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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-4506

Aguzzi, A; Baumann, F; Bremer, J (2008). The prion's elusive reason for being. Annual Review of Neuroscience, 31:439-477.

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Abstract

The protein-only hypothesis posits that the infectious agent causing transmissible spongiform encephalopathies consists of protein and lacks any informational nucleic acids. This agent, termed prion by Stanley Prusiner, is thought to consist partly of PrP(Sc), a conformational isoform of a normal cellular protein termed PrP(C). Scientists and lay persons have been fascinated by the prion concept, and it has been subjected to passionate critique and intense experimental scrutiny. As a result, PrP(C) and its isoforms rank among the most intensively studied proteins encoded by the mammalian genome. Despite all this research, both the physiological function of PrP(C) and the molecular pathways leading to neurodegeneration in prion disease remain unknown. Here we review the salient traits of those diseases ascribed to improper behavior of the prion protein and highlight how the physiological functions of PrP(C) may help explain the toxic phenotypes observed in prion disease.

Item Type:Journal Article, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2008
Deposited On:21 Oct 2008 07:26
Last Modified:28 Nov 2013 01:27
Publisher:Annual Reviews
ISSN:0147-006X
Publisher DOI:10.1146/annurev.neuro.31.060407.125620
PubMed ID:18558863
Citations:Web of Science®. Times Cited: 197
Google Scholar™
Scopus®. Citation Count: 199

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