@article{oai:nagasaki-u.repo.nii.ac.jp:00002144,
 author = {Takatsuki, Hanae and Fuse, Takayuki and Nakagaki, Takehiro and Mori, Tsuyoshi and Mihara, Ban and Takao, Masaki and Iwasaki, Yasushi and Yoshida, Mari and Murayama, Shigeo and Atarashi, Ryuichiro and Nishida, Noriyuki and Satoh, Katsuya},
 journal = {EBioMedicine},
 month = {Oct},
 note = {Human prion diseases are neurodegenerative disorders caused by abnormally folded prion proteins in the central nervous system. These proteins can be detected using the quaking-induced conversion assay. Compared with other bioassays, this assay is extremely sensitive and was used in the present study to determine prion distribution in sporadic Creutzfeldt-Jakob disease patients at autopsy. Although infectivity of the sporadic form is thought to be restricted within the central nervous system, results showed that prion-seeding activities reach 106/g from a 50% seeding dose in non-neuronal tissues, suggesting that prion-seeding activity exists in non-neural organs, and we suggested that non-neural tissues of 106/g SD50 did not exist the infectivity., EBioMedicine, 12, pp.150-155; 2016},
 pages = {150--155},
 title = {Prion-Seeding Activity Is widely Distributed in Tissues of Sporadic Creutzfeldt-Jakob Disease Patients},
 volume = {12},
 year = {2016}
}