Electron Microscopy in Prion Research: Tubulovesicular Structures Are Not Composed of Prion Protein (PrP) but They May Be Intimately Associated with PrP Amyloid Fibrils

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Prions and Brain Diseases in Animals and Humans

Part of the book series: NATO ASI Series ((NSSA,volume 295))

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Abstract

In a recent monograph on electron microscopy of prion diseases one of us wrote „Attempts, using thin-section transmission electron microscopy, to define the structure of the infectious virus of scrapie (and analogously, Creutzfeldt-Jakob disease, kuru and, recently, bovine spongiform encephalopathy) is an repeatable example of failures, falstarts and misinterpretations.”1 The presence of tubulovesicular structures is, however, a consistent finding.2

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Liberski, P.P., Jeffrey, M., Goodsir, C. (1998). Electron Microscopy in Prion Research: Tubulovesicular Structures Are Not Composed of Prion Protein (PrP) but They May Be Intimately Associated with PrP Amyloid Fibrils. In: Morrison, D.R.O. (eds) Prions and Brain Diseases in Animals and Humans. NATO ASI Series, vol 295. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1896-3_9

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  • DOI: https://doi.org/10.1007/978-1-4899-1896-3_9

  • Publisher Name: Springer, Boston, MA

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