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Roger A. Moore

Researcher at National Institutes of Health

Publications -  37
Citations -  1811

Roger A. Moore is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Scrapie & Dehydrogenase. The author has an hindex of 20, co-authored 36 publications receiving 1634 citations. Previous affiliations of Roger A. Moore include University of Toledo & Rocky Mountain Laboratories.

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Ultrasensitive detection of scrapie prion protein using seeded conversion of recombinant prion protein.

TL;DR: A much faster seeded polymerization method (rPrP-PMCA) is described which detects ≥50 ag of hamster PrPSc (≈0.003 lethal dose) within 2–3 d and should facilitate the development of rapid, ultrasensitive prion assays and diagnostic tests, in addition to aiding fundamental studies of structure and mechanism of PrP Sc formation.
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Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking.

TL;DR: A new prion assay, abbreviated QUIC for quaking-induced conversion, which uses rPrP-sen as a substrate and automated tube shaking rather than sonication is developed, which can detect about one lethal prion dose within a day, and is faster and simpler than previous described PMCA6 and rPrp-PMCA5 assays.
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Immunohistochemical localization of aspartoacylase in the rat central nervous system.

TL;DR: The predominant immunoreactivity in oligodendrocytes is consistent with the proposed role of ASPA in myelination, supporting the case for acetate supplementation as an immediate and inexpensive therapy for infants diagnosed with CD.
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Activation of the Innate Signaling Molecule MAVS by Bunyavirus Infection Upregulates the Adaptor Protein SARM1, Leading to Neuronal Death

TL;DR: It is shown that LACV infection induced the RNA helicase, RIG-I, and mitochondrial antiviral signaling protein (MAVS) signaling pathway, resulting in upregulation of the sterile alpha and TIR-containing motif 1 (SARM1), an adaptor molecule that was found to be directly involved in neuronal damage.
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Prion protein misfolding and disease.

TL;DR: The purpose of this review is to provide an overview of the existing structural information for PrP within the context of what is known about the biology of prion disease.