Calreticulin Inhibits Prion Protein PrP-(23–98) Aggregation in Vitro
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概要
- 論文の詳細を見る
Because prion protein PrP-(23–98) was recently found to polymerize into amyloid-like and proteinase K-resistant spherical aggregates in the presence of NADPH plus copper ions, we tested to determine whether calreticulin (CRT) inhibits PrP-(23–98) aggregation in vitro. The results indicated that CRT suppressed PrP-(23–98) aggregation, and that CRT-mediated solubilization occurred in the aggregates.
- 社団法人 日本農芸化学会の論文
著者
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Ihara Yoshito
Department of Biochemistry and Molecular Biology in Disease
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Hirano Yoshiaki
Department Of Applied Chemistry Faculty Of Engineering Osaka Institute Of Technology
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Shiraishi Noriyuki
Department Of Biochemistry Wakayama Medical University
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Inai Yoko
Department Of Biochemistry Wakayama Medical University
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