H
Hiroshi Tokumitsu
Researcher at Okayama University
Publications - 125
Citations - 6689
Hiroshi Tokumitsu is an academic researcher from Okayama University. The author has contributed to research in topics: Protein kinase A & Kinase. The author has an hindex of 41, co-authored 120 publications receiving 6301 citations. Previous affiliations of Hiroshi Tokumitsu include Kagawa University & Nagoya University.
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Journal ArticleDOI
KN-62, 1-[N,O-bis(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenylpiperazi ne, a specific inhibitor of Ca2+/calmodulin-dependent protein kinase II
Hiroshi Tokumitsu,Takashi Chijiwa,Masatoshi Hagiwara,Akihiro Mizutani,Motomu Terasawa,Hiroyoshi Hidaka +5 more
TL;DR: Results suggest that KN-62 affects the interaction between calmodulin and Ca2+/CaM kinase II following inhibition of this kinase activity by directly binding to theCalmodulin binding site of the enzyme but does not affect the cal modulin-independent activity of already autophosphorylated (activated) enzyme.
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Calcium promotes cell survival through CaM-K kinase activation of the protein-kinase-B pathway
TL;DR: A Ca2+/calmodulin-dependent protein kinase kinase (CaM-KK) activates PKB directly, resulting in phosphorylation of BAD on serine residue 136 and the interaction of BAD with protein 14-3-3, which protects cells from apoptosis.
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Calmodulin-Kinases: Modulators of Neuronal Development and Plasticity
TL;DR: Key neuronal functions of the CaMK cascade in signal transduction, gene transcription, synaptic development and plasticity, and behavior are summarized and the technical challenges of mapping cellular protein kinase signaling pathways are discussed.
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Regulation of mitogen-activated protein kinases by a calcium/calmodulin-dependent protein kinase cascade
TL;DR: A new Ca2+-dependent mechanism for regulating MAP kinase pathways and resultant transcription is established byutation of the phosphorylation site in CaM-KIV, which prevented activation of Elk-1, c-Jun, and ATF2 by the CaM kinase cascade.
Journal ArticleDOI
STO-609, a Specific Inhibitor of the Ca2+/Calmodulin-dependent Protein Kinase Kinase
Hiroshi Tokumitsu,Hiroyuki Inuzuka,Yumi Ishikawa,Masahiko Ikeda,Ikutaro Saji,Ryoji Kobayashi +5 more
TL;DR: Results indicate that STO-609 is a selective and cell-permeable inhibitor of CaM-KK and that it may be a useful tool for evaluating the physiological significance of the CaM/calmodulin-dependent protein kinase kinase pathway in vivo as well as in vitro.