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Motoko Ohnishi

Researcher at Chubu University

Publications -  40
Citations -  1059

Motoko Ohnishi is an academic researcher from Chubu University. The author has contributed to research in topics: Phosphatase & Protein phosphatase 2. The author has an hindex of 16, co-authored 39 publications receiving 1008 citations. Previous affiliations of Motoko Ohnishi include Tohoku University.

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Journal ArticleDOI

Regulation of the TAK1 Signaling Pathway by Protein Phosphatase 2C

TL;DR: Results indicate that PP2Cβ negatively regulates the TAK1 signaling pathway by direct dephosphorylation of TAK2 in vitro and in vivo.
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Quercetin suppresses bone resorption by inhibiting the differentiation and activation of osteoclasts.

TL;DR: The results suggest that osteoclast progenitors as well as mature osteoclasts, are quercetin's target cells in relation to bone resorption, and that quercETin's suppressive effect on bone Resorption results from both its inhibitory effect on the differentiation of osteoc last progenitor cells into pOCs and from its disruptive effect on actin rings in mature osteclasts.
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Selective suppression of stress-activated protein kinase pathway by protein phosphatase 2C in mammalian cells

TL;DR: The results suggest that PP2C selectively inhibits the SAPK pathways through suppression of MKK3b, MKK4,MKK6b and MKK7 activities in mammalian cells.
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Regulation of stress-activated protein kinase signaling pathways by protein phosphatases.

TL;DR: The properties of the proteinosphatases responsible for the regulation of SAPK signaling pathways are described and differences in substrate specificities and regulatory mechanisms for these phosphatases form the molecular basis for the complex regulation ofSAPK signaling.
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Enrichment and efficient screening of ES cells containing a targeted mutation: the use of DT-A gene with the polyadenylation signal as a negative selection maker.

TL;DR: The results indicate that the use of DT‐ApA for negative selection together with the application of LA‐PCR for screening ensures efficient and time‐saving screening for homologous recombinants.