Emanuela Urso, Raffaele Acierno, Maria Giulia Lionetto, Antonia Rizzello, Andrea Papa, Trifone Schettino and Michele Maffia Pages 1281 - 1290 ( 10 )
The cytotoxicity of hPrP[173-195] prion peptide against a neuroblastoma cell model was found independent of its tendency to aggregate over time. Cytosolic and nuclear inclusions of peptide were highlighted by confocal microscopy, suggesting a role as a transcription factor in activating signal transduction pathways involved in cell toxicity.
Prion disease, cellular prion protein (PrPC), helix-2, structural ambivalence, synthetic prion peptides, confocal microscopy
Department of Biological and Environmental Science and Technology, University of Salento, Lecce, Italy.