Issue Date: February 28, 2011
Picking Prion Infectivity Apart
Prion disorders such as Creutzfeldt–Jakob disease and bovine spongiform encephalopathy have long kept researchers guessing about exactly how the diseases’ characteristically misfolded proteins lead to infectivity and toxicity. Research from John Collinge and colleagues at UCL Institute of Neurology, in London, suggests that the infectious refolding of normal proteins into misfolded versions and prion diseases’ neurological toxicity are independent processes (Nature, DOI: 10.1038/nature09768). The researchers note that “prions themselves are not . . .
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