Literature DB >> 12794269

The cellular prion protein: biochemistry, topology, and physiologic functions.

Cristiana Griffoni1, Mattia Toni, Enzo Spisni, Maria Bianco, Spartaco Santi, Massimo Riccio, Vittorio Tomasi.   

Abstract

Studies on the transmission from man to animals of Creutzfeld-Jacob disease (CJD) led Prusiner to identify a proteinaceous infectious particle lacking nucleic acid, which was called prion. The identification of the infectious prion (PrPsc) then led to the discovery of the normal cellular counterpart (PrPc). One of the still enigmatic aspects regarding prion diseases is actually how, where, and when the transformation PrPc/PrPsc is occurring, this being due to the result of a large extent to the fact that so far most studies have been dedicated to the formation and transmission of PrPsc, whereas the understanding of physiologic roles of PrPc are in their infancy. In this review, we hope to identify the most reliable hypotheses for future experiments on PrPc. This is relevant not only for the understanding of PrPc functions but also to unravel the enigmatic nature of PrPc/PrPsc conversion.

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Year:  2003        PMID: 12794269     DOI: 10.1385/cbb:38:3:287

Source DB:  PubMed          Journal:  Cell Biochem Biophys        ISSN: 1085-9195            Impact factor:   2.194


  2 in total

1.  Signal transduction in neurons: effects of cellular prion protein on fyn kinase and ERK1/2 kinase.

Authors:  Vittorio Tomasi
Journal:  Immun Ageing       Date:  2010-12-16       Impact factor: 6.400

2.  Cellular prion protein and caveolin-1 interaction in a neuronal cell line precedes Fyn/Erk 1/2 signal transduction.

Authors:  Mattia Toni; Enzo Spisni; Cristiana Griffoni; Spartaco Santi; Massimo Riccio; Patrizia Lenaz; Vittorio Tomasi
Journal:  J Biomed Biotechnol       Date:  2006
  2 in total

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