Internalization and signal transduction of PrP106−126 in neuronal cells
✍ Scribed by Lars-Ove Brandenburg; Ralph Lucius; Azami Tameh Abolfazl; Markus Kipp; Christoph J. Wruck; Thomas Koch; Cordian Beyer; Thomas Pufe
- Book ID
- 113411750
- Publisher
- Elsevier Science
- Year
- 2009
- Tongue
- German
- Weight
- 393 KB
- Volume
- 191
- Category
- Article
- ISSN
- 0940-9602
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## 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
## 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