Efforts of the Professional Development Program at Hiroshima University Towards Fostering Teachers as Continuous Learners : The Case of the Teaching Practice and Development Course

In 2016, the Graduate School of Education at Hiroshima University established the Professional Development Program for Teachers and School Leaders which consists two courses: The Teaching Practice and Development Course and the School Management Course. Focusing on the former, this paper examines its achievements and problems in the first year to develop some perspectives of models for graduate education toward fostering teachers as continuous learners. We discuss from the following four points: a collaborative learning between teacher and non-teacher graduate students; an effective way to learn the basic skills; a circulation of theory and practice; a triumvirate and learning environment on the realization of them.本研究は，JSPS科学研究費補助金基盤研究（B）（一般）「「学び続ける教員」を支えるアクティブ・ラーニング型教員研修プログラムの開発」（JP16H03765）の助成を受けている。本稿は，平成28年度日本教育大学協会研究集会で発表した内容を加筆・修正したものである

2020 年におけるCOVID-19 の状況と看護学部の臨地実習への対応

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Identification of a DYRK1A Inhibitor that Induces Degradation of the Target Kinase using Co-chaperone CDC37 fused with Luciferase nanoKAZ

The protein kinase family includes attractive targets for drug development. Methods for screening of kinase inhibitors remain largely limited to in vitro catalytic assays. It has been shown that ATP-competitive inhibitors antagonize interaction between the target kinase and kinase-specific co-chaperone CDC37 in living cells. Here we show a cell-based method to screen kinase inhibitors using fusion protein of CDC37 with a mutated catalytic 19-kDa component of Oplophorus luciferase, nanoKAZ (CDC37-nanoKAZ). A dual-specificity kinase DYRK1A, an importance of which has been highlighted in Alzheimers disease, was targeted in this study. We established 293T cells stably expressing CDC37-nanoKAZ, and analyzed interaction between CDC37-nanoKAZ and DYRK1A. We revealed that DYRK1A interacted with CDC37-nanoKAZ. Importantly, point mutations that affect autophosphorylation strengthened the interaction, thus improving signal/noise ratio of the interaction relative to non-specific binding of CDC37-nanoKAZ. This high signal/noise ratio enabled screening of chemical library that resulted in identification of a potent inhibitor of DYRK1A, named CaNDY. CaNDY induced selective degradation of DYRK1A, and inhibited catalytic activity of recombinant DYRK1A with IC50 value of 7.9 nM by competing with ATP. This method based on a mutant target kinase and a bioluminescence-eliciting co-chaperone CDC37 could be applicable to evaluation and development of inhibitors targeting other kinases