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Human Prion Diseases
- Source :
- Archives of Neurology. 62:545
- Publication Year :
- 2005
- Publisher :
- American Medical Association (AMA), 2005.
-
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.
- Subjects :
- PrPSc Proteins
animal diseases
10208 Institute of Neuropathology
Brain
610 Medicine & health
Computational biology
Disease
Biology
Phenotype
Virology
Creutzfeldt-Jakob Syndrome
Prion Diseases
nervous system diseases
Encephalopathy, Bovine Spongiform
2728 Neurology (clinical)
Arts and Humanities (miscellaneous)
1201 Arts and Humanities (miscellaneous)
Animals
Humans
570 Life sciences
biology
Cattle
PrPC Proteins
Neurology (clinical)
Prion protein
Animal species
Subjects
Details
- ISSN :
- 00039942
- Volume :
- 62
- Database :
- OpenAIRE
- Journal :
- Archives of Neurology
- Accession number :
- edsair.doi.dedup.....c423c9899806b034364e1f12433db426