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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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Strain-Dependent Prion Infection in Mice Expressing Prion Protein with Deletion of Central Residues 91-106.

TL;DR: Results suggest that residues 91–106 or 91–104 of PrPC are crucially involved in prion pathogenesis in a strain-dependent manner and may play a similar role to digitonin and heparin in the conversion of Pr PC into PrPSc.
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Development of Radioiodinated Benzofuran Derivatives for in Vivo Imaging of Prion Deposits in the Brain

TL;DR: The development of 125I-labeled iodobenzofuran (IBF) derivatives as single photon emission computed tomography (SPECT) imaging probes to detect cerebralPrPSc deposits showed prospective binding properties to PrPSc.
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Spontaneous generation of distinct prion variants with recombinant prion protein from a baculovirus-insect cell expression system.

TL;DR: This paper used recombinant prion protein from a baculovirus-insect cell expression system (Bac-rPrP) and insect cell-derived cofactors to determine whether Bac-r-PrPSc is spontaneously produced in intermittent ultrasonic reactions.
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Feasibility studies of radioiodinated pyridyl benzofuran derivatives as potential SPECT imaging agents for prion deposits in the brain.

TL;DR: SPECT/computed tomography imaging and ex vivo autoradiography demonstrated that the [123I]IPBF-NHMe distribution in brain tissues of mBSE-infected mice co-localized with PrPSc deposits, appearing to be a prospective SPECT tracer for monitoring prion deposits in living brain tissues.

The Absence of Prion-Like Infectivity in Mice expressing Prion Protein-Like Protein

TL;DR: It is indicated that PrPLP/Dpl have no potential to undergo pathogenic conversion to form a prion-like infectious particle.