The polymorphisms at amino acid residues 136, 154, and 171 in ovine prion protein (PrP) have been associated with different susceptibility to scrapie: animals expressing PrPARQ [PrP(Ala136/Arg154/Gln171)] show vulnerability, whereas those that express PrPARR [PrP(Ala136/Arg154/Arg171)] are resistant to scrapie. The aim of this study was to...
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2007 (v1)PublicationUploaded on: March 25, 2023
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2007 (v1)Publication
J Neurochem. 2007 Dec;103(6):2597-609. Epub 2007 Oct 18. Intracellular accumulation of a mild-denatured monomer of the human PrP fragment 90-231, as possible mechanism of its neurotoxic effects. Chiovitti K, Corsaro A, Thellung S, Villa V, Paludi D, D'Arrigo C, Russo C, Perico A, Ianieri A, Di Cola D, Vergara A, Aceto A, Florio...
Uploaded on: February 13, 2024 -
2007 (v1)Publication
Because of high tendency of the prion protein (PrP) to aggregate, the exact PrP isoform responsible for prion diseases as well as the pathological mechanism that it activates remains still controversial. In this study, we show that a pre-fibrillar, monomeric or small oligomeric conformation of the human PrP fragment 90-231 (hPrP90-231), rather...
Uploaded on: March 25, 2023