Elsevier

The Lancet

Volume 365, Issue 9454, 8–14 January 2005, Page 122
The Lancet

Correspondence
A prion lexicon (out of control)

https://doi.org/10.1016/S0140-6736(05)17700-9Get rights and content

References (5)

  • A Serban et al.

    Immunoglobulins in urine of hamsters with scrapie

    J Biol Chem

    (2004)
  • B Caughey et al.

    Normal and scrapie-associated forms of prion protein differ in their sensitivities to phospholipase and proteases in intact neuroblastoma cells

    J Virol

    (1990)
There are more references available in the full text version of this article.

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