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Hideyo Sato

Researcher at Niigata University

Publications -  96
Citations -  8149

Hideyo Sato is an academic researcher from Niigata University. The author has contributed to research in topics: Cystine & Glutathione. The author has an hindex of 38, co-authored 93 publications receiving 7018 citations. Previous affiliations of Hideyo Sato include Yamagata University & Iwate University.

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Transcription Factor Nrf2 Coordinately Regulates a Group of Oxidative Stress-inducible Genes in Macrophages

TL;DR: It is shown that Nrf2 controls the expression of a group of electrophile- and oxidative stress-inducible proteins and activities, which includes heme oxygenase-1, A170, peroxiredoxin MSP23, and cystine membrane transport (system xc −) activity.
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Cloning and Expression of a Plasma Membrane Cystine/Glutamate Exchange Transporter Composed of Two Distinct Proteins

TL;DR: In this paper, the authors have isolated cDNA encoding the transporter for system xc- from mouse activated macrophages by expression in Xenopus oocytes, and the sequence analysis revealed that one is identical with the heavy chain of 4F2 cell surface antigen (4F2hc) and the other is a novel protein of 502 amino acids with 12 putative transmembrane domains.
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Electrophile response element-mediated induction of the cystine/glutamate exchange transporter gene expression.

TL;DR: The experiments using the mouse embryonic fibroblasts derived from the Nrf2-deficient mice revealed that the induction of xCT gene by electrophilic agents is mediated by NRF2, and it was demonstrated that xCT is a novel member of this protein family.
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The oxidative stress-inducible cystine/glutamate antiporter, system x (c) (-) : cystine supplier and beyond.

TL;DR: A comprehensive picture from the early days of system xc− research up to now is provided to provide a comprehensive picture of the oxidative stress-inducible cystine/glutamate exchange system and its role in cell signaling and communication.
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Redox Imbalance in Cystine/Glutamate Transporter-deficient Mice

TL;DR: It is demonstrated that system x–c contributes to maintaining the plasma redox balance in vivo but is dispensable in mammalian development, although it is vitally important to cells in vitro.