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Aguzzi, A (2006). Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis. Journal of Neurochemistry, 97(6):1726-1739.

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Abstract

Neuronal vacuolation (spongiosis), neuronal death, and pronounced glial reactions are the hallmarks of transmissible spongiform encephalopathies (TSEs), or prion diseases. A wealth of physical, biochemical, and immunological evidence indicates that the TSE agent, termed prion, does not contain agent-specific nucleic acid encoding its own constituents, as is the case for all other infectious pathogens. Also, no adaptive immune responses are elicited upon infection. A defining feature of TSEs is the deposition, mainly in the brain and lymphoreticular tissues, of an aggregated and structurally abnormal protein, designated PrP(Sc) or PrP-res, which represents a conformational isomer of the ubiquitous surface protein PrP(C). Biochemical and genetic evidence link PrP and its gene to the disease. Although TSEs are by definition transmissible, a growing number of Prnp-associated non-infectious neurodegenerative proteinopathies are now being recognized.

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:1 June 2006
Deposited On:11 Feb 2008 12:26
Last Modified:27 Nov 2013 18:38
Publisher:Wiley-Blackwell
ISSN:0022-3042
Publisher DOI:10.1111/j.1471-4159.2006.03909.x
PubMed ID:16805779
Citations:Web of Science®. Times Cited: 49
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