Picking Prion Infectivity Apart | February 28, 2011 Issue - Vol. 89 Issue 9 | Chemical & Engineering News
 
 
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Volume 89 Issue 9 | p. 48 | Concentrates
Issue Date: February 28, 2011

Picking Prion Infectivity Apart

New research suggests that infectious protein misfolding and Prion diseases’ neurological toxicity are independent processes
Department: Science & Technology
Keywords: prions, misfolded proteins

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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