fatty acid amide hydrolase (FAAH)

TL;DR: The fatty acid amide hydrolase (FAAH), is the enzyme responsible for the hydrolysis of anandamide, an endocannabinoid, and a large number of inhibitors have been synthesized and tested since 1994 and these are reviewed in terms of reversibility, potency, and specificity.
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Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase.

TL;DR: Comb complementary DNA cloning and functional expression of the enzyme termed “N-acylethanolamine-hydrolyzing acid amidase (NAAA)” from human, rat, and mouse demonstrated that NAAA is a novel N-acyleddylamine-Hydrolyzed enzyme that shows structural and functional similarity to acid ceramidase.