R
Ryuichiro Atarashi
Researcher at University of Miyazaki
Publications - 68
Citations - 9028
Ryuichiro Atarashi is an academic researcher from University of Miyazaki. The author has contributed to research in topics: PrPSc Proteins & Scrapie. The author has an hindex of 28, co-authored 64 publications receiving 8141 citations. Previous affiliations of Ryuichiro Atarashi include Nagasaki University & National Institutes of Health.
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Prion Strain-Dependent Differences in Conversion of Mutant Prion Proteins in Cell Culture
Ryuichiro Atarashi,Ryuichiro Atarashi,Valerie L. Sim,Noriyuki Nishida,Byron Caughey,Shigeru Katamine +5 more
TL;DR: Results show that two strains with the same PrP sequence but different conformations have differing abilities to convert the same mutated PrPC.
Journal ArticleDOI
Deletion of N-terminal Residues 23–88 from Prion Protein (PrP) Abrogates the Potential to Rescue PrP-deficient Mice from PrP-like Protein/Doppel-induced Neurodegeneration
Ryuichiro Atarashi,Noriyuki Nishida,Kazuto Shigematsu,Shinji Goto,Takahito Kondo,Suehiro Sakaguchi,Shigeru Katamine +6 more
TL;DR: Findings provide evidence that the N-terminal residues 23–88 of PrP containing the unique octapeptide-repeat region is crucial for preventing Purkinje cell death in Prnp0/0 mice expressing PrPLP/Dpl in the neuron.
A highly sensitive assay for prion detection
TL;DR: After assessment of more than 200 CSF specimens from Japanese and Australian patients, results indicate that the RT-QUIC, with its high sensitivity and specificity, will be of great use as an early, rapid and specific assay for prion diseases.
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Increased expression of p62/SQSTM1 in prion diseases and its association with pathogenic prion protein
Takujiro Homma,Daisuke Ishibashi,Takehiro Nakagaki,Katsuya Satoh,Kazunori Sano,Ryuichiro Atarashi,Noriyuki Nishida +6 more
TL;DR: Transient expression of the phosphomimic form of p62, which has enhanced ubiquitin-binding activity, reduced the amount of PrPSc in prion-infected cells, indicating that the activation of p 62 could accelerate the clearance ofPrPSc.
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Ubiquitin-specific protease 14 modulates degradation of cellular prion protein.
Takujiro Homma,Daisuke Ishibashi,Takehiro Nakagaki,Takayuki Fuse,Tsuyoshi Mori,Katsuya Satoh,Ryuichiro Atarashi,Noriyuki Nishida +7 more
TL;DR: Results suggest that USP14 prevents degradation of both normal and abnormal PrP, a deubiqutinating enzyme that catalyzes trimming of polyubiquitin chains and plays a role in regulation of proteasomal processes.