K
Kei Tobiume
Researcher at Hiroshima University
Publications - 35
Citations - 1894
Kei Tobiume is an academic researcher from Hiroshima University. The author has contributed to research in topics: Cell culture & Gene knockdown. The author has an hindex of 18, co-authored 35 publications receiving 1704 citations. Previous affiliations of Kei Tobiume include Nippon Medical School.
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Journal ArticleDOI
p53 regulates glucose metabolism through an IKK-NF-kappaB pathway and inhibits cell transformation.
TL;DR: The results suggest that a positive-feedback loop exists, whereby glycolysis drives IKK–NF-κB activation, and that hyperactivation of this loop by loss of p53 is important in oncogene-induced cell transformation.
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Involvement of ASK1 in Ca2+-induced p38 MAP kinase activation.
Kohsuke Takeda,Atsushi Matsuzawa,Hideki Nishitoh,Kei Tobiume,Satoshi Kishida,Jun Ninomiya-Tsuji,Kunihiro Matsumoto,Hidenori Ichijo +7 more
TL;DR: It is shown that Ca2+ signalling regulates the ASK1–p38 MAP kinase cascade, which is a critical intermediate of Ca2- signalling between CaMKII and p38 MAP Kinase.
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Loss of p53 enhances catalytic activity of IKKβ through O-linked β-N-acetyl glucosamine modification
TL;DR: A novel mechanism for the enhancement of NF-κB activity by loss of p53 is proposed, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
Journal ArticleDOI
Hedgehog signaling overrides p53-mediated tumor suppression by activating Mdm2.
Yoshinori Abe,Eri Oda-Sato,Kei Tobiume,Keiko Kawauchi,Yoichi Taya,Koji Okamoto,Moshe Oren,Nobuyuki Tanaka +7 more
TL;DR: It is found that accumulation of p53 is inhibited by Hh signaling in several human cancer cell lines, suggesting that the Hh pathway may be a powerful accelerator of oncogenesis by activating cell proliferation and inhibiting the p53-mediated anti-cancer barrier induced by oncogenic stress.
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Apoptosis signal-regulating kinase (ASK) 2 functions as a mitogen-activated protein kinase kinase kinase in a heteromeric complex with ASK1
Kohsuke Takeda,Rieko Shimozono,Takuya Noguchi,Tsuyoshi Umeda,Yoshifumi Morimoto,Isao Naguro,Kei Tobiume,Masao Saitoh,Atsushi Matsuzawa,Hidenori Ichijo +9 more
TL;DR: It is shown that ASK2, a highly related serine/threonine kinase to ASK1, also functions as a MAP3K only in a heteromeric complex with AsK1.