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See Latest ArticlesReduction of prion infectivity and levels of scrapie prion protein by lithium aluminum hydride: Implications for RNA in prion diseases
Journal of Neuropathology and Experimental Neurology, 08/07/09
Jeong BH et al. – Findings are the first evidence to suggest that RNA molecules are a component of cellular cofactors for abnormal proteinase-resistant prion protein (PrPSc). These data suggest that RNA molecules may be important for maintaining PrPSc structure and that oxidized molecules can be important in scrapie agent replication and prion infectivity.
Methods- Study of whether RNA molecules are cofactors for PrPSc propagation
- Use of chemicals to cleave phosphodiester bonds of RNA
- Assessment of their effects on an infectious agent
- RNase A treatment of partially purified PrPSc and of 263K scrapie brain homogenates
- RNase A treatment sufficient to increase PrPSc sensitivity to proteinase K degradation
- Treatment with RNase A alone and PrPSc degradation by RNase A plus proteinase K in vitro did not result in loss of scrapie infectivity vs the effects of lithium aluminum hydride
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