@article{oai:nagasaki-u.repo.nii.ac.jp:00004588,
 author = {Takatsuki, Hanae and Satoh, Katsuya and Sano, Kazunori and Fuse, Takayuki and Nakagaki, Takehiro and Mori, Tsuyoshi and Ishibashi, Daisuke and Mihara, Ban and Takao, Masaki and Iwasaki, Yasushi and Yoshida, Mari and Atarashi, Ryuichiro and Nishida, Noriyuki},
 issue = {6},
 journal = {PLOS ONE},
 month = {Jun},
 note = {The infectious agents of the transmissible spongiform encephalopathies are composed of amyloidogenic prion protein, PrPSc. Real-time quaking-induced conversion can amplify very small amounts of PrPSc seeds in tissues/body fluids of patients or animals. Using this in vitro PrP-amyloid amplification assay, we quantitated the seeding activity of affected human brains. End-point assay using serially diluted brain homogenates of sporadic Creutzfeldt-Jakob disease patients demonstrated that 50% seeding dose (SD50) is reached approximately 1010/g brain (values varies 108.79-10.63/g). A genetic case (GSS-P102L) yielded a similar level of seeding activity in an autopsy brain sample. The range of PrPSc concentrations in the samples, determined by dot-blot assay, was 0.6-5.4 μg/g brain; therefore, we estimated that 1 SD50 unit was equivalent to 0.06-0.27 fg of PrPSc. The SD50 values of the affected brains dropped more than three orders of magnitude after autoclaving at 121°C. This new method for quantitation of human prion activity provides a new way to reduce the risk of iatrogenic prion transmission., PLOS ONE, 10(6), e0126930; 2015},
 title = {Rapid and Quantitative Assay of Amyloid-Seeding Activity in Human Brains Affected with Prion Diseases},
 volume = {10},
 year = {2015}
}