T
Takehiko Shibata
Researcher at Saitama University
Publications - 29
Citations - 1539
Takehiko Shibata is an academic researcher from Saitama University. The author has contributed to research in topics: DNA & Endonuclease. The author has an hindex of 11, co-authored 29 publications receiving 1486 citations. Previous affiliations of Takehiko Shibata include University of Tokyo.
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An Endoplasmic Reticulum Stress-specific Caspase Cascade in Apoptosis CYTOCHROME c-INDEPENDENT ACTIVATION OF CASPASE-9 BY CASPASE-12
TL;DR: Li et al. as mentioned in this paper showed that recombinant caspase-12 specifically cleaves and activates procaspase 9 in cytosolic extracts, which catalyzes cleavage of -3, which is inhibited by a specific inhibitor.
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Translocation of Bim to the Endoplasmic Reticulum (ER) Mediates ER Stress Signaling for Activation of Caspase-12 during ER Stress-induced Apoptosis
TL;DR: Results suggest that translocation of Bim to the ER in response to ER stress is an important step toward activation of caspase-12 and initiation of the ER stress-specific caspases cascade.
An extended DNA structure through deoxyribose-base stacking induced by RecA protein (homologous genetic recombinationyNMRyNMR spectroscopyytransferred nuclear Overhauser effect)
TL;DR: A three-dimensional structure of the single-stranded DNA bound to RecA protein is determined and this novel structure well explains the axial extension of DNA in the RecA-filaments relative to B-form DNA and leads to a possible interpretation of the role of this extension in homologous pairing.
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Identification of a Caspase-9 Substrate and Detection of Its Cleavage in Programmed Cell Death during Mouse Development *
TL;DR: Immunohistochemical analysis showed that caspase-9 cleaves vimentin in apoptotic cells in the embryonic nervous system and the interdigital regions, consistent with observations that gene knockouts of caspases and its activator, Apaf-1, result in developmental defects in these tissues.
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A possible role of the C-terminal domain of the RecA protein: A gateway model for double-stranded DNA binding
Hitoshi Kurumizaka,Hideki Aihara,Shukuko Ikawa,Takamitsu Kashima,L. Rochelle Bazemore,Katsumi Kawasaki,Akinori Sarai,Charles M. Radding,Takehiko Shibata +8 more
TL;DR: In this paper, the RecA protein has a domain near the C terminus consisting of amino acid residues 270-328 (from the N terminus) and it has been shown that this domain is a part of the gateway through which double-stranded DNA finds a path for direct contact with single-standed DNA within a presynaptic RecA filament in search for homology.