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Glatzel, M; Stoeck, K; Seeger, H; Lührs, T; Aguzzi, A (2005). Human prion diseases: molecular and clinical aspects. Archives of Neurology, 62(4):545-552.

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Abstract

Compared with that of other human pathogens, the proposed replicative cycle of prions is disarmingly simple. It encompasses misfolding of a single protein, the cellular prion protein (PrPC), into a disease-associated form called PrPSc. This is followed by PrPSc aggregation and possibly fragmentation of aggregates, which may augment the number of replicative units. Although there is no formal proof of the correctness of this model, a wealth of evidence indicates that pathogen-encoded informational nucleic acids are dispensable for prion replication. Despite the simplicity of the replicative process, the human phenotypic range of prion diseases is extremely variable and includes the sporadic, inherited, and acquired forms of Creutzfeldt-Jakob disease. In addition, prion diseases occur in a wide range of animals and can be propagated within and between animal species. The present review article discusses current concepts and controversies surrounding the basic biological features of prions.

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
DDC:570 Life sciences; biology
610 Medicine & health
Language:English
Date:1 April 2005
Deposited On:11 Feb 2008 12:27
Last Modified:27 Nov 2013 22:40
Publisher:American Medical Association
ISSN:0003-9942
Publisher DOI:10.1001/archneur.62.4.545
PubMed ID:15824251
Citations:Web of Science®. Times Cited: 60
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