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Kei Tobiume
Researcher at Tokyo Medical and Dental University
Publications - 11
Citations - 5915
Kei Tobiume is an academic researcher from Tokyo Medical and Dental University. The author has contributed to research in topics: ASK1 & MAP kinase kinase kinase. The author has an hindex of 8, co-authored 9 publications receiving 5654 citations. Previous affiliations of Kei Tobiume include Japanese Foundation for Cancer Research.
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Journal ArticleDOI
Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1.
Masao Saitoh,Hideki Nishitoh,Makiko Fujii,Kohsuke Takeda,Kei Tobiume,Yasuhiro Sawada,Masahiro Kawabata,Kohei Miyazono,Hidenori Ichijo +8 more
TL;DR: Evidence that Trx is a negative regulator of ASK1 suggests possible mechanisms for redox regulation of the apoptosis signal transduction pathway as well as the effects of antioxidants against cytokine‐ and stress‐induced apoptosis.
Journal ArticleDOI
ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
Hideki Nishitoh,Atsushi Matsuzawa,Kei Tobiume,Kaoru Saegusa,Kohsuke Takeda,Kiyoshi Inoue,Seiji Hori,Seiji Hori,Akira Kakizuka,Akira Kakizuka,Hidenori Ichijo +10 more
TL;DR: It is suggested that ASK1 is a key element in ER stress-induced cell death that plays an important role in the neuropathological alterations in polyQ diseases.
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ASK1 is required for sustained activations of JNK/p38 MAP kinases and apoptosis
Kei Tobiume,Atsushi Matsuzawa,Takumi Takahashi,Hideki Nishitoh,Kei Ichi Morita,Kohsuke Takeda,Osamu Minowa,Kohei Miyazono,Tetsuo Noda,Hidenori Ichijo +9 more
TL;DR: It is shown that by deleting ASK1 in mice, TNF‐ and H2O2‐induced sustained activations of JNK and p38 are lost inASK1−/− embryonic fibroblasts, and that ASK 1−-/− cells are resistant to TNF- and H1N1‐induced apoptosis.
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Activation of apoptosis signal-regulating kinase 1 by the stress-induced activating phosphorylation of pre-formed oligomer.
TL;DR: It is shown that phosphorylation of Thr845 at the activation loop is essential for ASK1 to be activated by H2O2, and it is proposed that this potential Thr8 45 kinase may be an ignition kinase that triggers Thr 845 phosphorylated in oligomerized and activation‐competent forms of AsK1.
Journal ArticleDOI
Negative feedback regulation of ASK1 by protein phosphatase 5 (PP5) in response to oxidative stress.
Kei-ichi Morita,Masao Saitoh,Kei Tobiume,Hiroshi Matsuura,Shoji Enomoto,Hideki Nishitoh,Hidenori Ichijo +6 more
TL;DR: PP5 appears to act as a physiological inhibitor of ASK1–JNK/p38 pathways by negative feedback and inhibited not only H2O2‐induced sustained activation of AsK1 but also ASK 1‐dependent apoptosis.