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Yoshitatsu Sei

Researcher at National Institutes of Health

Publications -  75
Citations -  3532

Yoshitatsu Sei is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Ryanodine receptor & Receptor. The author has an hindex of 32, co-authored 73 publications receiving 3390 citations. Previous affiliations of Yoshitatsu Sei include University of Eastern Finland & Uniformed Services University of the Health Sciences.

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Early increases in TNF-α, IL-6 and IL-1β levels following transient cerebral ischemia in gerbil brain

TL;DR: The effects of transient global ischemia using bilateral carotid artery occlusion on regional cytokine levels in gerbil brain were investigated using enzyme-linked immunoassay techniques.
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The G-Protein−Coupled Receptor GPR40 Directly Mediates Long-Chain Fatty Acid−Induced Secretion of Cholecystokinin

TL;DR: Long-chain fatty acid receptor GPR40 induces secretion of CCK by I cells in response to dietary fat, and olive oil gavage significantly increased plasma levels ofCCK compared with pregavage levels.
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DISC1 splice variants are upregulated in schizophrenia and associated with risk polymorphisms.

TL;DR: The results implicate a molecular mechanism of genetic risk associated with DISC1 involving specific alterations in gene processing, and suggest that truncated DISC 1 proteins were expressed more abundantly during fetal development than during postnatal ages.
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Induction of Apoptosis in HL-60 Human Promyelocytic Leukemia Cells by Adenosine A3Receptor Agonists☆

TL;DR: Results suggest that activation of ADO A(3) receptors is responsible for the ADO-induced apoptosis in HL-60 cells and could be of potential therapeutic value in the treatment of leukemia.
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The extracellular calcium sensing receptor is required for cholecystokinin secretion in response to L-phenylalanine in acutely isolated intestinal I cells

TL;DR: The present data suggest that CaSR is required for hormone secretion in the specific response to L-Phe by the native I cell, and that a receptor-mediated mechanism may inhibit hormone release in the absence of a fully functional CaSR.