Calreticulin Inhibits Prion Protein PrP-(23–98) Aggregationin Vitro | Zendy

Noriyuki Shiraishi | Zendy; Yoko Inai | Zendy; Yoshiaki Hirano | Zendy; Yoshito Ihara | Zendy

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Calreticulin Inhibits Prion Protein PrP-(23–98) Aggregationin Vitro

Author(s) -

Noriyuki Shiraishi,

Yoko Inai,

Yoshiaki Hirano,

Yoshito Ihara

Publication year - 2011

Publication title -

bioscience biotechnology and biochemistry

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.110287

Subject(s) - calreticulin , in vitro , chemistry , solubilization , protein aggregation , prion protein , amyloid (mycology) , biochemistry , microbiology and biotechnology , biophysics , biology , medicine , endoplasmic reticulum , pathology , inorganic chemistry , disease

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.

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