Spontaneous Deamidation and Isomerization of Asn108 in Prion Peptide 106–126 and in Full-Length Prion Protein
✍ Scribed by E. Sandmeier; P. Hunziker; B. Kunz; R. Sack; P. Christen
- Book ID
- 115584159
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- English
- Weight
- 80 KB
- Volume
- 261
- Category
- Article
- ISSN
- 0006-291X
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## Abstract A synthetic peptide corresponding to the 106–126 amyloidogenic region of the cellular human prion protein (PrP^c^) is useful for in vitro study of prion‐induced neuronal cell death. The aim of the present work was to examine the implication of the cellular prion protein in the toxicity
## Abstract Using the lipid bilayer technique, we have found that age‐related derivatives, PrP[106–126] (L‐Asp108) and PrP[106–126] (L‐iso‐Asp108), of the prion protein fragment 106–126 (PrP[106–126] (Asn108)) form heterogeneous ion channels. The deamidated isoforms, PrP[106–126] (L‐Asp108) and PrP
## Abstract Prion diseases are neurodegenerative disorders that are characterized by the presence of the misfolded prion protein (PrP). Neurotoxicity in these diseases may result from prion‐induced modulation of ion channel function, changes in neuronal excitability, and consequent disruption of ce