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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-25983

Aguzzi, A; Calella, A M (2009). Prions: protein aggregation and infectious diseases. Physiological Reviews, 89(4):1105-1152.

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Abstract

Transmissible spongiform encephalopathies (TSEs) are inevitably lethal neurodegenerative diseases that affect humans and a large variety of animals. The infectious agent responsible for TSEs is the prion, an abnormally folded and aggregated protein that propagates itself by imposing its conformation onto the cellular prion protein (PrPC) of the host. PrPC is necessary for prion replication and for prion-induced neurodegeneration, yet the proximal causes of neuronal injury and death are still poorly understood. Prion toxicity may arise from the interference with the normal function of PrPC, and therefore, understanding the physiological role of PrPC may help to clarify the mechanism underlying prion diseases. Here we discuss the evolution of the prion concept and how prion-like mechanisms may apply to other protein aggregation diseases. We describe the clinical and the pathological features of the prion diseases in human and animals, the events occurring during neuroinvasion, and the possible scenarios underlying brain damage. Finally, we discuss potential antiprion therapies and current developments in the realm of prion diagnostics.

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136 citations in Web of Science®
144 citations in Scopus®
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Additional indexing

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:2009
Deposited On:21 Dec 2009 16:58
Last Modified:28 Dec 2013 10:43
Publisher:American Physiological Society
ISSN:0031-9333
Publisher DOI:10.1152/physrev.00006.2009
PubMed ID:19789378

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