分子シャペロンとプロテアソーム : タンパク質の生成と分解をコントロールする仕組み(セミナー「ストレスと生物の応答・適応 : その分子・細胞機構と応用」)
スポンサーリンク
概要
- 論文の詳細を見る
We have shown that the 90-kDa heat shock protein (Hsp90) is able to bind partially unfolded firefly luciferase and maintain it in a refoldable state, and that the subsequent successive action of the 20S proteasome activator, PA28, Hsc70 and Hsp40 enables the refolding of the unfolded luciferase. It is most plausible that both the N- and C-terminal chaperone sites of Hsp90 participate in this protein refolding pathway.
- 低温生物工学会の論文
- 2003-08-30