Related Experiment Video
Updated: May 30, 2026

Real-time Quaking-induced Conversion Assay for Detection of CWD Prions in Fecal Material
Published on: September 29, 2017
Calreticulin inhibits prion protein PrP-(23-98) aggregation in vitro
Noriyuki Shiraishi1, Yoko Inai, Yoshiaki Hirano
1Department of Nutrition, Tokai Gakuen University, Nagoya, Japan. shiraish@tokaigakuen-u.ac.jp
Abstract:
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.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Folding Quality Check in the RER
Regulation of the Unfolded Protein Response
The Unfolded Protein Response

